Membranes: A meeting point for lipids, proteins and therapies

Escribá, Pablo V.; González‐Ros, José M.; Goñi, Félix M.; Kinnunen, Paavo K. J.; Vigh, Lászlo; Sánchez‐Magraner, Lissete; Fernández, Asia M.; Busquets, Xavier; Horváth, Ibolya; Barceló‐Coblijn, Gwendolyn

doi:10.1111/j.1582-4934.2008.00281.x

Cited by 454Lipid Membrane Structure and BehaviorCaveolin-1 and cellular processesSphingolipid Metabolism and Signaling

Membranes: A meeting point for lipids, proteins and therapies

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Escribá, Pablo V., González‐Ros, José M., Goñi, Félix M., Kinnunen, Paavo K. J., Vigh, Lászlo, Sánchez‐Magraner, Lissete, Fernández, Asia M., Busquets, Xavier +2 more·2008·Journal of Cellular and Molecular Medicine

DOI 10.1111/j.1582-4934.2008.00281.xPMC PMC4401130

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Abstract

Membranes constitute a meeting point for lipids and proteins. Not only do they define the entity of cells and cytosolic organelles but they also display a wide variety of important functions previously ascribed to the activity of proteins alone. Indeed, lipids have commonly been considered a mere support for the transient or permanent association of membrane proteins, while acting as a selective cell/organelle barrier. However, mounting evidence demonstrates that lipids themselves regulate the location and activity of many membrane proteins, as well as defining membrane microdomains that serve as spatio-temporal platforms for interacting signalling proteins. Membrane lipids are crucial in the fission and fusion of lipid bilayers and they also act as sensors to control environmental or physiological conditions. Lipids and lipid structures participate directly as messengers or regulators of signal transduction. Moreover, their alteration has been associated with the development of numerous diseases. Proteins can interact with membranes through lipid co-/post-translational modifications, and electrostatic and hydrophobic interactions, van der Waals forces and hydrogen bonding are all involved in the associations among membrane proteins and lipids. The present study reviews these interactions from the molecular and biomedical point of view, and the effects of their modulation on the physiological activity of cells, the aetiology of human diseases and the design of clinical drugs. In fact, the influence of lipids on protein function is reflected in the possibility to use these molecular species as targets for therapies against cancer, obesity, neurodegenerative disorders, cardiovascular pathologies and other diseases, using a new approach called membrane-lipid therapy.

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The depolarized resting Vm in cancer cells relative to that in non-cancer cells is thought to be caused by altered lipid and sterol membrane composition, which results in an influx of sodium ions into the cell and a collection of negative charges on the cell coat.
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From Permeabilizing Cell Membranes with Electric Fields (2021) · cites this paper as [70]

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The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158 · see citing works
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
Lipid rafts and signal transduction
Simons, K., & Toomre, D. K. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 6,252 · see citing works
Intracellular Signaling by Hydrolysis of Phospholipids and Activation of Protein Kinase C
Nishizuka, Y. (1992) · Science · doi:10.1126/science.1411571 · Cited by 4,472 · see citing works
Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
Fadok, V. A., Voelker, D. R., Campbell, P. A., Cohen, J., Bratton, D. L., & Henson, P. M. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.7.2207 · Cited by 3,321 · see citing works
Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore
Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996) · Science · doi:10.1126/science.274.5294.1859 · Cited by 2,378 · see citing works
PROTEIN PRENYLATION: Molecular Mechanisms and Functional Consequences
Zhang, F. L., & Casey, P. J. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.001325 · Cited by 2,018 · see citing works
Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulatorsPreprint
Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898 · see citing works
All ras proteins are polyisoprenylated but only some are palmitoylated
Hancock, J. F., Magee, A. I., Childs, J. E., & Marshall, C. J. (1989) · Cell · doi:10.1016/0092-8674(89)90054-8 · Cited by 1,775 · see citing works
Experimentally determined hydrophobicity scale for proteins at membrane interfaces
Wimley, W. C., & White, S. H. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb1096-842 · Cited by 1,657 · see citing works
Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600 · cited 1× · see citing works
“In mammals, a number of MAPK pathways coexist, including the ERK1/2, c-Jun N-terminal kinase (JNK) and p38 MAPK cascades [237, 238].”
