Lipid–protein interactions in biological membranes: A structural perspective

Lee, A.G

doi:10.1016/s0005-2736(03)00056-7

Cited by 886Lipid Membrane Structure and BehaviorProtein Structure and DynamicsReceptor Mechanisms and Signaling

Lipid–protein interactions in biological membranes: A structural perspective

Open access

Lee, A.G·2003·Biochimica et Biophysica Acta (BBA) - Biomembranes

DOI 10.1016/s0005-2736(03)00056-7

Open this paper in CoChat — free account Open PDF

Abstract

Lipid molecules bound to membrane proteins are resolved in some high-resolution structures of membrane proteins. An analysis of these structures provides a framework within which to analyse the nature of lipid-protein interactions within membranes. Membrane proteins are surrounded by a shell or annulus of lipid molecules, equivalent to the solvent layer surrounding a water-soluble protein. The lipid bilayer extends right up to the membrane protein, with a uniform thickness around the protein. The surface of a membrane protein contains many shallow grooves and protrusions to which the fatty acyl chains of the surrounding lipids conform to provide tight packing into the membrane. An individual lipid molecule will remain in the annular shell around a protein for only a short period of time. Binding to the annular shell shows relatively little structural specificity. As well as the annular lipid, there is evidence for other lipid molecules bound between the transmembrane alpha-helices of the protein; these lipids are referred to as non-annular lipids. The average thickness of the hydrophobic domain of a membrane protein is about 29 A, with a few proteins having significantly smaller or greater thicknesses than the average. Hydrophobic mismatch between a membrane protein and the surrounding lipid bilayer generally leads to only small changes in membrane thickness. Possible adaptations in the protein to minimise mismatch include tilting of the helices and rotation of side chains at the ends of the helices. Packing of transmembrane alpha-helices is dependent on the chain length of the surrounding phospholipids. The function of membrane proteins is dependent on the thickness of the surrounding lipid bilayer, sometimes on the presence of specific, usually anionic, phospholipids, and sometimes on the phase of the phospholipid.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/s0005-2736(03)00056-7

