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Membranes: a meeting point for lipids, proteins and therapies
Open accessAbstract
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 [70].”
From Permeabilizing Cell Membranes with Electric Fields (2021) · cites this paper as [70]
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Citations
Cites
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
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 6,851
Lipid rafts and signal transduction
Simons, K., & Toomre, D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 5,371
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
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
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 2,426
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
Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898
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
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 1,691
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×
“In mammals, a number of MAPK pathways coexist, including the ERK1/2, c-Jun N-terminal kinase (JNK) and p38 MAPK cascades [237, 238].”
BackgroundMOLECULAR 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 1,556
Physical principles of membrane organization
Israelachvili, J. N., Marĉelja, S., & Horn, R. G. (1980) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500001645 · Cited by 1,440
Biochemistry of Lipids, Lipoproteins and Membranes
(2021) · Elsevier eBooks · doi:10.1016/c2020-0-00089-7 · Cited by 1,402
Lipid sorting in epithelial cells
Simons, K., & Gerrit van, M. E. E. R. (1988) · Biochemistry · doi:10.1021/bi00417a001 · Cited by 1,373
den Kamp, J. A. F. O. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.000403 · Cited by 1,262
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
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
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 1,128
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
Kellenberger, S., & Schild, L. (2002) · Physiological Reviews · doi:10.1152/physrev.00007.2002 · Cited by 1,029
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 1,006
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
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
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
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
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×
“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.”
ResultEmerging structure of the Nicotinic Acetylcholine receptors
Karlin, A. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn731 · Cited by 924
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
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
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 743
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 731
Molecular basis of mechanosensory transduction
Gillespie, P. G., & Walker, R. G. (2001) · Nature · doi:10.1038/35093011 · Cited by 708
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
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
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
Perozo, E., Kloda, A., Cortés, D. M., & Martinac, B. (2002) · Nature Structural Biology · doi:10.1038/nsb827 · Cited by 661
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
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
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
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
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
Takai, Y., Kishimoto, A., Inoue, M., & Nishizuka, Y. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41009-x · Cited by 595
Triantafilou, M., Miyake, K., Golenbock, D. T., & Triantafilou, K. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2603 · Cited by 581
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
Regulation of transbilayer plasma membrane phospholipid asymmetry
Daleke, D. L. (2003) · Journal of Lipid Research · doi:10.1194/jlr.r200019-jlr200 · Cited by 570
The Structure of Biological Membranes
Yèagle, P. L. (2011) · CRC Press eBooks · doi:10.1201/b11018 · Cited by 565
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
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
Self-citationExosome-dependent Trafficking of HSP70
Lancaster, G. I., & Febbraio, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502017200 · Cited by 547
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
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
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
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 521
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
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
PIKE, L. J., Han, X., Chung, K.-N., & Gross, R. W. (2002) · Biochemistry · doi:10.1021/bi0156557 · Cited by 512
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
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
The Lateral Pressure Profile in Membranes: A Physical Mechanism of General Anesthesia
Cantor, R. S. (1997) · Biochemistry · doi:10.1021/bi9627323 · Cited by 467
Marshall, C. J. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80066-4 · Cited by 463
Lipid translocation across the plasma membrane of mammalian cells
Bevers, E. M., Comfurius, P., Dekkers, D. W. C., & Zwaal, R. F. A. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00110-9 · Cited by 455
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
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 450
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
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
Self-citationLipids 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
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 420