Background
MOLECULAR AND EVOLUTIONARY BASIS OF THE CELLULAR STRESS RESPONSE
Kültz, D. (2004) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.040403.103635 · Cited by 1,520 · see citing works
Physical principles of membrane organization
Israelachvili, J. N., Marĉelja, S., & Horn, R. G. (1980) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500001645 · Cited by 1,406 · see citing works
Biochemistry of Lipids, Lipoproteins and Membranes
(2021) · Elsevier eBooks · doi:10.1016/c2020-0-00089-7 · Cited by 1,400 · see citing works
Lipid sorting in epithelial cells
Simons, K., & Gerrit van, M. E. E. R. (1988) · Biochemistry · doi:10.1021/bi00417a001 · Cited by 1,373 · see citing works
Lipid Asymmetry in Membranes
den Kamp, J. A. F. O. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.000403 · Cited by 1,262 · see citing works
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
FUNCTION AND REGULATION OF RAS
Lowy, D. R., & Willumsen, B. M. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004223 · Cited by 1,164 · see citing works
The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Comfurius, P., Kastelijn, D., & Deenen, L. L. M. V. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90143-0 · Cited by 1,105 · see citing works
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
Epithelial Sodium Channel/Degenerin Family of Ion Channels: A Variety of Functions for a Shared Structure
Kellenberger, S. B., & Schild, L. (2002) · Physiological Reviews · doi:10.1152/physrev.00007.2002 · Cited by 1,017 · see citing works
Caveolins, Liquid-Ordered Domains, and Signal Transduction
Smart, E. J., Graf, G. A., McNiven, M. A., Sessa, W. C., Engelman, J. A., Scherer, P. E., Okamoto, T., & Lisanti, M. P. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7289 · Cited by 1,005 · see citing works
Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
Pebay‐Peyroula, E., Dahout-Gonzalez, C., Kahn, R., Trézéguet, V., Lauquin, G. J. ‐., & Brandolin, G. (2003) · Nature · doi:10.1038/nature02056 · Cited by 998 · see citing works
Sphingolipid–Cholesterol Rafts Diffuse as Small Entities in the Plasma Membrane of Mammalian Cells
Pralle, A., Keller, P., Florin, E., Simons, K., & Hörber, J. K. H. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.997 · Cited by 988 · see citing works
Hsp27 negatively regulates cell death by interacting with cytochrome c
Bruey, J., Ducasse, C., Bonniaud, P., Ravagnan, L., Susín, S. A., Diaz‐Latoud, C., Gurbuxani, S. K., Arrigo, A., Kroemer, G., Solary, É., et al. (2000) · Nature Cell Biology · doi:10.1038/35023595 · Cited by 986 · see citing works
Protein kinase C and other diacylglycerol effectors in cancer
Griner, E. M., & Kazanietz, M. G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2110 · Cited by 978 · see citing works
Architecture of succinate dehydrogenase and reactive oxygen species generation
Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927 · cited 1× · see citing works
“Interestingly, there are reports on the detection on lipid bound in the crystal structures of other membrane proteins [127–129] and, therefore, it is likely that such proteins might be regulated by lipid in a manner similar to that of KcsA.”
Result
Emerging structure of the Nicotinic Acetylcholine receptors
Karlin, A. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn731 · Cited by 921 · see citing works
Abnormal Proteins Serve as Eukaryotic Stress Signals and Trigger the Activation of Heat Shock Genes
Ananthan, J., Goldberg, A. L., & Voellmy, R. W. (1986) · Science · doi:10.1126/science.3083508 · Cited by 905 · see citing works
The role of phosphatidylserine in recognition of apoptotic cells by phagocytes
Fadok, V. A., Bratton, D. L., Frasch, S. C., Warner, M. L., & Henson, P. M. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400404 · Cited by 776 · see citing works
Direct visualization of Ras proteins in spatially distinct cell surface microdomains
Prior, I. A., Muncke, C., Parton, R. G., & Hancock, J. F. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209091 · Cited by 735 · see citing works
Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling
Hollinger, S., & Hepler, J. R. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.527 · Cited by 727 · see citing works
Molecular basis of mechanosensory transduction
Gillespie, P. G., & Walker, R. G. (2001) · Nature · doi:10.1038/35093011 · Cited by 708 · see citing works
Heat Shock Protein 70 Surface-Positive Tumor Exosomes Stimulate Migratory and Cytolytic Activity of Natural Killer Cells
Gastpar, R., Gehrmann, M., Bausero, M. A., Asea, A. A. A., Groß, C. C., Schroeder, J. A., & Multhoff, G. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3804 · Cited by 696 · see citing works
The Regulation of Exosome Secretion: a Novel Function of the p53 Protein
Yu, X., Harris, S. L., & Levine, A. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4579 · Cited by 688 · see citing works
SNAREs are concentrated in cholesterol‐dependent clusters that define docking and fusion sites for exocytosis
Lang, T., Bruns, D., Wenzel, D., Riedel, D., Holroyd, P., Thiele, C., & Jahn, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2202 · Cited by 686 · see citing works
Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
Perozo, E., Kloda, A., Cortés, D. M., & Martinac, B. (2002) · Nature Structural Biology · doi:10.1038/nsb827 · Cited by 661 · see citing works
Insights into G Protein Structure, Function, and Regulation
Cabrera-Vera, T. M., Vanhauwe, J. F. M., Thomas, T. O., Medkova, M., Preininger, A. M., Mazzoni, M. R., & Hamm, H. E. (2003) · Endocrine Reviews · doi:10.1210/er.2000-0026 · Cited by 660 · see citing works
A mammalian two pore domain mechano‐gated S‐like K+ channel
Patel, A. J., Honoré, É., Maingret, F., Lesage, F., Fink, M., Duprat, F., & Lazdunski, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4283 · Cited by 644 · see citing works
Phospholipase D: a Downstream Effector of ARF in Granulocytes
Cockcroft, S., Thomas, G. M. H., Fensome, A. C., Geny, B., Cunningham, E., Gout, I. T., Hiles, I. D., Totty, N. F., Truong, O., & Hsuan, J. J. (1994) · Science · doi:10.1126/science.8290961 · Cited by 631 · 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
The Comprehensive Sourcebook of Bacterial Protein Toxins
ALOUF, J. E., Ladant, D., & Popoff, M. R. (2015) · Elsevier eBooks · doi:10.1016/c2013-0-14258-4 · Cited by 612 · see citing works
Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. I. Purification and characterization of an active enzyme from bovine cerebellum.