Cites

224 of 224 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Fatty acyl chain length alters binding constants of several membrane proteins.
“Fatty acyl chain length alters binding constants of several membrane proteins [169], making it tempting to speculate that VLCFAs might alter neural cell membrane structure, stability, and function [170].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [169]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D., Morais-Cabral, J. H., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,816 · see citing works
Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
McDermott, G., Prince, S. M., Freer, A. A., Hawthornthwaite, A. M., Papiz, M. Z., Cogdell, R. J., & Isaacs, N. W. (1995) · Nature · doi:10.1038/374517a0 · Cited by 2,741 · see citing works
Structure of lipid bilayers
Nagle, J. F., & Tristram‐Nagle, S. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(00)00016-2 · Cited by 2,660 · see citing works
Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
Jordan, P., Fromme, P., Witt, H. T., Klukas, O., Saenger, W., & Krauß, N. (2001) · Nature · doi:10.1038/35082000 · Cited by 2,494 · see citing works
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102 · see citing works
Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution
Zhou, Y., Morais-Cabral, J. H., Kaufman, A., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102009 · Cited by 2,092 · see citing works
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,006 · see citing works
Structural determinants of water permeation through aquaporin-1
Murata, K., Mitsuoka, K., Hirai, T., Walz, T., Agre, P. C., Heymann, J. B., Engel, A. H., & Fujiyoshi, Y. (2000) · Nature · doi:10.1038/35036519 · Cited by 1,810 · see citing works
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
Toyoshima, C., Nakasako, M., NOMURA, H., & Ogawa, H. (2000) · Nature · doi:10.1038/35015017 · Cited by 1,798 · see citing works
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,767 · see citing works
Bacterial endotoxin: molecular relationships of structure to activity and function
Rietschel, E., Kirikae, T., Schade, F. U., Mamat, U., Schmidt, G., Loppnow, H., Ulmer, A. J., Zähringer, U., Seydel, U., Padova, F. D., et al. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.2.8119492 · Cited by 1,608 · see citing works
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
Dutzler, R., Campbell, E., Cadene, M., Chait, B., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,567 · see citing works
Crystal structures explain functional properties of two E. coli porins
Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., & Rosenbusch, J. P. (1992) · Nature · doi:10.1038/358727a0 · Cited by 1,521 · see citing works
IDENTIFYING NONPOLAR TRANSBILAYER HELICES IN AMINO ACID SEQUENCES OF MEMBRANE PROTEINS
Engelman, D. M., Steitz, T. A., & Goldman, A. (1986) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.15.060186.001541 · Cited by 1,508 · see citing works
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · see citing works
Structure of bacteriorhodopsin at 1.55 Å resolution
Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J., & Lanyi, J. Κ. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3027 · Cited by 1,452 · see citing works
The open pore conformation of potassium channels
Jiang, Y., Lee, A., Chen, J., Cadène, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/417523a · Cited by 1,189 · see citing works
Self-citation
Phase equilibria in the phosphatidylcholine-cholesterol system
Ipsen, J. H., Karlström, G., Mourtisen, O. G., Wennerström, H., & Zuckermann, M. J. (1987) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(87)90020-4 · Cited by 1,061 · see citing works
Structure of a Glycerol-Conducting Channel and the Basis for Its Selectivity
Fu, D., Libson, A. M., Miercke, L. J. W., Weitzman, C., Nollert, P., Krucinski, J., & Stroud, R. M. (2000) · Science · doi:10.1126/science.290.5491.481 · Cited by 1,000 · see citing works
Structure of the MscL Homolog from Mycobacterium tuberculosis : A Gated Mechanosensitive Ion Channel
Chang, G. A., Spencer, R. H., Lee, A. T., Barclay, M. T., & Rees, D. C. (1998) · Science · doi:10.1126/science.282.5397.2220 · Cited by 990 · see citing works
Self-citation
Structure and dynamics of membranes
Lipowsky, R., & Sackmann, E. (1995) · Cited by 956 · see citing works
Electron-crystallographic Refinement of the Structure of Bacteriorhodopsin
Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M., & Henderson, R. A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0328 · Cited by 956 · see citing works
The Preference of Tryptophan for Membrane Interfaces
Yau, W., Wimley, W. C., Gawrisch, K., & White, S. H. (1998) · Biochemistry · doi:10.1021/bi980809c · Cited by 929 · see citing works
Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ
Huang, C.-L., Feng, S., & Hilgemann, D. W. (1998) · Nature · doi:10.1038/35882 · Cited by 885 · see citing works
Structural changes in the calcium pump accompanying the dissociation of calcium
Toyoshima, C., & NOMURA, H. (2002) · Nature · doi:10.1038/nature00944 · Cited by 881 · see citing works
The biosynthesis and functional role of cardiolipin
Schlame, M., Rua, D., & Greenberg, M. L. (2000) · Progress in Lipid Research · doi:10.1016/s0163-7827(00)00005-9 · Cited by 810 · see citing works
Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787 · see citing works
Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
Lewis, B. A., & Engelman, D. M. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80007-2 · Cited by 786 · see citing works
Mattress model of lipid-protein interactions in membranes
Mouritsen, O. G., & Bloom, M. J. (1984) · Biophysical Journal · doi:10.1016/s0006-3495(84)84007-2 · Cited by 762 · see citing works
Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
Esnouf, R. M. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998017363 · Cited by 754 · see citing works
High pressure effects on protein structure and function
Mozhaev, V. V., Heremans, K., Jzn, J. F., Masson, P., & Balny, C. (1996) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199601)24:1 · Cited by 716 · see citing works
Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
Wiener, M. C., & White, S. H. (1992) · Biophysical Journal · doi:10.1016/s0006-3495(92)81849-0 · Cited by 706 · see citing works
Hydrophobic mismatch between proteins and lipids in membranes
Killian, J. A. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00017-3 · Cited by 647 · see citing works
Amphipathic helix motif: Classes and properties
Segrest, J. P., Loof, H. D., Dohlman, J. G., Brouillette, C. G., & Anantharamaiah, G. M. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340080202 · Cited by 642 · see citing works
Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids.
Grüner, S. M. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.11.3665 · Cited by 616 · see citing works
Open channel structure of MscL and the gating mechanism of mechanosensitive channels
Perozo, E., Cortés, D. M., Sompornpisut, P., Kloda, A., & Martinac, B. (2002) · Nature · doi:10.1038/nature00992 · Cited by 616 · see citing works
An introduction to the principles of surface chemistry
Haydon, D. A. (1974) · Journal of Chromatography A · doi:10.1016/s0021-9673(00)97214-5 · Cited by 518 · see citing works
Effects of Phospholipid Acyl Chain Fluidity, Phase Transitions, and Cholesterol on (Na+ + K+)-stimulated Adenosine Triphosphatase
Kimelberg, H. K., & Papahadjopoulos, D. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42943-8 · Cited by 512 · see citing works
Lipids in Plants and Microbes
Harwood, J. L., & Russell, N. J. (1984) · Springer eBooks · doi:10.1007/978-94-011-5989-0 · Cited by 505 · see citing works
Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N
Jormakka, M., Törnroth‐Horsefield, S., Byrne, B., & Iwata, S. (2002) · Science · doi:10.1126/science.1068186 · Cited by 502 · see citing works
Progress in protein-lipid interactions
Watts, A., & Pont, J. J. H. H. M. D. (1985) · Elsevier eBooks · Cited by 480 · see citing works
Structure of the outer membrane protein A transmembrane domain
Pautsch, A., & Schulz, G. E. (1998) · Nature Structural Biology · doi:10.1038/2983 · Cited by 476 · see citing works
Specific roles of protein–phospholipid interactions in the yeast cytochrome bc1 complex structure
Lange, C. M., Nett, J. H., Trumpower, B. L., & Hunte, C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.23.6591 · Cited by 444 · see citing works
The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices
Jacobs, R. E., & White, S. H. (1989) · Biochemistry · doi:10.1021/bi00434a042 · Cited by 437 · see citing works
Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution
Belrhali, H., Nollert, P., Royant, A., Menzel, C., Rosenbusch, J. P., Landau, E. M., & Pebay‐Peyroula, E. (1999) · Structure · doi:10.1016/s0969-2126(99)80118-x · Cited by 436 · see citing works
CRC handbook of lipid bilayers
Marsh, D. (1990) · Medical Entomology and Zoology · Cited by 431 · see citing works
Reconstitution of a Calcium Pump Using Defined Membrane Components
Warren, G., Toon, P. A., Birdsall, N. J. M., et al. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.3.622 · Cited by 424 · see citing works
Self-citation
Modulation of rhodopsin function by properties of the membrane bilayer
Brown, M. F. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90180-5 · Cited by 422 · see citing works
Absence of Cardiolipin in the crd1 Null Mutant Results in Decreased Mitochondrial Membrane Potential and Reduced Mitochondrial Function
Jiang, F., Ryan, M. T., Schlame, M., Zhao, M., Gu, Z., Klingenberg, M., Pfanner, N., & Greenberg, M. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909868199 · Cited by 414 · see citing works
Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
Essen, L., Siegert, R., Lehmann, W. D., & Oesterhelt, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11673 · Cited by 413 · see citing works
Amino acid distributions in integral membrane protein structures
Ulmschneider, M. B., & Sansom, M. S. P. (2001) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(01)00299-1 · Cited by 385 · see citing works
Non-random Distribution of Amino Acids in the Transmembrane Segments of Human Type I Single Span Membrane Proteins
Landolt-Marticorena, C., Williams, K. A., Deber, C. M., & Reithmeier, R. A. F. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1066 · Cited by 383 · see citing works
Modulation of membrane function by cholesterol
Yèagle, P. L. (1991) · Biochimie · doi:10.1016/0300-9084(91)90093-g · Cited by 354 · see citing works
Crystal Structure of Sensory Rhodopsin II at 2.4 Angstroms: Insights into Color Tuning and Transducer Interaction
Luecke, H., Schobert, B., Lanyi, J. Κ., et al. (2001) · Science · doi:10.1126/science.1062977 · Cited by 350 · see citing works
Energetics of Inclusion-Induced Bilayer Deformations
Hélix‐Nielsen, C., Goulian, M., & Andersen, O. S. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77904-4 · Cited by 336 · see citing works
Lipids in the Structure, Folding, and Function of the KcsA K+ Channel