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
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
Mabrey, S., Mateo, P. L., & Sturtevant, J. M. (1978) · Biochemistry · doi:10.1021/bi00605a034 · Cited by 408
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
Thelen, M., Rosen, A., Nairn, A. C., & Aderem, A. A. (1991) · Nature · doi:10.1038/351320a0 · Cited by 394
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
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
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
Heat shock proteins as emerging therapeutic targets
Sőti, C., Nagy, E., Giricz, Z., Vı́gh, L., Csermely, P., & Ferdinandy, P. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706396 · Cited by 381
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
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
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
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
Schrempf, H., Schmidt, O., Kümmerlen, R., Hinnah, S. C., Müller, D., Betzler, M., Steinkamp, T., & Wagner, R. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00201.x · Cited by 349
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
Self-citationChalfant, 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
The G Protein Subunit Gene Families
Downes, G. B., & Gautam, N. (1999) · Genomics · doi:10.1006/geno.1999.5992 · Cited by 329
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
Interaction of cholesterol with various glycerophospholipids and sphingomyelin
Sankaram, M. B., & Thompson, T. E. (1990) · Biochemistry · doi:10.1021/bi00499a014 · Cited by 316
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
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
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
Self-citationPhospholipid-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
Self-citationCorrelation between acetylcholine receptor function and structural properties of membranes
Fong, T. M., & McNamee, M. G. (1986) · Biochemistry · doi:10.1021/bi00352a015 · Cited by 306
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
Broquet, A. H., Thomas, G., Masliah, J., Trugnan, G., & Bachelet, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302326200 · Cited by 303
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
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
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
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
Bretscher, M. S. (1972) · Journal of Molecular Biology · doi:10.1016/s0022-2836(72)80020-2 · Cited by 291
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
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
Iwabuchi, K., Handa, K., & Hakomori, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33766 · Cited by 286
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
Self-citationGlomset, J. A., & Farnsworth, C. C. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.001145 · Cited by 283
Träuble, H., & Overath, P. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90296-4 · Cited by 279
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
Self-citationHolopainen, J. M., Subramanian, M., & Kinnunen, P. K. J. (1998) · Biochemistry · doi:10.1021/bi980915e · Cited by 277
Self-citationFormation 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 277
Self-citationTörök, 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
Self-citationReceptor-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
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
Goñi, F. M., & Alonso, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.011 · Cited by 269
Self-citationThe 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 269
Self-citationAmphitropic proteins: regulation by reversible membrane interactions (Review)
Johnson, J. E., & Cornell, R. B. (1999) · Molecular Membrane Biology · doi:10.1080/096876899294544 · Cited by 266
Heat Shock Proteins, Inflammation, and Cardiovascular Disease
Pockley, A. G. (2002) · Circulation · doi:10.1161/hc0802.103729 · Cited by 266
Goñi, F. M., & Alonso, A. (1999) · Progress in Lipid Research · doi:10.1016/s0163-7827(98)00021-6 · Cited by 257
Self-citationEvidence 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
Self-citationReversible palmitoylation of signaling proteins
Mumby, S. M. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80056-7 · Cited by 254
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
Eyster, K. M. (2007) · AJP Advances in Physiology Education · doi:10.1152/advan.00088.2006 · Cited by 249
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 235
Self-citationVı́gh, 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 233
Self-citationIsoform-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
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
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
Self-citationVillalba, 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
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
Chen, W., Wang, J., Shao, C.-S., Liu, S., Yu, Y., Wang, Q., & Cao, X. (2006) · European Journal of Immunology · doi:10.1002/eji.200535501 · Cited by 214
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 213
Self-citationBrusés, J. L., Chauvet, N., & Rutishauser, U. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00504.2001 · Cited by 212
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
PIKE, L. J., Han, X., & Gross, R. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503805200 · Cited by 206
Jones, O., & McNamee, M. G. (1988) · Biochemistry · doi:10.1021/bi00407a018 · Cited by 204
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
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
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
Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts.