Takai, Y., Kishimoto, A., Inoue, M., & Nishizuka, Y. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41009-x · Cited by 595 · see citing works
Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation
Triantafilou, M., Miyake, K., Golenbock, D. T., & Triantafilou, K. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2603 · Cited by 581 · see citing works
Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
Schütz, G. J., Kada, G., Pastushenko, V. P., & Schindler, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.5.892 · Cited by 576 · see citing works
Regulation of transbilayer plasma membrane phospholipid asymmetry
Daleke, D. L. (2003) · Journal of Lipid Research · doi:10.1194/jlr.r200019-jlr200 · Cited by 570 · see citing works
The Structure of Biological Membranes
Yèagle, P. L. (2011) · CRC Press eBooks · doi:10.1201/b11018 · Cited by 565 · see citing works
Lipid activation of protein kinase C.
Bell, R. M., & Burns, D. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67698-2 · Cited by 555 · see citing works
HSP72 protects against obesity-induced insulin resistance
Chung, J., Nguyen, A.-K., Henstridge, D. C., Holmes, A. G., Chan, M. H. S., Mesa, J. L., Lancaster, G. I., Southgate, R. J., Bruce, C. R., Duffy, S. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705799105 · Cited by 553 · see citing works
Self-citation
Exosome-dependent Trafficking of HSP70
Lancaster, G. I., & Febbraio, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502017200 · Cited by 547 · see citing works
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545 · see citing works
COFACTOR PROTEINS IN THE ASSEMBLY AND EXPRESSION OF BLOOD CLOTTING ENZYME COMPLEXES
Mann, K. G., Jenny, R. J., & Krishnaswamy, S. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.004411 · Cited by 534 · see citing works
Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex
Nichols, B. J., Kenworthy, A. K., Polishchuk, R., Lodge, R., Roberts, T. H., Hirschberg, K., Phair, R. D., & Lippincott‐Schwartz, J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.3.529 · Cited by 525 · see citing works
Dynamic, yet structured: The cell membrane three decades after the Singer–Nicolson model
Vereb, G., Szöllõsi, J., Matkó, J., Nagy, P., Farkas, T., Vı́gh, L., Mátyus, L., Waldmann, T. A., & Damjanovich, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332550100 · Cited by 519 · see citing works
Lipid domains in membranes. Evidence derived from structural perturbations induced by free fatty acids and lifetime heterogeneity analysis.
Klausner, R. D., Kleinfeld, A. M., Hoover, R. L., et al. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86027-1 · Cited by 517 · see citing works
GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
Prior, I. A., Harding, A. S., Yan, J., Sluimer, J. C., Parton, R. G., & Hancock, J. F. (2001) · Nature Cell Biology · doi:10.1038/35070050 · Cited by 513 · see citing works
Lipid Rafts Are Enriched in Arachidonic Acid and Plasmenylethanolamine and Their Composition Is Independent of Caveolin-1 Expression: A Quantitative Electrospray Ionization/Mass Spectrometric Analysis
PIKE, L. J., Han, X., Chung, K.-N., & Gross, R. W. (2002) · Biochemistry · doi:10.1021/bi0156557 · Cited by 512 · see citing works
The concept of lipid domains in membranes.
Karnovsky, M. J., Kleinfeld, A. M., Hoover, R. L., & Klausner, R. D. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.1.1 · Cited by 470 · see citing works
Pore-forming protein toxins: from structure to function
Parker, M. W., & Feil, S. C. (2004) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2004.01.009 · Cited by 468 · see citing works
The Lateral Pressure Profile in Membranes: A Physical Mechanism of General Anesthesia
Cantor, R. S. (1997) · Biochemistry · doi:10.1021/bi9627323 · Cited by 467 · see citing works
Ras effectors
Marshall, C. J. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80066-4 · Cited by 463 · see citing works
Induction of heat shock proteins in B-cell exosomes
Clayton, A., Turkes, A., Navabi, H., Mason, M. D., & Tabi, Z. (2005) · Journal of Cell Science · doi:10.1242/jcs.02494 · Cited by 454 · see citing works
Lipid translocation across the plasma membrane of mammalian cells
Bevers, E. M., Comfurius, P., Dekkers, D. W. C., et al. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00110-9 · Cited by 445 · see citing works
Physiological Regulation of G Protein-Linked Signaling
Morris, A. J., & Malbon, C. C. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1373 · Cited by 444 · 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
Biophysical properties of lipids and dynamic membranes
Janmey, P. A., & Kinnunen, P. K. J. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.08.009 · Cited by 431 · see citing works
Self-citation
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
Phospholipids and the origin of cationic gating charges in voltage sensors
Schmidt, D., Jiang, Q.-X., & MacKinnon, R. (2006) · Nature · doi:10.1038/nature05416 · Cited by 417 · 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 412 · see citing works
Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
Parker, M. W., Buckley, J. T., Postma, J. P. M., Tucker, A. D., Leonard, K., Pattus, F., & Tsernoglou, D. (1994) · Nature · doi:10.1038/367292a0 · Cited by 411 · see citing works
Does the membrane's physical state control the expression of heat shock and other genes?