Valiyaveetil, F. I., Zhou, Y., & MacKinnon, R. (2002) · Biochemistry · doi:10.1021/bi026215y · Cited by 331 · see citing works
Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane α-Helical Peptides
de Planque, M. R. R., Kruijtzer, J. A. W., Liskamp, R. M. J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20839 · Cited by 328 · see citing works
The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
VOGT, J. R. A., & Schulz, G. E. (1999) · Structure · doi:10.1016/s0969-2126(00)80063-5 · Cited by 327 · see citing works
Helix packing in membrane proteins
Bowie, J. U. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1279 · Cited by 325 · see citing works
Anionic Phospholipids Activate ATP-sensitive Potassium Channels
Fan, Z., & Makielski, J. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5388 · Cited by 323 · see citing works
Annular lipids determine the ATPase activity of a calcium transport protein complexed with dipalmitoyllecithin
Hesketh, T. R., Smith, G. A., Houslay, M. D., McGill, K. A., Birdsall, N. J. M., Metcalfe, J. C., & Warren, G. (1976) · Biochemistry · doi:10.1021/bi00664a002 · Cited by 315 · see citing works
Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes
Nezil, F. A., & Bloom, M. J. (1992) · Biophysical Journal · doi:10.1016/s0006-3495(92)81926-4 · Cited by 312 · see citing works
ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by phosphorus-31 nuclear magnetic resonance
Beyer, K., & Klingenberg, M. (1985) · Biochemistry · doi:10.1021/bi00336a001 · Cited by 301 · see citing works
How Membranes Shape Protein Structure
White, S. H., Ladokhin, A. S., Jayasinghe, S. A., & Hristova, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100008200 · Cited by 299 · see citing works
Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes
Warren, G., Toon, P. A., Birdsall, N. J. M., et al. (1974) · Biochemistry · doi:10.1021/bi00724a008 · Cited by 299 · see citing works
Self-citation
Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide
Anderson, R. A., & Marchesi, V. T. (1985) · Nature · doi:10.1038/318295a0 · Cited by 285 · see citing works
PROTEIN-LIPID INTERACTIONS
Gennis, R. B., & Jonas, A. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001211 · Cited by 280 · see citing works
Models of Lipid-Protein Interactions in Membranes
Mouritsen, O. G., & Bloom, M. J. (1993) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.22.060193.001045 · Cited by 277 · see citing works
Lipid selectivity of the calcium and magnesium ion dependent adenosine triphosphatase, studied with fluorescence quenching by a brominated phospholipid
East, J. M., & Lee, A. G. (1982) · Biochemistry · doi:10.1021/bi00260a035 · Cited by 268 · see citing works
Self-citation
Functional binding of cardiolipin to cytochromec oxidase
Robinson, N. C. (1993) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762857 · Cited by 265 · see citing works
The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution 1 1Edited by R. Huber
Mitsuoka, K., Hirai, T., Murata, K., Miyazawa, A., Kidera, A., Kimura, Y., & Fujiyoshi, Y. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2529 · Cited by 262 · see citing works
Ions and Counterions in a Biological Channel: A Molecular Dynamics Simulation of OmpF Porin from Escherichia coli in an Explicit Membrane with 1M KCl Aqueous Salt Solution
Im, W., & Roux, B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00380-7 · Cited by 259 · see citing works
Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
Marsh, D., & Horváth, L. I. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00009-4 · Cited by 252 · see citing works
Modulation of phospholipid acyl chain order by cholesterol. A solid-state deuterium nuclear magnetic resonance study
Sankaram, M. B., & Thompson, T. E. (1990) · Biochemistry · doi:10.1021/bi00499a015 · Cited by 238 · see citing works
Influence of Lipid/Peptide Hydrophobic Mismatch on the Thickness of Diacylphosphatidylcholine Bilayers. A 2H NMR and ESR Study Using Designed Transmembrane α-Helical Peptides and Gramicidin A
de Planque, M. R. R., Greathouse, D. V., Koeppe, R. E., Schäfer, H., Marsh, D., & Killian, J. A. (1998) · Biochemistry · doi:10.1021/bi980233r · Cited by 237 · see citing works
Structural details of an interaction between cardiolipin and an integral membrane protein
McAuley, K. E., Fyfe, P. K., Ridge, J. P., Isaacs, N. W., Cogdell, R. J., & Jones, M. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14706 · Cited by 236 · see citing works
Fluorescence quenching of model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
Caffrey, M., & Feigenson, G. W. (1981) · Biochemistry · doi:10.1021/bi00510a034 · Cited by 232 · see citing works
A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch
Fattal, D. R., & Ben‐Shaul, A. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81249-9 · Cited by 222 · see citing works
Interactions of proteins and cholesterol with lipids in bilayer membranes
Kleemann, W., & McConnell, H. M. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90347-3 · Cited by 218 · see citing works
The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants.
Hoffmann, B., Stöckl, A., Schlame, M., Beyer, K., & Klingenberg, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42117-x · Cited by 217 · see citing works
Molecular Dynamics Simulation of Melittin in a Dimyristoylphosphatidylcholine Bilayer Membrane
Bernèche, S., Nina, M., & Roux, B. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77604-0 · Cited by 216 · see citing works
Theoretical analysis of protein organization in lipid membranes
Gil, T., Ipsen, J. H., Mouritsen, O. G., Sabra, M. C., Sperotto, M. M., & Zuckermann, M. J. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00022-7 · Cited by 210 · see citing works
Functional Reconstitution of a Prokaryotic K+ Channel
Heginbotham, L., Kolmakova-Partensky, L., & Miller, C. (1998) · The Journal of General Physiology · doi:10.1085/jgp.111.6.741 · Cited by 208 · see citing works
Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor
Jones, O., & McNamee, M. G. (1988) · Biochemistry · doi:10.1021/bi00407a018 · Cited by 204 · see citing works
A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins
Ferguson, A. D., Welte, W., Hofmann, E., Lindner, B., Holst, O., Coulton, J. W., & Diederichs, K. (2000) · Structure · doi:10.1016/s0969-2126(00)00143-x · Cited by 204 · see citing works
Specificity and promiscuity in membrane helix interactions
Lemmon, M. A., & Engelman, D. M. (1994) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500004522 · Cited by 200 · see citing works
Role of sn-1-saturated,sn-2-polyunsaturated phospholipids in control of membrane receptor conformational equilibrium: effects of cholesterol and acyl chain unsaturation on the metarhodopsin I .tautm. metarhodopsin II equilibrium
Mitchell, D. C., Straume, M., & Litman, B. J. (1992) · Biochemistry · doi:10.1021/bi00118a005 · Cited by 193 · see citing works
Modulation of Na,K-ATPase and Na-ATPase Activity by Phospholipids and Cholesterol. I. Steady-State Kinetics
Cornelius, F. (2001) · Biochemistry · doi:10.1021/bi010541g · Cited by 188 · see citing works
The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum.
Johannsson, A., Keightley, C. A., Smith, G. A., et al. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69855-8 · Cited by 182 · see citing works
Overexpression of mammalian integral membrane proteins for structural studies
Tate, C. G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02711-9 · Cited by 180 · see citing works
Lipid Properties and the Orientation of Aromatic Residues in OmpF, Influenza M2, and Alamethicin Systems: Molecular Dynamics Simulations
Tieleman, D. P., Forrest, L. R., Sansom, M. S. P., & Berendsen, H. J. C. (1998) · Biochemistry · doi:10.1021/bi981802y · Cited by 179 · see citing works
Membrane protein diffusion sets the speed of rod phototransduction
Calvert, P. D., GOVARDOVSKII, V. I., Krasnoperova, N. V., Anderson, R. E., Lem, J., & Makino, C. L. (2001) · Nature · doi:10.1038/35075083 · Cited by 173 · see citing works
Conformational Energetics of Rhodopsin Modulated by Nonlamellar-Forming Lipids
Botelho, A. V., Gibson, N. J., Thurmond, R. L., Wang, Y., & Brown, M. F. (2002) · Biochemistry · doi:10.1021/bi011995g · Cited by 171 · see citing works
Anionic Phospholipids Regulate Native and Expressed Epithelial Sodium Channel (ENaC)
Ma, H.-P., Saxena, S., & Warnock, D. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100737200 · Cited by 170 · see citing works
2H nuclear magnetic resonance order parameter profiles suggest a change of molecular shape for phosphatidylcholines containing a polyunsaturated acyl chain
Holte, L. L., Peter, S. A., Sinnwell, T., & Gawrisch, K. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80422-4 · Cited by 169 · see citing works
Fourier transform infrared spectroscopic studies of the effect of calcium ions on phosphatidylserine
Dluhy, R. A., Cameron, D. G., Mantsch, H. H., et al. (1983) · Biochemistry · doi:10.1021/bi00295a043 · Cited by 169 · see citing works
A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension
Betanzos, M., Chiang, C.-S., Guy, H. R., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb828 · Cited by 168 · see citing works
Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum : Thermostability and electron transfer
Nogi, T., Fathir, I., Kobayashi, M., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240224997 · Cited by 166 · see citing works
Annular and non-annular binding sites on the (Ca2+ + Mg2+)-ATPase
Simmonds, A. C., East, J. M., Jones, O., et al. (1982) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(82)90447-3 · Cited by 165 · see citing works
Self-citation
Self-assembly of large, ordered lamellae from non-bilayer lipids and integral membrane proteins in vitro
Simidjiev, I., Stoylova, S. S., Amenitsch, H. W., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1473 · Cited by 165 · see citing works
Sensitivity of Single Membrane-Spanning α-Helical Peptides to Hydrophobic Mismatch with a Lipid Bilayer: Effects on Backbone Structure, Orientation, and Extent of Membrane Incorporation
de Planque, M. R. R., Goormaghtigh, E., Greathouse, D. V., Koeppe, R. E., Kruijtzer, J. A. W., Liskamp, R. M. J., KRUIJFF, B. D., & Killian, J. A. (2001) · Biochemistry · doi:10.1021/bi000804r · Cited by 164 · see citing works
Lipid-protein interactions mediate the photochemical function of rhodopsin
Wiedmann, T. S., Pates, R. D., Beach, J. M., Salmon, A., & Brown, M. F. (1988) · Biochemistry · doi:10.1021/bi00417a041 · Cited by 164 · see citing works
Geometry and Intrinsic Tilt of a Tryptophan-Anchored Transmembrane α-Helix Determined by 2H NMR
van der Wel, P. C. A., Strandberg, E., Killian, J. A., et al. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)73918-0 · Cited by 162 · see citing works
Effects of cholesterol on sodium-potassium ATPase ATP hydrolyzing activity in bovine kidney
Yèagle, P. L., Young, J., & Rice, D. (1988) · Biochemistry · doi:10.1021/bi00417a037 · Cited by 158 · see citing works
Phospholipase A2 Digestion of Cardiolipin Bound to Bovine Cytochrome c Oxidase Alters Both Activity and Quaternary Structure†