Martens, J., O'Connell, K. M. S., & Tamkun, M. (2004) · TIPS - Trends in Pharmacological Sciences · doi:10.1016/j.tips.2003.11.007 · Cited by 197
Ktistakis, N. T., Brown, H. A., Sternweis, P. C., & Roth, M. G. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4952 · Cited by 197
Biochemistry of lipids, lipoproteins and membranes
Higgins, J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81166-j · Cited by 193
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
Regulation of G proteins by covalent modification
Chen, C. A., & Manning, D. R. (2001) · Oncogene · doi:10.1038/sj.onc.1204185 · Cited by 191
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 190
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
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
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
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
Self-citationEmoto, K., Inadome, H., Kanaho, Y., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504282200 · Cited by 181
Lipid regulation of the synaptic vesicle cycle
Rohrbough, J. C., & Broadie, K. S. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1608 · Cited by 179
Phospholipid transfer proteins revisited
WIRTZ, K. W. A. (1997) · Biochemical Journal · doi:10.1042/bj3240353 · Cited by 178
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 178
Self-citationThe 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
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
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
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 171
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
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
The structure of biological membranes
Wiederschain, G. Y. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906030175 · Cited by 165
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 163
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
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
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
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 157
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
Funari, S. S., Barceló, F., & Escribá, P. V. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m200356-jlr200 · Cited by 156
Self-citationThermal 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
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
Balogh, G. E., Horváth, I., Nagy, E., Hoyk, Z., Benkö, S., Bensaude, O., & Vı́gh, L. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04999.x · Cited by 150
Self-citationLipid 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 150
Self-citationBijur, G. N., & Jope, R. S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752401.x · Cited by 145
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
Self-citationNew TRP Channels in Hearing and Mechanosensation
Corey, D. P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00505-1 · Cited by 138
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
Self-citationBarlič, A., Gutiérrez‐Aguirre, I., Caaveiro, J. M. M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313817200 · Cited by 136
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
Marius, P., Zagnoni, M., Sandison, M. E., et al. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117507 · Cited by 135
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
Self-citationElion, E. A. (1998) · Science · doi:10.1126/science.281.5383.1625 · Cited by 133
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
Fong, T. M., & McNamee, M. G. (1987) · Biochemistry · doi:10.1021/bi00387a020 · Cited by 130
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
Davies, S. M. A., Epand, R. M., Kraayenhof, R., et al. (2001) · Biochemistry · doi:10.1021/bi010904c · Cited by 128
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
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
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
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
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
Observation of Topical Catalysis by Sphingomyelinase Coupled To Microspheres
Nurminen, T. A., Holopainen, J. M., Zhao, H., et al. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017807r · Cited by 120
Wittinghofer, A. (1998) · PubMed · Cited by 119
Pertile, P., Liscovitch, M., Caspi, V. C., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5130 · Cited by 119
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
Self-citationShah, M., Patel, K., Fried, V. A., & Sehgal, P. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205935200 · Cited by 118
Gating prokaryotic mechanosensitive channels
Perozo, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1833 · Cited by 117
Role for lipid rafts in regulating interleukin-2 receptor signaling
Marmor, M. D., & Julius, M. (2001) · Blood · doi:10.1182/blood.v98.5.1489 · Cited by 116
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
Self-citationHolthuis, J. C. M., Gerrit van, M. E. E. R., & Huitema, K. (2003) · Molecular Membrane Biology · doi:10.1080/0988768031000100768 · Cited by 114
Yu, J.-Z., & Rasenick, M. M. (2002) · Molecular Pharmacology · doi:10.1124/mol.61.2.352 · Cited by 113
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
Hynes, T. R., Mervine, S. M., Yost, E. A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405151200 · Cited by 112
Martinac, B., & Hamill, O. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072632899 · Cited by 111
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
Self-citation
Research works printed but not linked: 4
- Kinnunen PKJ, 1996, Nonmedical applications of liposomes, 153
- Kinnunen PKJ, 2002, Ceramide signaling. Molecular biology intellingence unit 21, 9
- Kolonics A, 2006, BGP‐15, a new type of insuline sensitizer, Diabetes., 55, A483
- Kovacs E, 1994, Heat stress induces association of the GroEL‐analog chaperonin with thylakoid membranes in cyanobacterium, Synechocystis PCC 6803, Plant Physiol Biochem., 32, 285
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Metadata
- 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
- 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
- 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
- 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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