Vı́gh, L., Maresca, B., & Harwood, J. L. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01279-1 · Cited by 408 · see citing works
High-sensitivity scanning calorimetric study of mixtures of cholesterol with dimyristoyl- and dipalmitoylphosphatidylcholines
Mabrey, S., Mateo, P. L., & Sturtevant, J. M. (1978) · Biochemistry · doi:10.1021/bi00605a034 · Cited by 408 · see citing works
Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
Thelen, M., Rosen, A., Nairn, A. C., & Aderem, A. A. (1991) · Nature · doi:10.1038/351320a0 · Cited by 394 · see citing works
Lysophospholipids Open the Two-pore Domain Mechano-gated K+ Channels TREK-1 and TRAAK
Maingret, F., Patel, A. J., Lesage, F., Lazdunski, M., & Honoré, É. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10128 · Cited by 391 · see citing works
HSP60 trafficking in adult cardiac myocytes: role of the exosomal pathway
Gupta, S., & Knowlton, A. A. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01355.2006 · Cited by 390 · see citing works
CALORIMETRIC EVIDENCE FOR THE LIQUID-CRYSTALLINE STATE OF LIPIDS IN A BIOMEMBRANE
Steim, J. M., Tourtellotte, M. E., Reinert, J. C., et al. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.1.104 · Cited by 382 · see citing works
Heat shock proteins as emerging therapeutic targets
Sőti, C., Nagy, E., Giricz, Z., et al. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706396 · Cited by 380 · see citing works
Modulation of Ras and a-Factor Function by Carboxyl-Terminal Proteolysis
Boyartchuk, V., Ashby, M. N., & Rine, J. (1997) · Science · doi:10.1126/science.275.5307.1796 · Cited by 361 · see citing works
The Product of par-4, a Gene Induced during Apoptosis, Interacts Selectively with the Atypical Isoforms of Protein Kinase C
Díaz-Meco, M. T., Municio, M. M., Frutos, S., Sánchez‐Gómez, P., Lozano, J., Sanz, L., & Moscat, J. (1996) · Cell · doi:10.1016/s0092-8674(00)80152-x · Cited by 361 · see citing works
Extracellular heat shock proteins in cell signaling
Calderwood, S. K., Mambula, S. S., Gray, P. J., et al. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.044 · Cited by 360 · see citing works
A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans.
Schrempf, H., Schmidt, O., Kümmerlen, R., et al. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00201.x · Cited by 353 · see citing works
Proteomic Analysis of Exosomes Secreted by Human Mesothelioma Cells
Hegmans, J. P., Bard, M. P. L., Hemmes, A., Luider, T. M., Kleijmeer, M. J., Prins, J., Zitvogel, L., Burgers, S. A., Hoogsteden, H. C., & Lambrecht, B. N. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63739-x · Cited by 350 · see citing works
Small heat-shock proteins regulate membrane lipid polymorphism
Tsvetkova, N. M., Horváth, I., Török, Z., Wolkers, W. F., Balogi, Z., Shigapova, N., Crowe, L. M., Tablin, F., Vierling, E., Crowe, J. H., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192468399 · Cited by 340 · see citing works
Self-citation
De Novo Ceramide Regulates the Alternative Splicing of Caspase 9 and Bcl-x in A549 Lung Adenocarcinoma Cells
Chalfant, C. E., Rathman, K., Pinkerman, R. L., Wood, R. E., Obeid, L. M., Öğretmen, B., & Hannun, Y. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112010200 · Cited by 337 · see citing works
The G Protein Subunit Gene Families
Downes, G. B., & Gautam, N. (1999) · Genomics · doi:10.1006/geno.1999.5992 · Cited by 329 · 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
Interaction of cholesterol with various glycerophospholipids and sphingomyelin
Sankaram, M. B., & Thompson, T. E. (1990) · Biochemistry · doi:10.1021/bi00499a014 · Cited by 316 · see citing works
The small heat shock proteins and their clients
Nakamoto, H., & Vı́gh, L. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6321-2 · Cited by 316 · see citing works
The dynamic role of palmitoylation in signal transduction
Milligan, G., Parenti, M. D., & Magee, A. I. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89004-0 · Cited by 316 · see citing works
Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: Identification of hsp17 as a “fluidity gene”
Horváth, I., Glatz, A., Varvasovszki, V., Török, Z., Páli, T., Balogh, G. E., Kovács, E., Nádasdi, L., Benkö, S., Joó, F., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3513 · Cited by 313 · see citing works
Self-citation
Phospholipid-Cytochrome c Interaction
Tuominen, E. K. J., Wallace, C. J. A., & Kinnunen, P. K. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200056200 · Cited by 309 · see citing works
Self-citation
Correlation between acetylcholine receptor function and structural properties of membranes
Fong, T. M., & McNamee, M. G. (1986) · Biochemistry · doi:10.1021/bi00352a015 · Cited by 306 · see citing works
Spin labels as enzyme substrates Heterogeneous lipid distribution in liver microsomal membranes
STIER, A., & Sackmann, E. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90320-9 · Cited by 305 · see citing works
Expression of the Molecular Chaperone Hsp70 in Detergent-resistant Microdomains Correlates with Its Membrane Delivery and Release
Broquet, A. H., Thomas, G., Masliah, J., Trugnan, G., & Bachelet, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302326200 · Cited by 303 · see citing works
Regulators and Effectors of ras Proteins
Bollag, G. E., & McCormick, F. P. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.003125 · Cited by 302 · see citing works
Signal transduction from multiple Ras effectors
Katz, M. E., & McCormick, F. (1997) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(97)80112-8 · Cited by 299 · see citing works
Spontaneous Curvature of Phosphatidic Acid and Lysophosphatidic Acid
Kooijman, E. E., Chupin, V., Fuller, N. L., Kozlov, M. M., KRUIJFF, B. D., Burger, K. N. J., & Rand, P. R. (2005) · Biochemistry · doi:10.1021/bi0478502 · Cited by 299 · see citing works
Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha.