Sedlák, E., & Robinson, N. C. (1999) · Biochemistry · doi:10.1021/bi9914053 · Cited by 154 · see citing works
Temperature-dependent aggregation of bacteriorhodopsin in dipalmitoyl- and dimyristoylphosphatidylcholine vesicles
Cherry, R. J., Müller, U., Henderson, R. A., et al. (1978) · Journal of Molecular Biology · doi:10.1016/s0022-2836(78)80010-2 · Cited by 151 · see citing works
[13] Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
Kates, M., Kushwaha, S. C., & Sprott, G. D. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)88016-6 · Cited by 147 · see citing works
Determination of component volumes of lipid bilayers from simulations
Petrache, H. I., Feller, S. E., & Nagle, J. F. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78867-2 · Cited by 146 · see citing works
The Aromatic Residues Trp and Phe Have Different Effects on the Positioning of a Transmembrane Helix in the Microsomal Membrane
Braun, P., & von HEIJNE, G. (1999) · Biochemistry · doi:10.1021/bi990923a · Cited by 143 · see citing works
Manipulation of Cholesterol Levels in Rod Disk Membranes by Methyl-β-cyclodextrin
Niu, S., Mitchell, D. C., & Litman, B. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200594200 · Cited by 140 · see citing works
Lipid-protein multiple binding equilibriums in membranes
Brotherus, J. R., Griffith, O. H., Brotherus, M. O., et al. (1981) · Biochemistry · doi:10.1021/bi00521a026 · Cited by 140 · see citing works
Interactions between lipids and bacterial reaction centers determined by protein crystallography
Cámara-Artigas, A., Brune, D. C., & Allen, J. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162368399 · Cited by 139 · see citing works
How lipids interact with an intrinsic membrane protein: the case of the calcium pump
Lee, A. G. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(98)00010-0 · Cited by 139 · see citing works
Self-citation
Interactions of divalent cations with phosphatidylserine bilayer membranes
Hauser, H., & Shipley, G. G. (1984) · Biochemistry · doi:10.1021/bi00296a006 · Cited by 139 · see citing works
Interaction of a peptide model of a hydrophobic transmembrane .alpha.-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies
Zhang, Y. P., Lewis, R. N. A. H., Hodges, R. S., et al. (1992) · Biochemistry · doi:10.1021/bi00161a042 · Cited by 138 · see citing works
Molecular Order and Dynamics in Bilayers Consisting of Highly Polyunsaturated Phospholipids
Mitchell, D. C., & Litman, B. J. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)74011-1 · Cited by 137 · see citing works
Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses
Lewis, B. A., & Engelman, D. M. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80006-0 · Cited by 137 · see citing works
Effects of lipid environment on the light-induced conformational changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state
Baldwin, P. A., & Hubbell, W. L. (1985) · Biochemistry · doi:10.1021/bi00332a007 · Cited by 133 · see citing works
The Cytochrome c Oxidase from Paracoccus denitrificans Does Not Change the Metal Center Ligation upon Reduction
Harrenga, A., & Michel, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33296 · Cited by 132 · see citing works
Nucleotides and phospholipids compete for binding to the C terminus of KATP channels
MacGregor, G., Dong, K., Vanoye, C., Tang, L., Giebisch, G., & Hebert, S. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.042688899 · Cited by 131 · see citing works
Lipids and their effects on membrane proteins: Evidence against a role for fluidity
Lee, A. J. (1991) · Progress in Lipid Research · doi:10.1016/0163-7827(91)90002-m · Cited by 128 · see citing works
Self-citation
Cardiolipin-depleted bovine heart cytochrome c oxidase: binding stoichiometry and affinity for cardiolipin derivatives
Robinson, N. C., Zborowski, J., & Talbert, L. H. (1990) · Biochemistry · doi:10.1021/bi00490a012 · Cited by 126 · see citing works
Optimization of Receptor-G Protein Coupling by Bilayer Lipid Composition I
Mitchell, D. C., Niu, S., & Litman, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105772200 · Cited by 123 · see citing works
Lipid-Protein Interactions at the Nicotinic Acetylcholine Receptor
daCosta, C. J. B., Ogrel, A. A., McCardy, E. A., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108341200 · Cited by 123 · see citing works
Molecular Ordering of Interfacially Localized Tryptophan Analogs in Ester- and Ether-Lipid Bilayers Studied by 2H-NMR
Persson, S., Killian, J. A., & Lindblom, G. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)74054-8 · Cited by 122 · see citing works
Alignment of Lysine-Anchored Membrane Peptides under Conditions of Hydrophobic Mismatch: A CD, 15N and 31P Solid-State NMR Spectroscopy Investigation
Harzer, U., & Bechinger, B. (2000) · Biochemistry · doi:10.1021/bi000770n · Cited by 122 · see citing works
What the structure of a calcium pump tells us about its mechanism
LEE, A. G. J., & East, J. M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560665 · Cited by 120 · see citing works
Self-citation
Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosine triphosphatase
East, J. M., Melville, D., & Lee, A. G. (1985) · Biochemistry · doi:10.1021/bi00332a005 · Cited by 119 · see citing works
Self-citation
Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments
Dencher, N. A., Kohl, K.-D., & Heyn, M. P. (1983) · Biochemistry · doi:10.1021/bi00275a002 · Cited by 114 · see citing works
Structure of the KcsA Potassium Channel from Streptomyces lividans: A Site-Directed Spin Labeling Study of the Second Transmembrane Segment
Gross, A., Columbus, L. M., Hideg, K., Altenbach, C., & Hubbell, W. L. (1999) · Biochemistry · doi:10.1021/bi990856k · Cited by 114 · see citing works
Fluorescence quenching in model membranes. 2. Determination of the local lipid environment of the calcium adenosinetriphosphatase from sarcoplasmic reticulum
London, E., & Feigenson, G. W. (1981) · Biochemistry · doi:10.1021/bi00510a033 · Cited by 112 · see citing works
Specific labelling of the protein and lipid on the extracellular surface of purple membrane
Henderson, R. A., Jubb, J. S., & Whytock, S. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90325-x · Cited by 112 · see citing works
Structure and Fluctuations of Bacteriorhodopsin in the Purple Membrane: A Molecular Dynamics Study
Edholm, O., Berger, O., & Jähnig, F. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0361 · Cited by 111 · see citing works
Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance
Ryba, N. J. P., & Marsh, D. (1992) · Biochemistry · doi:10.1021/bi00148a011 · Cited by 111 · see citing works
The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor
Rankin, S. E., Addona, G. H., Kloczewiak, M. A., Bugge, B., & Miller, K. W. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78273-0 · Cited by 110 · see citing works
Simulation Study of a Gramicidin/Lipid Bilayer System in Excess Water and Lipid. I. Structure of the Molecular Complex
Chiu, S.-W., Subramaniam, S., & Jakobsson, E. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77352-2 · Cited by 110 · see citing works
Optimization of Receptor-G Protein Coupling by Bilayer Lipid Composition II
Niu, S., Mitchell, D. C., & Litman, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105778200 · Cited by 109 · see citing works
Hydrophobic Mismatch and the Incorporation of Peptides into Lipid Bilayers: A Possible Mechanism for Retention in the Golgi
Webb, R. J., East, J. M., Sharma, R. P., et al. (1998) · Biochemistry · doi:10.1021/bi972441+ · Cited by 109 · see citing works
Self-citation
Protein-lipid interaction
Gómez-Fernández, J. C., Goñi, F. M., Bach, D., et al. (1980) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(80)90031-0 · Cited by 109 · see citing works
Visualization of Highly Ordered Striated Domains Induced by Transmembrane Peptides in Supported Phosphatidylcholine Bilayers
Rinia, H. A., Kik, R. A., DEMEL, R. A., et al. (2000) · Biochemistry · doi:10.1021/bi000010c · Cited by 105 · see citing works
Transmembrane Helix M6 in Sarco(endo)plasmic Reticulum Ca2+-ATPase Forms a Functional Interaction Site with Phospholamban
Asahi, M., Kimura, Y., Kurzydlowski, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32855 · Cited by 105 · see citing works
Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidase
Robinson, N. C. (1982) · Biochemistry · doi:10.1021/bi00530a031 · Cited by 104 · see citing works
Lipid modulation of nicotinic acetylcholine receptor function: the role of membrane lipid composition and fluidity
Sunshine, C., & McNamee, M. G. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)90233-x · Cited by 104 · see citing works
Detergent structure in tetragonal crystals of OmpF porin
Pebay‐Peyroula, E., Garavito, R. M., Rosenbusch, J. P., et al. (1995) · Structure · doi:10.1016/s0969-2126(01)00241-6 · Cited by 102 · see citing works
Interactions of Phospholipids with the Potassium Channel KcsA
Williamson, I. M., Alvis, S. J., East, J. M., et al. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)73964-7 · Cited by 100 · see citing works
Self-citation
Molecular dynamics study of aquaporin‐1 water channel in a lipid bilayer
Zhu, F., Tajkhorshid, E., & Schulten, K. J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02749-1 · Cited by 99 · see citing works
Polymorphic phase behaviour of dilinoleoylphosphatidylethanolamine and palmitoyloleoylphosphatidylcholine mixtures
Boni, L. T., & Hui, S. W. (1983) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(83)90007-x · Cited by 96 · see citing works
Effects of lipid environment on the light-induced conformational changes of rhodopsin. 1. Absence of metarhodopsin II production in dimyristoylphosphatidylcholine recombinant membranes
Baldwin, P. A., & Hubbell, W. L. (1985) · Biochemistry · doi:10.1021/bi00332a006 · Cited by 94 · see citing works
Peptide Models of Helical Hydrophobic Transmembrane Segments of Membrane Proteins. 2. Differential Scanning Calorimetric and FTIR Spectroscopic Studies of the Interaction of Ac-K2-(LA)12-K2-amide with Phosphatidylcholine Bilayers
Zhang, Y.-P., Lewis, R. N. A. H., Hodges, R. S., et al. (1995) · Biochemistry · doi:10.1021/bi00007a032 · Cited by 93 · see citing works
Human erythrocyte hexose transporter activity is governed by bilayer lipid composition in reconstituted vesicles
Carruthers, A., & Melchior, D. L. (1984) · Biochemistry · doi:10.1021/bi00321a096 · Cited by 89 · see citing works
Protein-Lipid Interactions
(1993) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)x6014-4 · Cited by 88 · see citing works
Effects of phosphatidylcholine fatty acyl chain length on calcium binding and other functions of the calcium-magnesium-ATPase
Starling, A. P., East, J. M., & Lee, A. G. (1993) · Biochemistry · doi:10.1021/bi00057a025 · Cited by 88 · see citing works
Self-citation
Cholesterol is required for the reconstruction of the sodium- and chloride-coupled, gamma-aminobutyric acid transporter from rat brain.
Shouffani, A., & Kanner, B. I. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39282-8 · Cited by 87 · see citing works