Wedegaertner, P., Chu, D. H., Wilson, P. T., et al. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74563-3 · Cited by 296 · see citing works
Phosphatidyl-ethanolamine: Differential labelling in intact cells and cell ghosts of human erythrocytes by a membrane-impermeable reagent
Bretscher, M. S. (1972) · Journal of Molecular Biology · doi:10.1016/s0022-2836(72)80020-2 · Cited by 291 · see citing works
Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases
Puri, V., Watanabe, R., Dominguez, M., Sun, X., Wheatley, C. L., Marks, D. L., & Pagano, R. E. (1999) · Nature Cell Biology · doi:10.1038/14084 · Cited by 289 · see citing works
Dynamics in the plasma membrane: how to combine fluidity and order
Marguet, D., Lenne, P., Rigneault, H., & He, H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601204 · Cited by 288 · see citing works
Separation of “Glycosphingolipid Signaling Domain” from Caveolin-containing Membrane Fraction in Mouse Melanoma B16 Cells and Its Role in Cell Adhesion Coupled with Signaling
Iwabuchi, K., Handa, K., & Hakomori, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33766 · Cited by 286 · see citing works
The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803.
Vı́gh, L., Los, D. A., Horváth, I., & Murata, N. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9090 · Cited by 286 · see citing works
Self-citation
Role of Protein Modification Reactions in Programming Interactions Between Ras-Related GTPases and Cell Membranes
Glomset, J. A., & Farnsworth, C. C. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.001145 · Cited by 283 · see citing works
The structure of Escherichia coli membranes studied by fluorescence measurements of lipid phase transitions
Träuble, H., & Overath, P. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90296-4 · Cited by 279 · see citing works
Bimoclomol: A nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects
Vígh, L., Literáti, P. N., Horváth, I., Török, Z., Balogh, G. E., Glatz, A., Kovács, E., Boros, I., Ferdinándy, P., Parkas, B., et al. (1997) · Nature Medicine · doi:10.1038/nm1097-1150 · Cited by 278 · see citing works
Self-citation
Sphingomyelinase Induces Lipid Microdomain Formation in a Fluid Phosphatidylcholine/Sphingomyelin Membrane
Holopainen, J. M., Subramanian, M., & Kinnunen, P. K. J. (1998) · Biochemistry · doi:10.1021/bi980915e · Cited by 277 · see citing works
Self-citation
Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
Török, Z., Goloubinoff, P., Horváth, I., Tsvetkova, N. M., Glatz, A., Balogh, G. E., Varvasovszki, V., Los, D. A., Vierling, E., Crowe, J. H., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051619498 · Cited by 275 · see citing works
Self-citation
Receptor-independent Activators of Heterotrimeric G-protein Signaling Pathways
Takesono, A., Cismowski, M. J., Ribas, C., Bernard, M., Chung, P., Hazard, S., Duzic, E., & Lanier, S. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33202 · Cited by 274 · see citing works
Formation of Amyloid Fibers Triggered by Phosphatidylserine-Containing Membranes
Zhao, H., Tuominen, E. K. J., & Kinnunen, P. K. J. (2004) · Biochemistry · doi:10.1021/bi049002c · Cited by 273 · see citing works
Self-citation
Redistribution of phosphatidylethanolamine at the cleavage furrow of dividing cells during cytokinesis
Emoto, K., Kobayashi, T., Yamaji, A., Aizawa, H., Yahara, I., Inoue, K., & Umeda, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12867 · Cited by 269 · see citing works
Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids
Goñi, F. M., & Alonso, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.011 · Cited by 269 · see citing works
Self-citation
The role of lipid–protein interactions in amyloid-type protein fibril formation
Gorbenko, G. P., & Kinnunen, P. K. J. (2006) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2006.02.006 · Cited by 267 · see citing works
Self-citation
Amphitropic proteins: regulation by reversible membrane interactions (Review)
Johnson, J. E., & Cornell, R. B. (1999) · Molecular Membrane Biology · doi:10.1080/096876899294544 · Cited by 266 · see citing works
Heat Shock Proteins, Inflammation, and Cardiovascular Disease
Pockley, A. G. (2002) · Circulation · doi:10.1161/hc0802.103729 · Cited by 266 · see citing works
Structure and functional properties of diacylglycerols in membranes1This work is dedicated to Professor Vittorio Luzzati on occasion of his 75th birthday.1
Goñi, F. M., & Alonso, A. (1999) · Progress in Lipid Research · doi:10.1016/s0163-7827(98)00021-6 · Cited by 257 · see citing works
Self-citation
Evidence for two distinct acidic phospholipid-binding sites in cytochrome c.
Rytömaa, M., & Kinnunen, P. K. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42094-1 · Cited by 254 · see citing works
Self-citation
Reversible palmitoylation of signaling proteins
Mumby, S. M. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80056-7 · Cited by 254 · see citing works
An Essential Role for a Membrane Lipid in Cytokinesis
Emoto, K., & Umeda, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1215 · Cited by 252 · see citing works
The membrane and lipids as integral participants in signal transduction: lipid signal transduction for the non-lipid biochemist
Eyster, K. M. (2007) · AJP Advances in Physiology Education · doi:10.1152/advan.00088.2006 · Cited by 236 · see citing works
Isoform-specific Localization of Voltage-gated K+Channels to Distinct Lipid Raft Populations
Martens, J. R., Sakamoto, N., Sullivan, S. A., Grobaski, T. D., & Tamkun, M. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009948200 · Cited by 230 · 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
Self-citation
Membrane-lipid therapy: a new approach in molecular medicine
Escribá, P. V. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.11.004 · Cited by 229 · see citing works
Self-citation
Activation of protein kinase C by lipoxin A and other eicosanoids. Intracellular action of oxygenation products of arachidonic acid
Hansson, A., Serhan, C. N., Haeggström, J. Z., et al. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(86)90380-3 · Cited by 226 · see citing works
Evidence for a lipochaperonin: Association of active proteinfolding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
Török, Z., Horváth, I., Goloubinoff, P., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2192 · Cited by 222 · see citing works
Self-citation
Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells
Villalba, M., Bi, K., Rodrı́guez, F., Tanaka, Y., Schoenberger, S. P., & Altman, A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200107080 · Cited by 220 · see citing works
Stimulus-dependent myristoylation of a major substrate for protein kinase C
Aderem, A. A., Albert, K. A., Keum, M. M., et al. (1988) · Nature · doi:10.1038/332362a0 · Cited by 215 · see citing works
On the principles of functional ordering in biological membranes
Kinnunen, P. K. J. (1991) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(91)90087-r · Cited by 211 · see citing works
Self-citation
Efficient induction of antitumor T cell immunity by exosomes derived from heat‐shocked lymphoma cells
Chen, W., Wang, J., Shao, C.-S., et al. (2006) · European Journal of Immunology · doi:10.1002/eji.200535501 · Cited by 209 · see citing works
Membrane Lipid Rafts Are Necessary for the Maintenance of the α7 Nicotinic Acetylcholine Receptor in Somatic Spines of Ciliary Neurons
Brusés, J. L., Chauvet, N., & Rutishauser, U. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00504.2001 · Cited by 208 · 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
Epidermal Growth Factor Receptors Are Localized to Lipid Rafts That Contain a Balance of Inner and Outer Leaflet Lipids
PIKE, L. J., Han, X., & Gross, R. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503805200 · Cited by 206 · 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
Genetic screens in yeast to identify mammalian nonreceptor modulators of G-protein signaling
Cismowski, M. J., Takesono, A., Ma, C., et al. (1999) · Nature Biotechnology · doi:10.1038/12867 · Cited by 202 · see citing works
Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast.
Carratù, L., Franceschelli, S., Pardini, C. L., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.3870 · Cited by 202 · see citing works
Folding of β-sheet membrane proteins: a hydrophobic hexapeptide model
Wimley, W. C., Hristova, K. A., Ladokhin, A. S., et al. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1640 · Cited by 198 · see citing works
Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A.
Ktistakis, N. T., Brown, H. A., Sternweis, P. C., et al. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4952 · Cited by 195 · see citing works
Biochemistry of lipids, lipoproteins and membranes
Higgins, J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81166-j · Cited by 193 · see citing works
Cell Surface-bound Heat Shock Protein 70 (Hsp70) Mediates Perforin-independent Apoptosis by Specific Binding and Uptake of Granzyme B
Groß, C. C., Kolch, W., DeMaio, A., Arispe, N. J., & Multhoff, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302644200 · Cited by 193 · see citing works
Regulation of G proteins by covalent modification
Chen, C. A., & Manning, D. R. (2001) · Oncogene · doi:10.1038/sj.onc.1204185 · Cited by 191 · 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
Ras proteins in the control of the cell cycle and cell differentiation
Crespo, P., & León, J. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000645 · Cited by 189 · see citing works
Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
Ellena, J. F., Blazing, M. A., & McNamee, M. G. (1983) · Biochemistry · doi:10.1021/bi00293a012 · Cited by 187 · see citing works
Ceramide-induced inhibition of T lymphocyte voltage-gated potassium channel is mediated by tyrosine kinases
Gulbins, E., Szabó, I., Baltzer, K., & Lang, F. J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7661 · Cited by 187 · see citing works
Detection of HSP60 on the membrane surface of stressed human endothelial cells by atomic force and confocal microscopy
Pfister, G., Stroh, C. M., Perschinka, H., Kind, M., Knoflach, M., Hinterdorfer, P., & Wick, G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02292 · Cited by 187 · see citing works
Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: Implications for a novel mechanism of action
Zhao, H., Sood, R., Jutila, A., Bose, S., Fimland, G., Nissen-Meyer, J., & Kinnunen, P. K. J. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.037 · Cited by 183 · see citing works
Self-citation
Local Change in Phospholipid Composition at the Cleavage Furrow Is Essential for Completion of Cytokinesis
Emoto, K., Inadome, H., Kanaho, Y., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504282200 · Cited by 181 · see citing works
Phospholipid transfer proteins revisited
WIRTZ, K. W. A. (1997) · Biochemical Journal · doi:10.1042/bj3240353 · Cited by 178 · see citing works
The Effect of Phospholipid Fatty Acid Composition on Membranous Enzymes in Escherichia coli
Mavis, R. D., & Vagelos, P. R. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45658-5 · Cited by 175 · see citing works
Lipid–protein interactions in GPCR-associated signaling