A Novel Glycolipid and Phospholipid in the Purple Membrane
Corcelli, A., Colella, M., Mascolo, G., Fanizzi, F. P., & Kates, M. (2000) · Biochemistry · doi:10.1021/bi992462z · Cited by 86 · see citing works
Hydrophobic Matching Mechanism Investigated by Molecular Dynamics Simulations
Petrache, H. I., Zuckerman, D. M., Sachs, J. N., Killian, J. A., Koeppe, R. E., & Woolf, T. B. (2002) · Langmuir · doi:10.1021/la011338p · Cited by 85 · see citing works
Membrane solubilization by detergent: use of brominated phospholipids to evaluate the detergent-induced changes in calcium-ATPase/lipid interaction
de FORESTA, B., le Maire, M., Orlowski, S., et al. (1989) · Biochemistry · doi:10.1021/bi00432a032 · Cited by 84 · see citing works
Self-citation
Localization of Glycolipids in Membranes by In Vivo Labeling and Neutron Diffraction
Weik, M., Patzelt, H., Zaccaı̈, G., et al. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80041-6 · Cited by 84 · see citing works
Lipids—Plants and Microbes
Cunningham, B. (1985) · Biochemical Society Transactions · doi:10.1042/bst0130537 · Cited by 82 · see citing works
Statistical thermodynamic analysis of peptide and protein insertion into lipid membranes
Ben‐Shaul, A., Ben‐Tal, N., & Honig, B. H. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79208-1 · Cited by 80 · see citing works
Quantitative study of the fluidity of Escherichia coli membranes using deuterium magnetic resonance
Nichol, C. P., Davis, J. H., Weeks, G., et al. (1980) · Biochemistry · doi:10.1021/bi00544a008 · Cited by 79 · see citing works
Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane
Corcelli, A., Lattanzio, V. M. T., Mascolo, G., et al. (2002) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)30196-6 · Cited by 79 · see citing works
Dependence of lipid membrane phase transition temperature on the mismatch of protein and lipid hydrophobic thickness
Sperotto, M. M., & Mouritsen, O. G. (1988) · European Biophysics Journal · doi:10.1007/bf00255320 · Cited by 79 · see citing works
Activation of beef-heart cytochrome c oxidase by cardiolipin and analogues of cardiolipin
Abramovitch, D. A., Marsh, D., & Powell, G. L. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90090-q · Cited by 77 · see citing works
Selectivity in Lipid Binding to the Bacterial Outer Membrane Protein OmpF
O’Keeffe, A. H., East, J. M., & LEE, A. G. J. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76454-x · Cited by 77 · see citing works
Self-citation
The essential role of specific Halobacterium halobium polar lipids in 2D-array formation of bacteriorhodopsin
Papahadjopoulos‐Sternberg, B., L'Hostis, C., Whiteway, C. A., et al. (1992) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(92)90110-8 · Cited by 77 · see citing works
Simultaneous modeling of phase and calorimetric behavior in an amphiphilic peptide phospholipid model membrane
Morrow, M. R., Huschilt, J. C., & Davis, J. H. (1985) · Biochemistry · doi:10.1021/bi00341a018 · Cited by 75 · see citing works
Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex
Montecucco, C., Smith, G. A., Dabbeni‐Sala, F., et al. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80588-7 · Cited by 75 · see citing works
Molecular Theory of Chain Packing, Elasticity and Lipid-Protein Interaction in Lipid Bilayers
Ben‐Shaul, A. (1995) · Handbook of biological physics · doi:10.1016/s1383-8121(06)80024-2 · Cited by 73 · see citing works
Molecular Organization and Dynamics of 1-Palmitoyl-2-oleoylphosphatidylcholine Bilayers Containing a Transmembrane α-Helical Peptide
Subczynski, W. K., Lewis, R. N. A. H., McElhaney, R. N., et al. (1998) · Biochemistry · doi:10.1021/bi972148+ · Cited by 73 · see citing works
Consequences of Hydrophobic Mismatch between Lipids and Melibiose Permease on Melibiose Transport
Dumas, F., Tocanne, J., Leblanc, G., et al. (2000) · Biochemistry · doi:10.1021/bi992634s · Cited by 72 · see citing works
Structure and Dynamics of K Channel Pore-Lining Helices: A Comparative Simulation Study
Shrivastava, I. H., Capener, C. E., Forrest, L. R., & Sansom, M. S. P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76574-x · Cited by 71 · see citing works
Where does cholesterol act during activation of the nicotinic acetylcholine receptor?
Addona, G. H., Sandermann, H., Kloczewiak, M. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00280-0 · Cited by 71 · see citing works
Self-Association of Model Transmembrane α-Helices Is Modulated by Lipid Structure
Mall, S., Broadbridge, R. J., Sharma, R. P., et al. (2001) · Biochemistry · doi:10.1021/bi011075y · Cited by 70 · see citing works
Self-citation
Hydrophobic mismatch and long‐range protein/lipid interactions in bacteriorhodopsin/phosphatidylcholine vesicles
Piknova, B., Pérochon, E., & Tocanne, J. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18388.x · Cited by 70 · see citing works
Effects of Bilayer Thickness on the Activity of Diacylglycerol Kinase of Escherichia coli
Pilot, J. D., East, J. M., & LEE, A. G. J. (2001) · Biochemistry · doi:10.1021/bi0103258 · Cited by 69 · see citing works
Self-citation
Ca2+-ATPase structure in the E1 and E2 conformations: mechanism, helix–helix and helix–lipid interactions
Lee, A. G. (2002) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(02)00573-4 · Cited by 66 · see citing works
Self-citation
[17] The spin-labeling technique
Jost, P. C., & Griffith, O. H. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)49019-6 · Cited by 64 · see citing works
Free energy determinants of peptide association with lipid bilayers
Kessel, A., & Ben‐Tal, N. (2002) · Current topics in membranes · doi:10.1016/s1063-5823(02)52010-x · Cited by 63 · see citing works
Interactions of insecticides with biological membranes
LEE, A. G. J., East, J. M., & Balgavý, P. (1991) · Pesticide Science · doi:10.1002/ps.2780320306 · Cited by 63 · see citing works
Self-citation
Fourier transform infrared spectroscopy characterization of the lamellar and nonlamellar structures of free lipid A and Re lipopolysaccharides from Salmonella minnesota and Escherichia coli
Brandenburg, K. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81488-7 · Cited by 60 · see citing works
Effects Of Lipid Environment On Membrane Transport: The Human Erythrocyte Sugar Transport Protein/Lipid Bilayer System
Carruthers, A., & Melchior, D. L. (1988) · Annual Review of Physiology · doi:10.1146/annurev.ph.50.030188.001353 · Cited by 60 · see citing works
Structural Properties of Docosahexaenoyl Phospholipid Bilayers Investigated by Solid-State 2H NMR Spectroscopy
Petrache, H. I., Salmon, A., & Brown, M. F. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011745n · Cited by 59 · see citing works
Light-induced Reorganization of Phospholipids in Rod Disc Membranes
Hessel, E., Müller, P. (. 1., Herrmann, A., & Hofmann, K. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009061200 · Cited by 58 · see citing works
Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: differential scanning calorimetric and Fourier transform infrared spectroscopic studies
Zhang, Y., Lewis, R., Hodges, R. S., et al. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80261-4 · Cited by 56 · see citing works
Effect of Protein Hydration on Receptor Conformation: Decreased Levels of Bound Water Promote Metarhodopsin II Formation
Mitchell, D. C., & Litman, B. J. (1999) · Biochemistry · doi:10.1021/bi990634m · Cited by 52 · see citing works
A determination of the mobility gradient in lipid bilayers by 13C nuclear magnetic resonance
Lee, A., Birdsall, N. J. M., Metcalfe, J. C., et al. (1976) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1976.0045 · Cited by 52 · see citing works
Self-citation
Effects of Aromatic Residues at the Ends of Transmembrane α-Helices on Helix Interactions with Lipid Bilayers
Mall, S., Broadbridge, R. J., Sharma, R. P., LEE, A. G. J., & East, J. M. (2000) · Biochemistry · doi:10.1021/bi992205u · Cited by 52 · see citing works
Self-citation
Association of spin-labelled cardiolipin with dimyristoylphosphatidylcholine-substituted bovine heart cytochrome c oxidase. A generalized specificity increase rather than highly specific binding sites
Powell, G. L., Knowles, P. F., & Marsh, D. (1985) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(85)90409-2 · Cited by 51 · see citing works
Binding of long-chain alkyl derivatives to lipid bilayers and to calcium-magnesium ATPase
Froud, R. J., East, J. M., Rooney, E. K., & Lee, A. G. (1986) · Biochemistry · doi:10.1021/bi00371a042 · Cited by 51 · see citing works
Self-citation
Importance of Specific Native Lipids in Controlling the Photocycle of Bacteriorhodopsin
Joshi, M. K., Dracheva, S., Mukhopadhyay, A. K., et al. (1998) · Biochemistry · doi:10.1021/bi980965j · Cited by 50 · see citing works
Expression of the Mitochondrial ADP/ATP Carrier inEscherichia coli
Heimpel, S., Basset, G., Odoy, S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010586200 · Cited by 49 · see citing works
Band 3 protein—cholesterol interactions in erythrocyte membranes
Schubert, D., & Boss, K. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)81295-7 · Cited by 48 · see citing works
Reconstituted human erythrocyte sugar transporter activity is determined by bilayer lipid groups
Tefft, R. E., Carruthers, A., & Melchior, D. L. (1986) · Biochemistry · doi:10.1021/bi00360a035 · Cited by 46 · see citing works
Is There a Conserved Interaction between Cardiolipin and the Type II Bacterial Reaction Center?
Wakeham, M. C., Sessions, R. B., Jones, M. R., & Fyfe, P. K. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76112-7 · Cited by 46 · see citing works
Interactions of cholesterol hemisuccinate with phospholipids and calcium-magnesium ATPase
Simmonds, A. C., Rooney, E. K., & Lee, A. G. (1984) · Biochemistry · doi:10.1021/bi00302a015 · Cited by 46 · see citing works
Self-citation
Cell and Model Membrane Interactions
Ohki, S. (1991) · Springer eBooks · doi:10.1007/978-1-4615-3854-7 · Cited by 45 · see citing works
Protein-lipid interactions and differential scanning calorimetric studies of bacteriorhodopsin reconstituted lipid-water systems
Alonso, A., Restall, C. J., Turner, M., et al. (1982) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(82)90261-9 · Cited by 42 · see citing works
Identification of Protein Side Chains near the Membrane−Aqueous Interface: A Site-Directed Spin Labeling Study of KcsA
Gross, A., & Hubbell, W. L. (2001) · Biochemistry · doi:10.1021/bi015828s · Cited by 40 · see citing works
Characterization of the Thermotropic Behavior and Lateral Organization of Lipid-Peptide Mixtures by a Combined Experimental and Theoretical Approach: Effects of Hydrophobic Mismatch and Role of Flanking Residues
Morein, S., Killian, J. A., & Sperotto, M. M. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75495-7 · Cited by 37 · see citing works
Epidermal Growth Factor Receptor Transmembrane Domain: 2H NMR Implications for Orientation and Motion in a Bilayer Environment
Jones, D. H., Barber, K. R., VanDerLoo, E. W., et al. (1998) · Biochemistry · doi:10.1021/bi981520y · Cited by 36 · see citing works