Escribá, P. V., Wedegaertner, P., Goñi, F. M., & Vögler, O. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.001 · Cited by 175 · see citing works
Self-citation
Lipid polymorphism and biomembrane function
KRUIJFF, B. D. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80053-1 · Cited by 174 · see citing works
Lipid regulation of the synaptic vesicle cycle
Rohrbough, J. C., & Broadie, K. S. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1608 · Cited by 173 · see citing works
Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism
Wilson, J. E. (1978) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(78)80029-2 · 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
Ras effectors and their role in mitogenesis and oncogenesis
Joneson, T., & Bar‐Sagi, D. (1997) · Journal of Molecular Medicine · doi:10.1007/s001090050143 · Cited by 168 · see citing works
Talking point Amphitropic proteins: a new class of membrane proteins
Burn, P. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90043-6 · Cited by 167 · see citing works
The structure of biological membranes
Wiederschain, G. Y. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906030175 · Cited by 165 · see citing works
Interplay of C1 and C2 Domains of Protein Kinase C-α in Its Membrane Binding and Activation
Medkova, M., & Cho, W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19852 · Cited by 160 · see citing works
Cytosolic Heat Shock Protein 60, Hypoxia, and Apoptosis
Gupta, S., & Knowlton, A. A. (2002) · Circulation · doi:10.1161/01.cir.0000038112.64503.6e · Cited by 160 · see citing works
LIPID DOMAINS IN MEMBRANES*
Karnovsky, M. J., Kleinfeld, A. M., Hoover, R. L., et al. (1982) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1982.tb25707.x · Cited by 158 · see citing works
Release of the type I secreted α‐haemolysin via outer membrane vesicles from Escherichia coli
Balsalobre, C., Silván, J. M., Fick, S. B., et al. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04938.x · Cited by 156 · see citing works
Effects of oleic acid and its congeners, elaidic and stearic acids, on the structural properties of phosphatidylethanolamine membranes
Funari, S. S., Barceló, F., & Escribá, P. V. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m200356-jlr200 · Cited by 156 · see citing works
Self-citation
Role of membrane lipids in bacterial division-site selection
Mileykovskaya, E., & Dowhan, W. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.02.012 · Cited by 155 · see citing works
Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
Arispe, N. J., Doh, M., Šimáková, O., Kurganov, B. I., & Maio, A. D. (2004) · The FASEB Journal · doi:10.1096/fj.04-2088com · Cited by 154 · see citing works
Thermal behavior of synthetic sphingomyelin-cholesterol dispersions
Estep, T. N., Mountcastle, D. B., Barenholz, Y., et al. (1979) · Biochemistry · doi:10.1021/bi00577a042 · Cited by 153 · see citing works
Membrane Fatty Acid Replacements and Their Effect on Growth and Lectin-Induced Agglutinability
Horwitz, A. F., Hatten, M. E., & Burger, M. M. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.8.3115 · Cited by 151 · see citing works
Lipid dynamics and peripheral interactions of proteins with membrane surfaces
Kinnunen, P. K. J., Kõiv, A., Lehtonen, J. Y. A., Rytömaa, M., & Mustonen, P. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90181-3 · Cited by 148 · see citing works
Self-citation
The hyperfluidization of mammalian cell membranes acts as a signal to initiate the heat shock protein response
Balogh, G. E., Horváth, I., Nagy, E., et al. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04999.x · Cited by 145 · see citing works
Self-citation
Opposing Actions of Phosphatidylinositol 3‐Kinase and Glycogen Synthase Kinase‐3β in the Regulation of HSF‐1 Activity
Bijur, G. N., & Jope, R. S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752401.x · Cited by 144 · see citing works
Phospholipase A2 as a mechanosensor
Lehtonen, J. Y. A., & Kinnunen, P. K. J. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80366-8 · Cited by 142 · see citing works
Self-citation
New TRP Channels in Hearing and Mechanosensation
Corey, D. P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00505-1 · Cited by 140 · see citing works
Lipid microdomains in dimyristoylphosphatidylcholine–ceramide liposomes
Holopainen, J. M., Lehtonen, J. Y. A., & Kinnunen, P. K. J. (1997) · Chemistry and Physics of Lipids · doi:10.1016/s0009-3084(97)00040-6 · Cited by 136 · see citing works
Self-citation
Lipid Phase Coexistence Favors Membrane Insertion of Equinatoxin-II, a Pore-forming Toxin from Actinia equina
Barlič, A., Gutiérrez‐Aguirre, I., Caaveiro, J. M. M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313817200 · Cited by 136 · see citing works
The lateral pressure profile in membranes: a physical mechanism of general anesthesia
Cantor, R. S. (1998) · Toxicology Letters · doi:10.1016/s0378-4274(98)00220-3 · Cited by 135 · see citing works
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
Can the stress protein response be controlled by ‘membrane-lipid therapy’?
Vı́gh, L., Horváth, I., Maresca, B., et al. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.06.009 · Cited by 134 · see citing works
Self-citation
Routing MAP Kinase Cascades
Elion, E. A. (1998) · Science · doi:10.1126/science.281.5383.1625 · Cited by 133 · see citing works
Structural organization of mammalian lipid phosphate phosphatases: implications for signal transduction
Waggoner, D. W., Xu, J., Singh, I. N., Jasińska, R., Zhang, Q., & Brindley, D. N. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00102-x · Cited by 133 · see citing works
Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes
Fong, T. M., & McNamee, M. G. (1987) · Biochemistry · doi:10.1021/bi00387a020 · Cited by 130 · see citing works
HSP27 but not HSP70 has a potent protective effect against α‐synuclein‐induced cell death in mammalian neuronal cells
Zourlidou, A., Smith, M. D. P., & Latchman, D. S. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02273.x · Cited by 129 · see citing works
Regulation of CTP: Phosphocholine Cytidylyltransferase Activity by the Physical Properties of Lipid Membranes: An Important Role for Stored Curvature Strain Energy
Davies, S. M. A., Epand, R. M., Kraayenhof, R., et al. (2001) · Biochemistry · doi:10.1021/bi010904c · Cited by 128 · see citing works
Ceramide-1-phosphate Binds Group IVA Cytosolic Phospholipase a2 via a Novel Site in the C2 Domain
Stahelin, R. V., Subramanian, P., Vora, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701396200 · Cited by 127 · see citing works
Activation-induced subcellular redistribution of Gs alpha.