Flagged first, then by citations

Research works printed but not linked: 6

Davoust, 1982, J. Magn. Res., 48, 475
Mouritsen, 1993, Annu. Rev. Biophys. Bioeng., 22, 145, 10.1146/annurev.bb.22.060193.001045 · DOI
Verma, 1983, Adv. Lipid Res., 20, 257
White, 1999, Annu. Rev. Biophys. Biomol. Struct., 28, 319, 10.1146/annurev.biophys.28.1.319 · DOI
Hoffmann, 1980, J. Mol. Biol., 141, 132
Litman, 1996, vol. 2A, 1

Sorted by citations

Lipid rafts as a membrane-organizing principle
Lingwood, D., & Simons, K. (2010) · Science · doi:10.1126/science.1174621 · Cited by 4,417 · see citing works
Evidence for the Formation of Symmetric and Asymmetric DLPC-DAPC Lipid Bilayer Domains
Ritter, M., Schmidt, S., Jakab, M., Paulmichl, M., & Henderson, R. M. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350122 · Cited by 3,923 · see citing works
Membrane proteins, lipids and detergents: not just a soap opera
Seddon, A. M., Curnow, P., & Booth, P. J. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.04.011 · Cited by 1,340 · see citing works
“Crystallography of membrane proteins has also provided an insight into the roles of specific membrane lipids in key biophysical functions within the protein–lipid environment [83,84].”
Background
How lipids affect the activities of integral membrane proteins
LEE, A. G. J. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.05.012 · Cited by 1,195 · see citing works
“Most of the lipid molecules resolved in high-resolution crystal structures of membrane proteins are likely to be nonannular lipids, their strong binding to the protein leading to immobilization of at least part of the lipid molecule so that they appear in the high-resolution structure [7].”
BackgroundInfluentialSelf-citation
OPM: Orientations of Proteins in Membranes database
Lomize, M. A., Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btk023 · Cited by 1,178 · see citing works
“…X-ray scattering, neutron diffraction, electron cryo-microscopy, and NMR or infrared spectroscopy for several dozen cases, such as rhodopsin, lactose permease, mechanosensitive and potassium channels, or C2 domains (Frilingos et al., 1998, Lee 2003, Hubbell et al., 2003, Malmberg and Falke, 2005).”
Background
Lipid rafts: at a crossroad between cell biology and physics
Jacobson, K., Mouritsen, O. G., & Anderson, R. G. W. (2007) · Nature Cell Biology · doi:10.1038/ncb0107-7 · Cited by 1,101 · see citing works
Bilayer Thickness and Membrane Protein Function: An Energetic Perspective
Andersen, O. S., & Koeppe, R. E. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132643 · Cited by 870 · see citing works
“In fact, when lipid molecules can be discerned and identified in membrane protein structures, they usually are resolved only in part (59, 60)—even at cryogenic temperatures— suggesting limited chemical specificity, significant disorder/mobility, or both.”
Background
Getting Across the Cell Membrane: An Overview for Small Molecules, Peptides, and Proteins
Yang, N. J., & Hinner, M. J. (2015) · Methods in Molecular Biology · doi:10.1007/978-1-4939-2272-7_3 · Cited by 826 · see citing works
“Membrane proteins can actively influence the organization of the membrane by forming specific and nonspecific interactions with lipids in the immediate boundary [7, 8].”
Background
Protein–surfactant interactions: A tale of many states
Otzen, D. E. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.03.003 · Cited by 639 · see citing works
“The tetrameric potassium channel KcsA binds anionic phospholipids at a “non-annular” site [249], originally identified through crystallography [250] and mass spectrometry [251].”
Background
Regulation of membrane protein structure and function by their lipid nano-environment
Levental, I., & Lyman, E. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00524-4 · Cited by 590 · see citing works
What's so special about cholesterol?
Mouritsen, O. G., & Zuckermann, M. J. (2004) · Lipids · doi:10.1007/s11745-004-1336-x · Cited by 535 · see citing works
How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
Fantini, J., & Barrantes, F. J. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00031 · Cited by 532 · see citing works
“By the same token, Trp, and Tyr have an aromatic structure compatible with the apolar region of the membrane, but contain an −OH group (Tyr) or an N atom (Trp) capable of forming hydrogen bonds with polar groups (Lee, 2003).”
BackgroundInfluential
Freeze-Drying of Aqueous Solutions of Deep Eutectic Solvents: A Suitable Approach to Deep Eutectic Suspensions of Self-Assembled Structures
Gutiérrez, M. C., Ferrer, M. L., Mateo, C. R., & del Monte, F. (2009) · Langmuir · doi:10.1021/la900552b · Cited by 526 · see citing works
Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins
Hagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310901f · Cited by 499 · see citing works
Responses of microorganisms to osmotic stress.
Bremer, E., & Krämer, R. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-115504 · Cited by 463 · see citing works
Lipids in membrane protein structures
Pálsdóttir, H., & Hunte, C. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.012 · Cited by 424 · see citing works
Lipids do influence protein function—the hydrophobic matching hypothesis revisited
Jensen, M. Ø., & Mouritsen, O. G. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.009 · Cited by 407 · see citing works
The gramicidin ion channel: A model membrane protein
Kelkar, D. A., & Chattopadhyay, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.011 · Cited by 381 · see citing works
“It is becoming increasingly clear that subtle properties of the membrane environment such as membrane thickness and order, besides lipid composition, influence membrane protein function [132–135].”
Background
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354 · see citing works
Lateral Pressure Profile, Spontaneous Curvature Frustration, and the Incorporation and Conformation of Proteins in Membranes
Marsh, D. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.107938 · Cited by 369 · see citing works
“Prominent among these is, for instance, hydrophobic matching (89,116,117).”
Background
Structure of the Rotor of the V-Type Na + -ATPase from Enterococcus hirae
Murata, T., Yamato, I., Kakinuma, Y., Leslie, A. G. W., & Walker, J. E. (2005) · Science · doi:10.1126/science.1110064 · Cited by 354 · see citing works
The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane
Saidi, Y., Finka, A., Muriset, M., et al. (2009) · The Plant Cell · doi:10.1105/tpc.108.065318 · Cited by 351 · see citing works
“Severe changes in membrane fluidity have been previously found to impact on ion channel activity (Collins et al., 1993; Lee, 2003).”
Background
Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes
Lundbæk, J. A., Collingwood, S. A., Ingólfsson, H. I., Kapoor, R., & Andersen, O. S. (2009) · Journal of The Royal Society Interface · doi:10.1098/rsif.2009.0443 · Cited by 340 · see citing works
Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
Moon, C. P., & Fleming, K. G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103979108 · Cited by 333 · see citing works
Coarse-grained molecular dynamics simulations of membrane proteins and peptides
Bond, P. J., Holyoake, J., Ivetac, A., Khalid, S., & Sansom, M. S. P. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.10.004 · Cited by 325 · see citing works
Protein modulation of lipids, and vice-versa, in membranes
Marsh, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.01.015 · Cited by 320 · see citing works
“An alternative explanation for these rather low free energies was proposed by Lee and coworkers [20,246]: that the protein distorts to alleviate mismatch with the hydrophobic span of the lipid chains.”
BackgroundMethodInfluential
Insertion and Assembly of Membrane Proteins via Simulation
Bond, P. J., & Sansom, M. S. P. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0569104 · Cited by 307 · see citing works
Lipid metabolism in myelinating glial cells: lessons from human inherited disorders and mouse models
Chrast, R., Saher, G., Nave, K.-A., & Verheijen, M. H. G. (2011) · Journal of Lipid Research · doi:10.1194/jlr.r009761 · Cited by 314 · see citing works
Role of cholesterol in the function and organization of G-protein coupled receptors
Pucadyil, T. J., & Chattopadhyay, A. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.02.002 · Cited by 296 · see citing works
The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump
MØLLER, J. V., Olesen, C., Winther, A.-M. L., et al. (2010) · Quarterly Reviews of Biophysics · doi:10.1017/s003358351000017x · Cited by 284 · see citing works
“From such experiments, it has been concluded that there is no appreciable difference between the phospholipid compo- sition of the annulus and the bilayer, neither with respect to head group specificity nor hydro- carbon length (Lee, 2003).”
BackgroundInfluential
Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282 · see citing works
Computational Investigation of Interaction between Nanoparticles and Membranes: Hydrophobic/Hydrophilic Effect
Li, Y., Chen, X., & Gu, N. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp8051906 · Cited by 282 · see citing works
Simulation Studies of Protein-Induced Bilayer Deformations, and Lipid-Induced Protein Tilting, on a Mesoscopic Model for Lipid Bilayers with Embedded Proteins
Venturoli, M., Smit, B., & Sperotto, M. M. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.050849 · Cited by 274 · see citing works
“This knowledge is biologically relevant, since there are experimental evidences suggesting that a mismatch-induced change of the tilt-angle of individual helices in channel bundle-proteins is the cause of changed protein activity (Lee, 2003).”
Background
Regulation of Sodium Channel Function by Bilayer Elasticity
Lundbæk, J. A., Birn, P., Hansen, A. J., Søgaard, R., Hélix‐Nielsen, C., Girshman, J., Bruno, M. J., Tape, S. E., Egebjerg, J., Greathouse, D. V., et al. (2004) · The Journal of General Physiology · doi:10.1085/jgp.200308996 · Cited by 258 · see citing works
“Nonphysiological amphiphiles ( -octyl-glucoside, Genapol X-100, Triton X-100, and reduced Triton X-100) that make lipid bilayers less “stiff”, as measured using gA channels, shift the voltage dependence of sodium channel inactivation toward more hyperpolarized potentials.”
Background
Positioning of proteins in membranes: A computational approach
Lomize, A. L., Pogozheva, I. D., Lomize, M. A., & Mosberg, H. I. (2006) · Protein Science · doi:10.1110/ps.062126106 · Cited by 260 · see citing works
Niosomes, an alternative for liposomal delivery
Bartelds, R., Nematollahi, M. H., Pols, T., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194179 · Cited by 252 · see citing works
“Taken together, niosomes behave in many aspects similar to phospholipid-based vesicles but they may not provide the right lipid headgroup composition for functional membrane transport, that is, the requirement of many transporters for a fraction of anionic headgroups[27].”
Background
Cholesterol modulates ligand binding and G-protein coupling to serotonin1A receptors from bovine hippocampus
Pucadyil, T. J., & Chattopadhyay, A. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.03.010 · Cited by 249 · see citing works
“This raises the obvious possibility that the overall membrane order and dynamics could be an important modulator of receptor structure and function [15,16].”
Background
Intracellular sterol dynamics
Mesmin, B., & Maxfield, F. R. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.03.002 · Cited by 243 · see citing works
“In addition to phospholipids, cytosolic and membrane proteins can interact with cholesterol [13,14], and they may also influence the cholesterol distribution.”
Background
The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Kaur, H., Jakob, R. P., Marzinek, J. K., Green, R., Imai, Y., Bolla, J. R., Agustoni, E., Robinson, C. V., Bond, P. J., Lewis, K., et al. (2021) · Nature · doi:10.1038/s41586-021-03455-w · Cited by 244 · see citing works
Transmembrane proteins in the Protein Data Bank: identification and classification
Tusnády, G., Dosztányi, Z., & Simon, I. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth340 · Cited by 242 · see citing works
“With the exception of a few tightly bound lipid or detergent molecules, the deposited experimental data have no direct indication that the protein is immersed into the membrane under native conditions , and do not contain information about the exact location of the lipid bilayer (Lee, 2003).”
Background
ROLES OF BILAYER MATERIAL PROPERTIES IN FUNCTION AND DISTRIBUTION OF MEMBRANE PROTEINS
McIntosh, T. J., & Simon, S. A. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102022 · Cited by 232 · see citing works
Structural basis for self-assembly of a cytolytic pore lined by protein and lipid
Tanaka, K., Caaveiro, J. M. M., Morante, K., González‐Mañas, J. M., & Tsumoto, K. (2015) · Nature Communications · doi:10.1038/ncomms7337 · Cited by 227 · see citing works
The significance of lipid composition for membrane activity: New concepts and ways of assessing function
Vı́gh, L., Escribá, P. V., Sonnleitner, A., Sonnleitner, M., Piotto, S., Maresca, B., Horváth, I., & Harwood, J. L. (2005) · Progress in Lipid Research · doi:10.1016/j.plipres.2005.08.001 · Cited by 230 · see citing works
The Serotonin1A A Receptor: A Representative Member of the Serotonin Receptor Family
Pucadyil, T. J., Kalipatnapu, S., & Chattopadhyay, A. (2005) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-005-3969-3 · Cited by 226 · see citing works
“function of biological membranes (Lee, 2003).”
Background
Membrane structural biology: with biochemical and biophysical foundations
(2015) · Choice Reviews Online · doi:10.5860/choice.187617 · Cited by 230 · see citing works
The role of tryptophan side chains in membrane protein anchoring and hydrophobic mismatch
de Jesus, A. J., & Allen, T. W. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.09.009 · Cited by 220 · see citing works
“For membrane proteins, an important factor governing protein stability and function is the hydrophobic mismatch that arises from a difference in the hydrophobic length of the TM segment and the thickness of the surrounding lipid bilayer [9,17,38,39].”
Background
Lipid rafts as functional heterogeneity in cell membranes
Lingwood, D., Kaiser, H.-J., Levental, I., & Simons, K. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370955 · Cited by 218 · see citing works
Biological membranes: the importance of molecular detail
LEE, A. G. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.007 · Cited by 214 · see citing works
Self-citation
Lipid‐Induced ER Stress: Synergistic Effects of Sterols and Saturated Fatty Acids
Pineau, L., Colas, J., Dupont, S., Beney, L., Fleurat‐Lessard, P., Berjeaud, J., Bergès, T., & Ferreira, T. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00903.x · Cited by 206 · see citing works
“Interestingly, in the G phase, polytopic proteins tend to form aggregates (48).”
Background
Capsaicin Regulates Voltage-Dependent Sodium Channels by Altering Lipid Bilayer Elasticity
Lundbæk, J. A., Birn, P., Tape, S. E., Toombes, G. E. S., Søgaard, R., Koeppe, R. E., Gruner, S. M., Hansen, A. J., & Andersen, O. S. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.013573 · Cited by 206 · see citing works
“bilayer interface (Lee, 2003) perturb the surrounding bilayer”
Background
Portability of paddle motif function and pharmacology in voltage sensors
Alabi, A. A., Bahamonde, M. I., Jung, H. J., Kim, J. I., & Swartz, K. J. (2007) · Nature · doi:10.1038/nature06266 · Cited by 204 · see citing works