Wedegaertner, P., Bourne, H. R., & von Zastrow, M. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.8.1225 · Cited by 127 · see citing works
Relationship between cholesterol trafficking and signaling in rafts and caveolae
Fielding, C. J., & Fielding, P. E. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(03)00020-8 · Cited by 124 · see citing works
Optimization of Receptor-G Protein Coupling by Bilayer Lipid Composition I
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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
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Nurminen, T. A., Holopainen, J. M., Zhao, H., et al. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017807r · Cited by 120 · see citing works
Signal transduction via Ras.
Wittinghofer, A. (1998) · PubMed · Cited by 119 · see citing works
Phosphatidylinositol 4,5-Bisphosphate Synthesis Is Required for Activation of Phospholipase D in U937 Cells
Pertile, P., Liscovitch, M., Caspi, V. C., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5130 · Cited by 119 · see citing works
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Nagy, E., Balogi, Z., Gombos, I., Åkerfelt, M., Björkbom, A., Balogh, G. E., Török, Z., Maslyanko, A., Fiszer-Kierzkowska, A., Lisowska, K. M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702557104 · Cited by 118 · see citing works
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Perozo, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1833 · Cited by 117 · see citing works
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Marmor, M. D., & Julius, M. (2001) · Blood · doi:10.1182/blood.v98.5.1489 · Cited by 116 · see citing works
Interactions of STAT3 with Caveolin-1 and Heat Shock Protein 90 in Plasma Membrane Raft and Cytosolic Complexes
Shah, M., Patel, K., Fried, V. A., & Sehgal, P. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205935200 · Cited by 116 · see citing works
Role of lipid polymorphism in G protein-membrane interactions: Nonlamellar-prone phospholipids and peripheral protein binding to membranes
Escribá, P. V., Ozaita, A., Ribas, C., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11375 · Cited by 115 · see citing works
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Lipid microdomains, lipid translocation and the organization of intracellular membrane transport (Review)
Holthuis, J. C. M., Gerrit van, M. E. E. R., & Huitema, K. (2003) · Molecular Membrane Biology · doi:10.1080/0988768031000100768 · Cited by 114 · see citing works
Real-Time Visualization of a Fluorescent Gαs: Dissociation of the Activated G Protein from Plasma Membrane
Yu, J.-Z., & Rasenick, M. M. (2002) · Molecular Pharmacology · doi:10.1124/mol.61.2.352 · Cited by 113 · see citing works
Evidence That Helix 8 of Rhodopsin Acts as a Membrane-Dependent Conformational Switch
Krishna, A. G., Menon, S. T., Terry, T. J., et al. (2002) · Biochemistry · doi:10.1021/bi025534m · Cited by 113 · see citing works
Live Cell Imaging of Gs and the β2-Adrenergic Receptor Demonstrates That Both αs and β1γ7 Internalize upon Stimulation and Exhibit Similar Trafficking Patterns That Differ from That of the β2-Adrenergic Receptor
Hynes, T. R., Mervine, S. M., Yost, E. A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405151200 · Cited by 112 · see citing works
Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness
Martinac, B., & Hamill, O. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072632899 · Cited by 111 · see citing works
Disruption of cellular signaling pathways by daunomycin through destabilization of nonlamellar membrane structures.
Escribá, P. V., Sastre, M., & Garcı́a-Sevilla, J. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7595 · Cited by 110 · see citing works
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[52]Kinnunen PKJ Lasic D Arenholz Y On the mechanisms of the lamellar → hexagonal HII phase transition and the biological significance of the HII propensity Nonmedical applications of liposomes 1996 Boca Raton, FL CRC Press 153 71

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Authors: Escribá, P. V., González‐Ros, J. M., Goñi, F. M., Kinnunen, P. K. J., Vigh, L., Sánchez‐Magraner, L., Fernández, A. M., Busquets, X., Horváth, I., & Barceló‐Coblijn, G.
Affiliations: Research Institute of Health Sciences (ES)
University of the Basque Country (ES)
University of Helsinki (FI)
HUN-REN Szegedi Biológiai Kutatóközpont (HU)
Corresponding author: Escribá, Pablo V.
Goñi, Félix M.
Kinnunen, Paavo K. J.
Barceló‐Coblijn, Gwendolyn
ORCID: Escribá, Pablo V.
Goñi, Félix M.
Kinnunen, Paavo K. J.
Sánchez‐Magraner, Lissete
Busquets, Xavier
Horváth, Ibolya
Barceló‐Coblijn, Gwendolyn
Venue: Journal of Cellular and Molecular Medicine
Publisher: Wiley
Published: 2008-05-21
Volume: 12
Issue: 3
Pages: 829-875
ISSN: 1582-1838 (ISSN-L)
1582-4934
DOI: 10.1111/j.1582-4934.2008.00281.x
PMC: PMC4401130
OpenAlex: W2008091140
Cited by: 454
References: 347
Citations by year: 2026: 22 · 2025: 39 · 2024: 22 · 2023: 35 · 2022: 35 · 2021: 29 · 2020: 30 · 2019: 32 · 2018: 33 · 2017: 23 · 2016: 24 · 2015: 34 · 2014: 17 · 2013: 22 · 2012: 18
FWCI: 1.00
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Cellular and Molecular Medicine (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords: membrane lipids, membrane proteins, protein-lipid interactions, lipid rafts, signal transduction, lipid sensing, cancer therapy, obesity, neurodegenerative diseases, cardiovascular disease
MeSH terms: Animals, Drug Therapy, Humans, Membrane Lipids, Membrane Proteins, Models, Biological, Molecular Structure

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Membranes: A meeting point for lipids, proteins and therapies

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