Interaction of G protein coupled receptors and cholesterol
Gimpl, G. (2016) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2016.04.006 · Cited by 204 · see citing works
Convergent evolution of defensin sequence, structure and function
Shafee, T. M. A., Lay, F. T., Phan, T. K., Anderson, M. A., & Hulett, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2344-5 · Cited by 203 · see citing works
“Hydrophobic interactions are typically neither energetic, nor specific enough to achieve this [140, 141] and consequently the proteins rely on multiple electrostatic contacts with the charged head groups (on the order of 10 kJ mol energy each [142].”
Background
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR
Hagn, F., Nasr, M., & Wagner, G. (2017) · Nature Protocols · doi:10.1038/nprot.2017.094 · Cited by 180 · see citing works
Coarse-Grained MD Simulations of Membrane Protein-Bilayer Self-Assembly
Scott, K. A., Bond, P. J., Ivetac, A., Chetwynd, A. P., Khalid, S., & Sansom, M. S. P. (2008) · Structure · doi:10.1016/j.str.2008.01.014 · Cited by 207 · see citing works
“Several surveys have been conducted of lipid and/or detergent molecules bound to membrane proteins in crystal structures (Lee, 2003; Marsh and Pali, 2004, 2006; Palsdottir and Hunte, 2004).”
Background
Lipids and membrane protein structures
Hunte, C., & Richers, S. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.03.008 · Cited by 196 · see citing works
Membrane Cholesterol in the Function and Organization of G-Protein Coupled Receptors
Paila, Y. D., & Chattopadhyay, A. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-8622-8_16 · Cited by 195 · see citing works
“proteins remains in contact with the membrane (Lee, 2003), and reaction centers in them are often buried within the membrane, the function of membrane proteins depends on the surrounding membrane lipid environment.”
Background
Functional engineered channels and pores (Review)
Bayley, H., & Jayasinghe, L. (2004) · Molecular Membrane Biology · doi:10.1080/09687680410001716853 · Cited by 194 · see citing works
“There are several other situations where more attention should be given to the participation of lipids (Lee 2003, Hong and Tamm 2004).”
Background
Structural basis for the cooperative allosteric activation of the free fatty acid receptor GPR40
Lu, J., Byrne, N. J., Wang, J. C. K., Bricogne, G., Brown, F. K., Chobanian, H. R., Colletti, S. L., Salvo, J. D., Thomas-Fowlkes, B. S., Guo, Y., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3417 · Cited by 192 · see citing works
Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts
Martens, J. R., O’Connell, K. M. S., & Tamkun, M. M. (2003) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2003.11.007 · Cited by 189 · see citing works
Mechanistic role of ergosterol in membrane rigidity and cycloheximide resistance in Saccharomyces cerevisiae
Abe, F., & Hiraki, T. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.12.002 · Cited by 181 · see citing works
“The surface of a membrane protein contains shallow grooves and protrusions to which fatty acids and sterols conform to provide tight packing and function (reviewed in [46,47]).”
Lipid–protein interactions
LEE, A. G. J. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390761 · Cited by 179 · see citing works
Self-citation
Bacterial osmosensing: roles of membrane structure and electrostatics in lipid–protein and protein–protein interactions
Poolman, B., Spitzer, J. J., & Wood, J. M. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.013 · Cited by 177 · see citing works
“Although these lipids are less mobile than those in the bulk phase, the differences are relatively small and annular lipids are able to exchange with those in the bulk phase on the time scale of (sub)microsecond [7].”
Background
Chilling-injury and disturbance of ion homeostasis in the coxal muscle of the tropical cockroach (Nauphoeta cinerea)
Košťál, V., Yanagimoto, M., & Bastl, J. (2005) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2005.11.005 · Cited by 176 · see citing works
“The lipidic composition influences the membrane physico-chemical properties (Hazel, 1989, 1997), which, in turn, influences the function of membrane proteins (Lee, 2003; Palsdottir and Hunte, 2004), including ATPases (Cornelius, 2001; Haines, 2001).”
Background
Specificity of Intramembrane Protein-Lipid InteractionsPreprint
Contreras, F. ‐., Ernst, A. M., Wieland, F., & Brügger, B. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004705 · Cited by 167 · see citing works
“For membrane proteins, different types of interactions with lipid molecules can be distinguished by the relative “residence” time of a particular lipid at the protein–lipid interface (Lee 2003).”
Background
Receptor-independent actions of cannabinoids on cell membranes: Focus on endocannabinoids
Öz, M. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.09.009 · Cited by 164 · see citing works
“However, molecular insight into the functioning ion channels indicates that processes of voltage sensing or ligand-binding leads to conformational changes associated with the alterations of the 3-dimensional structure of the protein (Lee, 2003; Garcia, 2004; Lee & MacKinnon, 2004).”
BackgroundInfluential
Molecular Docking Characterizes Substrate-Binding Sites and Efflux Modulation Mechanisms within P-Glycoprotein.
Ferreira, R. J., Ferreira, M. U., & dos Santos, D. J. V. A. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci400195v · Cited by 163 · see citing works
Phosphatidylglycerol and sulfoquinovosyldiacylglycerol: anionic membrane lipids and phosphate regulation
Frentzen, M. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.03.001 · Cited by 161 · see citing works
Plant membrane assays with cytokinin receptors underpin the unique role of free cytokinin bases as biologically active ligands
Lomin, S. N., Krivosheev, D. M., Steklov, M. Y., et al. (2015) · Journal of Experimental Botany · doi:10.1093/jxb/eru522 · Cited by 158 · see citing works
Microbial diversity and adaptation to high hydrostatic pressure in deep-sea hydrothermal vents prokaryotes
Jebbar, M., Franzetti, B., Girard, É., & Oger, P. (2015) · Extremophiles · doi:10.1007/s00792-015-0760-3 · Cited by 158 · see citing works
“As can be expected, perturbation in lipid phase state has profound consequences on membrane structure and function (Lee 2003, 2004).”
Background
Examining the Contributions of Lipid Shape and Headgroup Charge on Bilayer Behavior
Dickey, A. N., & Faller, R. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.128074 · Cited by 157 · see citing works
Non-covalent binding of membrane lipids to membrane proteins
Yèagle, P. L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.11.009 · Cited by 157 · see citing works
“If however the protein is in a bilayer that is thinner than the hydrophobic surface on the protein, the protein may alter conformation (such as a tilt [1–3] or a bend [4,5] in the transmembrane portion) to better accommodate the hydrophobic portion of the bilayer, or the bilayer may distort to cover the hydrophobic su…”
Background
Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts
Fabiani, C., & Antollini, S. S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00309 · Cited by 152 · see citing works
“Contrarily, non-annular lipids are in close contact with the protein, probably in between α-helix transmembrane segments or subunits, and can be associated to lipid binding sites with a slow exchange rate with bulk lipids (Lee, 2003).”
Background
Exploring the membrane proteome—Challenges and analytical strategies
Helbig, A. O., Heck, A. J. R., & Slijper, M. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.01.005 · Cited by 153 · see citing works
“show crucial impact on the function of membrane proteins [64].”
Background
Synthetic peptides as models for intrinsic membrane proteins
Killian, J. A. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01154-2 · Cited by 152 · see citing works
Docosahexaenoic acid alters bilayer elastic properties
Bruno, M. J., Koeppe, R. E., & Andersen, O. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701015104 · Cited by 150 · see citing works
Multicompartment Lipid Cubic Nanoparticles with High Protein Upload: Millisecond Dynamics of Formation
Angelov, B., Angelova, A., Filippov, S. K., Drechsler, M., Štěpánek, P., & Lesieur, S. (2014) · ACS Nano · doi:10.1021/nn5012946 · Cited by 150 · see citing works
Adaptation of the membrane in Archaea
Oger, P., & Cario, A. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.020 · Cited by 149 · see citing works
“As can be expected from the central role of the membrane for the cell, perturbation in lipid phase state has profound consequences on membrane structure and function [41,42].”
TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates
Tusnády, G., Dosztányi, Z., & Simon, I. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti121 · Cited by 149 · see citing works
“With the exception of a few tightly bound lipid molecules, the deposited experimental data have no direct indication that the protein is immersed into the membrane under native conditions, and do not contain information about the exact location of the lipid bilayer (Lee, 2003).”
Background
Spin Selectivity in Photoinduced Charge-Transfer Mediated by Chiral Molecules
Abendroth, J. M., Stemer, D. M., Bloom, B. P., Roy, P., Naaman, R., Waldeck, D. H., Weiss, P. S., & Mondal, P. C. (2019) · ACS Nano · doi:10.1021/acsnano.9b01876 · Cited by 149 · see citing works
Specific protein–lipid interactions in membrane proteins
Hunte, C. (2005) · Biochemical Society Transactions · doi:10.1042/bst20050938 · Cited by 145 · see citing works
Control of the postsynaptic membrane viscosity
Renner, M., Choquet, D., & Triller, A. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4445-08.2009 · Cited by 145 · see citing works
“The rigidity of lipids that surround integral proteins is strongly affected by the protein (Anderson and Jacobson, 2002; Lee, 2003).”
Background
Lipids from Hermetia illucens, an Innovative and Sustainable Source
Franco, A., Scieuzo, C., Salvia, R., Petrone, A. M., Tafi, E., Moretta, A., Schmitt, É., & Falabella, P. (2021) · Sustainability · doi:10.3390/su131810198 · Cited by 161 · see citing works
Screening Blockers Against a Potassium Channel with a Droplet Interface Bilayer Array
Syeda, R., Holden, M. A., Hwang, W. L., & Bayley, H. (2008) · Journal of the American Chemical Society · doi:10.1021/ja804968g · Cited by 142 · see citing works
Identification of Cholesterol Binding Sites in the Serotonin1A Receptor
Sengupta, D., & Chattopadhyay, A. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp309888u · Cited by 141 · see citing works
Bacterial Reaction Centers Purified with Styrene Maleic Acid Copolymer Retain Native Membrane Functional Properties and Display Enhanced Stability
Swainsbury, D. J. K., Scheidelaar, S., van Grondelle, R., Killian, J. A., & Jones, M. R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201406412 · Cited by 138 · see citing works
Lipids in photosynthetic reaction centres: Structural roles and functional holes
Jones, M. R. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.06.001 · Cited by 138 · see citing works
Interactions between lipids and voltage sensor paddles detected with tarantula toxins
Milescu, M., Bosmans, F., Lee, S., Alabi, A. A., Kim, J. I., & Swartz, K. J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1679 · Cited by 137 · see citing works
“1, the effects of modification of sphingomyelin can be diminished by toxins that bind to voltage sensors 7, raising the possibility that sphingomyelin interacts directly with voltage sensors in the channel, perhaps similar to the non-annular lipids observed for other membrane proteins 13,14.”
Binding of Anionic Lipids to at Least Three Nonannular Sites on the Potassium Channel KcsA is Required for Channel Opening
Marius, P., Zagnoni, M., Sandison, M. E., et al. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117507 · Cited by 135 · see citing works
“In studies of lipid binding, it is convenient to distinguish between two classes of site, annular or boundary sites on the transmembrane surface of a membrane protein, and nonannular sites located between transmembrane a-helices (9,10); according to this definition, the lipid binding sites identified in the crystal st…”
BackgroundSelf-citation
Flotillins functionally organize the bacterial membrane
Bach, J. N., & Bramkamp, M. (2013) · Molecular Microbiology · doi:10.1111/mmi.12252 · Cited by 137 · see citing works
“of membrane embedded protein machineries such as the protein secretion system need a specialized lipid environment (Lee, 2003).”
BackgroundInfluential
Principles of membrane protein interactions with annular lipids deduced from aquaporin‐0 2D crystals
Hite, R. K., Li, Z., & Walz, T. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.68 · Cited by 134 · see citing works
“Together, these observations suggest that the exact chemical identities of the phospholipid headgroups have a negligible role in the interaction of annular lipids with membrane proteins, corroborating previous results obtained by spin-labelling studies (Lee, 2003).”
BackgroundResult
Characterization of Two Oxidatively Modified Phospholipids in Mixed Monolayers with DPPC
Sabatini, K., Mattila, J.-P., Megli, F. M., & Kinnunen, P. K. J. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080176 · Cited by 126 · see citing works
Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method
Bagos, P. G., Liakopoulos, T. D., & Hamodrakas, S. J. (2005) · BMC Bioinformatics · doi:10.1186/1471-2105-6-7 · Cited by 126 · see citing works
“Thus, it is believed that the outer membrane possesses an average thickness around 25–30 Å, a fact mainly explainable by its lipid composition, average hydrophobicity and asymmetry [51].”
How lipids and proteins interact in a membrane: a molecular approach
LEE, A. G. J. (2005) · Molecular BioSystems · doi:10.1039/b504527d · Cited by 125 · see citing works
Self-citation
Interaction of Melittin with Membrane Cholesterol: A Fluorescence Approach
Raghuraman, H., & Chattopadhyay, A. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.043596 · Cited by 125 · see citing works
“Lipid-protein interactions are vital for the organization and function of biological membranes (Lee, 2003).”
Background
A subset of annular lipids is linked to the flippase activity of an ABC transporter
Bechara, C., Noll, A., Morgner, N., Degiacomi, M. T., Tampé, R., & Robinson, C. V. (2015) · Nature Chemistry · doi:10.1038/nchem.2172 · Cited by 124 · see citing works
Coarse-grained simulation: a high-throughput computational approach to membrane proteins
Sansom, M. S. P., Scott, K. A., & Bond, P. J. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360027 · Cited by 123 · see citing works
Complete Predicted Three-Dimensional Structure of the Facilitator Transmembrane Protein and Hepatitis C Virus Receptor CD81: Conserved and Variable Structural Domains in the Tetraspanin Superfamily
Seigneuret, M. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.069666 · Cited by 122 · see citing works
“Complete spanning of the lipid bilayer (;40 Å) by a transmembrane helix requires an at least 26-residue length (42).”
Background
Insights on P-Glycoprotein’s Efflux Mechanism Obtained by Molecular Dynamics Simulations
Ferreira, R. J., Ferreira, M. U., & dos Santos, D. J. V. A. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300083m · Cited by 121 · see citing works
Nanostructured bicontinuous cubic lipid self-assembly materials as matrices for protein encapsulation
Conn, C. E., & Drummond, C. J. (2013) · Soft Matter · doi:10.1039/c3sm27743g · Cited by 120 · see citing works

Authors: Lee, A. G.
Affiliations: University of Southampton (GB)
Corresponding author: Lee, A.G
Venue: Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher: Elsevier BV
Published: 2003-05
Volume: 1612
Issue: 1
Pages: 1-40
ISSN: 0005-2736 (ISSN-L)
DOI: 10.1016/s0005-2736(03)00056-7
OpenAlex: W2128882835
Cited by: 886
References: 224
Citations by year: 2026: 31 · 2025: 30 · 2024: 25 · 2023: 16 · 2022: 32 · 2021: 33 · 2020: 31 · 2019: 51 · 2018: 37 · 2017: 33 · 2016: 32 · 2015: 51 · 2014: 47 · 2013: 38 · 2012: 32
FWCI: 3.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3766 d)
Locations: Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: protein-lipid interactions, membrane proteins, lipid bilayers, transmembrane helices, hydrophobic mismatch, membrane thickness, helix tilt, anionic phospholipids, lipid phase, membrane protein structure
MeSH terms: Animals, Bacteriorhodopsins, Crystallization, Humans, Lipid Bilayers, Membrane Lipids, Membrane Proteins, Protein Structure, Secondary, Photosynthetic Reaction Center Complex Proteins, Hydrophobic and Hydrophilic Interactions

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Lipid–protein interactions in biological membranes: A structural perspective

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks