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Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
Open accessAbstract
Membrane proteins mediate processes that are fundamental for the flourishing of biological cells. Membrane-embedded transporters move ions and larger solutes across membranes; receptors mediate communication between the cell and its environment and membrane-embedded enzymes catalyze chemical reactions. Understanding these mechanisms of action requires knowledge of how the proteins couple to their fluid, hydrated lipid membrane environment. We present here current studies in computational and experimental membrane protein biophysics, and show how they address outstanding challenges in understanding the complex environmental effects on the structure, function, and dynamics of membrane proteins.
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“Dynamic interconversion between multiple conformations underpins the functions of integral membrane proteins in all domains of life (Campbell et al., 2016; Cournia et al., 2015; Shaw et al., 2010; Boehr et al., 2009).”
From Sampling alternative conformational states of transporters and receptors with AlphaFold2 (2022) · cites this paper as Cournia et al., 2015
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Items 201–279 of 279
Evolutionary imprint of activation: The design principles of VSDs
Palovcak, E. J., Delemotte, L., Klein, M. L., & Carnevale, V. (2014) · The Journal of General Physiology · doi:10.1085/jgp.201311103 · Cited by 65
Self-citationPlath, K., Wilkinson, B. M., Stirling, C. J., & Rapoport, T. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-06-0390 · Cited by 64
Voronoi-Based Extraction and Visualization of Molecular Paths
Lindow, N., Baum, D., & Hege, H. (2011) · IEEE Transactions on Visualization and Computer Graphics · doi:10.1109/tvcg.2011.259 · Cited by 63
Self-citationMiddlemas, D. S., & Raftery, M. A. (1987) · Biochemistry · doi:10.1021/bi00379a003 · Cited by 59
Tian, P., & Andricioaei, I. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.035 · Cited by 58
Self-citationEnsemble theory for force networks in hyperstatic granular matter
Snoeijer, J. H., Vlugt, T. J. H., Ellenbroek, W. G., van Hecke, M., & van Leeuwen, J. M. J. (2004) · Physical Review E · doi:10.1103/physreve.70.061306 · Cited by 57
Forcing independent velocity distributions in an experimental granular fluid
Reis, P. M., Ingale, R., & Shattuck, M. D. (2007) · Physical Review E · doi:10.1103/physreve.75.051311 · Cited by 55
Kilian, P. L., Dunlap, C. R., Müeller, P., Schell, M. A., Huganir, R. L., & Racker, E. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91092-x · Cited by 55
Modulation of Alzheimer’s Aβ Protofilament-Membrane Interactions by Lipid Headgroups
Tofoleanu, F., Brooks, B. R., & Buchete, N. (2015) · ACS Chemical Neuroscience · doi:10.1021/cn500277f · Cited by 55
Self-citationSimulations of rigid bodies in an angle-axis framework
Chakrabarti, D., & Wales, D. J. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b818054g · Cited by 54
Self-citationXue, Y., & Ha, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310482 · Cited by 54
Conformational Change in Rhomboid Protease GlpG Induced by Inhibitor Binding to Its S′ Subsites
Xue, Y., Chowdhury, S., Liu, X., Akiyama, Y., Ellman, J. A., & Ha, Y. (2012) · Biochemistry · doi:10.1021/bi300368b · Cited by 53
Initial Response of the Potassium Channel Voltage Sensor to a Transmembrane Potential
Treptow, W. L., Tarek, M., & Klein, M. L. (2009) · Journal of the American Chemical Society · doi:10.1021/ja807330g · Cited by 51
Self-citationMolecular basis of voltage gating of OmpF porin
Robertson, K. M., & Tieleman, D. P. (2002) · Biochemistry and Cell Biology · doi:10.1139/o02-145 · Cited by 50
Aggregation of amyloids in a cellular context: modelling and experiment
Friedman, R. (2011) · Biochemical Journal · doi:10.1042/bj20110369 · Cited by 50
Self-citationProbabilistic Local Features in Uncertain Vector Fields with Spatial Correlation
Petz, C., Pöthkow, K., & Hege, H. (2012) · Computer Graphics Forum · doi:10.1111/j.1467-8659.2012.03097.x · Cited by 50
Self-citationInsights into Aβ Aggregation: A Molecular Dynamics Perspective
Shea, J., & Urbanc, B. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611212220012 · Cited by 50
Two pools of cholesterol in acetylcholine receptor-rich membranes from Torpedo
Leibel, W. S., Firestone, L. L., Legler, D. C., Braswell, L. M., & Miller, K. W. (1987) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(87)90421-4 · Cited by 48
Dynamics of SecY Translocons with Translocation-Defective Mutations
Bondar, A., del Val, C., Freites, J. A., Tobias, D. J., & White, S. H. (2010) · Structure · doi:10.1016/j.str.2010.04.010 · Cited by 48
Self-citationGkeka, P., Eleftheratos, S., Kolocouris, A., & Cournia, Z. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300899n · Cited by 48
Self-citationVoltage-gated ion channel modulation by lipids: Insights from molecular dynamics simulations
Kasimova, M. A., Tarek, M., Shaytan, A. К., Шайтан, К. В., & Delemotte, L. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.01.024 · Cited by 47
Self-citationInteractive Rendering of Materials and Biological Structures on Atomic and Nanoscopic Scale
Lindow, N., Baum, D., & Hege, H. (2012) · Computer Graphics Forum · doi:10.1111/j.1467-8659.2012.03128.x · Cited by 46
Self-citationHelix Self-Assembly from Anisotropic Molecules
Fejer, S. N., & Wales, D. J. (2007) · Physical Review Letters · doi:10.1103/physrevlett.99.086106 · Cited by 45
Self-citationForce distributions in a triangular lattice of rigid bars
Tighe, B. P., Socolar, J. E. S., Schaeffer, D. G., Mitchener, W. G., & Huber, M. (2005) · Physical Review E · doi:10.1103/physreve.72.031306 · Cited by 45
Dual Effect of Phosphatidyl (4,5)-Bisphosphate PIP2 on Shaker K+ Channels
Abderemane-Ali, F., Es‐Salah‐Lamoureux, Z., Delemotte, L., Kasimova, M. A., Labro, A. J., Snyders, D. J., Fedida, D., Tarek, M., Baró, I., & Loussouarn, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.382085 · Cited by 43
Self-citationKrasilnikov, O. V., Merzlyak, P. G., Yuldasheva, L. N., Rodrigues, C. G., Bhakdi, S., & Valeva, A. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02080.x · Cited by 43
Membrane fusion and vesicular transformation induced by Alzheimer's amyloid beta
Vestergaard, M. C. M., Morita, M., Hamada, T., & Takagi, M. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.01.015 · Cited by 43
Arias, H. R., Sankaram, M. B., Marsh, D., & Barrantes, F. J. (1990) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(90)90320-n · Cited by 42
Atomistic Visualization of Mesoscopic Whole‐Cell Simulations Using Ray‐Casted Instancing
Falk, M., Krone, M., & Ertl, T. (2013) · Computer Graphics Forum · doi:10.1111/cgf.12197 · Cited by 42
Sooksawate, T., & Simmonds, M. A. (1998) · Neuropharmacology · doi:10.1016/s0028-3908(98)00113-0 · Cited by 41
Perspectives on: Ion selectivity
Andersen, O. S. (2011) · The Journal of General Physiology · doi:10.1085/jgp.201110651 · Cited by 40
Baggett, A. W., Cournia, Z., Han, M. S., Patargias, G., Glass, A. C., Liu, S., & Nolen, B. J. (2012) · ChemMedChem · doi:10.1002/cmdc.201200104 · Cited by 40
Self-citationFree Energy Calculations on the Two Drug Binding Sites in the M2 Proton Channel
Gu, R., Liu, L. A., Wei, D., Du, J., Liu, H., & Liu, H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1114198 · Cited by 40
Growth of β2-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH
Hasegawa, K., Tsutsumi, S., Ookoshi, T., Ohhashi, Y., Kimura, H., Takahashi, N., Yoshida, H., Miyazaki, R., Goto, Y., & Naiki, H. (2008) · Biochemical Journal · doi:10.1042/bj20080543 · Cited by 39
Bristow, D. R., & Martin, I. L. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb01004.x · Cited by 38
Critical Scaling and Aging in Cooling Systems Near the Jamming Transition
Head, D. A. (2009) · Physical Review Letters · doi:10.1103/physrevlett.102.138001 · Cited by 38
Mereuta, L., Schiopu, I., Asandei, A., Park, Y., Hahm, K., & Luchian, T. (2012) · Langmuir · doi:10.1021/la303782d · Cited by 38
Bruno, A., Costantino, G., Fabritiis, G. D., Pastor, M., & Selent, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042023 · Cited by 37
Self-citationBinding Hot Spots and Amantadine Orientation in the Influenza A Virus M2 Proton Channel
Chuang, G., Kozakov, D., Brenke, R., Beglov, D., Guarnieri, F., & Vajda, S. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.09.004 · Cited by 37
Exploring cavity dynamics in biomolecular systems
Lindow, N., Baum, D., Bondar, A., & Hege, H. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-s19-s5 · Cited by 36
Self-citationDomain Swapping in the Cytoplasmic Domain of the Escherichia coli Rhomboid Protease
Lazareno-Saez, C., Arutyunova, E. I., Coquelle, N., & Lemieux, M. J. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.01.019 · Cited by 35
Self-citationCoupling of Retinal, Protein, and Water Dynamics in Squid Rhodopsin
Jardón‐Valadez, E., Bondar, A., & Tobias, D. J. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.067 · Cited by 34
Self-citationMembrane Simulations of OpcA: Gating in the Loops?
Bond, P. J., Derrick, J. P., & Sansom, M. S. P. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.097311 · Cited by 34
Effect of salt bridges on the energy landscape of a model protein
Wales, D. J., & Dewsbury, P. E. J. (2004) · The Journal of Chemical Physics · doi:10.1063/1.1810471 · Cited by 33
Self-citationDelemotte, L., Klein, M. L., & Tarek, M. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00097 · Cited by 33
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Rheingans, P. L., & Joshi, S. (1999) · Eurographics · doi:10.1007/978-3-7091-6803-5_30 · Cited by 32
Insights into Substrate Gating in H. influenzae Rhomboid
Brooks, C. L., Lazareno-Saez, C., Lamoureux, J. S., Mak, M. W., & Lemieux, M. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.046 · Cited by 32
Self-citationHalothane-induced changes in acetylcholine receptor channel kinetics are attenuated by cholesterol
Lechleiter, J. D., Wells, M. A., & Gruener, R. (1986) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(86)90159-8 · Cited by 31
Molecular Modeling and Simulation of Membrane Lipid-Mediated Effects on GPCRs
Sadiq, S. K., Guixà-González, R., Dainese, E., Pastor, M., Fabritiis, G. D., & Selent, J. (2012) · Current Medicinal Chemistry · doi:10.2174/0929867311320010004 · Cited by 31
Self-citationAsandei, A., Apetrei, A., Park, Y., Hahm, K., & Luchian, T. (2010) · Langmuir · doi:10.1021/la104264f · Cited by 30
Modeling and simulations of a bacterial outer membrane protein: OprF from Pseudomonas aeruginosa
Khalid, S., Bond, P. J., Deol, S. S., & Sansom, M. S. P. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20845 · Cited by 29
Self-citationTuning voltage-gated channel activity and cellular excitability with a sphingomyelinase
Combs, D. J., Shin, H.-G., Xu, Y., Ramu, Y., & Lü, Z. (2013) · The Journal of General Physiology · doi:10.1085/jgp.201310986 · Cited by 29
Functional reconstitution of the bovine brain GABAA receptor from solubilized components
Dunn, S. M. J., Martin, C. R., Agey, M. W., & Miyazaki, R. (1989) · Biochemistry · doi:10.1021/bi00432a030 · Cited by 28
Dynamic channels in biomolecular systems: Path analysis and visualization
Lindow, N., Baum, D., Bondar, A., & Hege, H. (2012) · IEEE Symposium on Biological Data Visualization (BioVis) · doi:10.1109/biovis.2012.6378599 · Cited by 28
Self-citationSurfactant Effects on Amyloid Aggregation Kinetics
Friedman, R., & Caflisch, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.10.011 · Cited by 27
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Lee, J. Y., & Lyman, E. R. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.2967 · Cited by 27
Oligomeric state study of prokaryotic rhomboid proteases
Sampathkumar, P., Mak, M. W., Witholt, S. J., Guigard, E., Kay, C. M., & Lemieux, M. J. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.08.004 · Cited by 26
Self-citationZhao, C., Caplan, D. A., & Noskov, S. Y. (2010) · Journal of Chemical Theory and Computation · doi:10.1021/ct9006597 · Cited by 26
Holdbrook, D. A., Piggot, T. J., Sansom, M. S. P., & Khalid, S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.09.002 · Cited by 26
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Krone, M., Reina, G., Schulz, C., Kulschewski, T., Pleiss, J., & Ertl, T. (2013) · Computer Graphics Forum · doi:10.1111/cgf.12120 · Cited by 25
Khemtémourian, L., Casarramona, G. L., Suylen, D. P. L., Hackeng, T. M., Meeldijk, J. D., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2009) · Biochemistry · doi:10.1021/bi901076d · Cited by 24
Tarek, M., & Delemotte, L. (2013) · Accounts of Chemical Research · doi:10.1021/ar300290u · Cited by 22
Self-citationForman, C. J., Nickson, A. A., Anthony‐Cahill, S. J., Baldwin, A. J., Kaggwa, G. B., Feber, U., Sheikh, K. H., Jarvis, S., & Barker, P. D. (2012) · ACS Nano · doi:10.1021/nn204140a · Cited by 22
Embedding Aβ42 in Heterogeneous Membranes Depends on Cholesterol Asymmetries
Liguori, N., Nerenberg, P. S., & Head-Gordon, T. L. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.06.046 · Cited by 20
Visualizing dynamic molecular conformations
Schmidt-Ehrenberg, J., Baum, D., & Hege, H. (2003) · doi:10.1109/visual.2002.1183780 · Cited by 20
Self-citationThe Role of Lipids in the Function of the Acetylcholine Receptor
Zabrecky, J. R., & Raftery, M. A. (1985) · Journal of Receptor Research · doi:10.3109/10799898509041890 · Cited by 19
Inhibition of peptide aggregation by lipids: Insights from coarse-grained molecular simulations
Hung, A., & Yarovsky, I. (2010) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2010.11.001 · Cited by 19
Friedman, R., Pellarin, R., & Caflisch, A. (2009) · The Journal of Physical Chemistry Letters · doi:10.1021/jz900318t · Cited by 18
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Goddard, A. D., Dijkman, P. M., Adamson, R. J., & Watts, A. (2013) · Methods in cell biology · doi:10.1016/b978-0-12-408143-7.00018-9 · Cited by 17
Channelrhodopsins: A bioinformatics perspective
del Val, C., Royuela-Flor, J., Milenkovic, S., & Bondar, A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.11.005 · Cited by 15
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Forman, C. J., Fejer, S. N., Chakrabarti, D., Barker, P. D., & Wales, D. J. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp4040503 · Cited by 15
Self-citationBáez-Pagán, C. A., Martinez, Y., Otero-Cruz, J. D., Salgado, I. K., Velazquez, G., Ortiz‐Acevedo, A., Quesada, O., Silva, W. I., & Lasalde‐Dominicci, J. A. (2008) · Channels · doi:10.4161/chan.2.3.6155 · Cited by 13
Visual Analysis of Dynamic Protein Cavities and Binding Sites
Krone, M., Kauker, D., Reina, G., & Ertl, T. (2014) · IEEE Pacific Visualization Symposium · doi:10.1109/pacificvis.2014.32 · Cited by 12
The importance of solvation in the design of ligands targeting membrane proteins
González, Á., Murcia, M., Benhamú, B., Campillo, M., López-Rodríguez, M. L., & Pardo, L. (2011) · MedChemComm · doi:10.1039/c0md00258e · Cited by 11
Similarities between protein folding and granular jamming
Jose, P. P., & Andricioaei, I. (2012) · Nature Communications · doi:10.1038/ncomms2177 · Cited by 10
Self-citationFibril elongation mechanisms of HET‐s prion‐forming domain: Topological evidence for growth polarity
Baiesi, M., Seno, F., & Trovato, A. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23133 · Cited by 8
Coarse-Grained Models for Protein Folding and Aggregation
Derreumaux, P. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-017-5_22 · Cited by 7
Friedman, R., & Caflisch, A. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24402 · Cited by 5
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Schmidt-Ehrenberg, J. (2008) · Cited by 2
Flagged first, then by citations
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Research works printed but not linked: 1
- Wales D (2003) Energy landscapes. Cambridge University Press, Cambridge
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Sampling alternative conformational states of transporters and receptors with AlphaFold2
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“Dynamic interconversion between multiple conformations underpins the functions of integral membrane proteins in all domains of life ( Campbell et al., 2016 ; Cournia et al., 2015 ; Shaw et al., 2010 ; Boehr et al., 2009 ).”
BackgroundUbiquitination and the Regulation of Membrane Proteins
Foot, N. J., Henshall, T. L., & Kumar, S. (2016) · Physiological Reviews · doi:10.1152/physrev.00012.2016 · Cited by 272
Mori, T., Miyashita, N., Im, W., Feig, M., & Sugita, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.12.032 · Cited by 150
Dynamic Nuclear Polarization for Sensitivity Enhancement in Biomolecular Solid-State NMR
Biedenbänder, T., Aladin, V., Saeidpour, S., & Corzilius, B. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00776 · Cited by 141
DPPC-cholesterol phase diagram using coarse-grained Molecular Dynamics simulations
Wang, Y., Gkeka, P., Fuchs, J. E., Liedl, K. R., & Cournia, Z. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.08.005 · Cited by 138
Self-citation
Metadata
- Authors
- Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., Friedman, R., Gkeka, P., Hege, H.-C., Hénin, J., Kasimova, M. A., Kolocouris, A., Klein, M. L., Khalid, S., Lemieux, M. J., Lindow, N., Roy, M., Selent, J., Tarek, M., Tofoleanu, F., Vanni, S., Urban, S., Wales, D. J., Smith, J. C., & Bondar, A.-N.
- Affiliations
- Academy of Athens (GR)
- RMIT University (AU)
- University of California, Irvine (US)
- Centre National de la Recherche Scientifique (FR)
- Zuse Institute Berlin (DE)
- Rutgers, The State University of New Jersey (US)
- University College Dublin (IE)
- Temple University (US)
- Linnaeus University (SE)
- Lomonosov Moscow State University (RU)
- National and Kapodistrian University of Athens (GR)
- University of Southampton (GB)
- University of Alberta (CA)
- Universitat Pompeu Fabra (ES)
- University of Cambridge (GB)
- Oak Ridge National Laboratory (US)
- Freie Universität Berlin (DE)
- Corresponding author
- Cournia, Zoe
- Smith, Jeremy C.
- Bondar, Ana-Nicoleta
- ORCID
- Cournia, Zoe
- Allen, Toby W.
- Andricioaei, Ioan
- Antonny, Bruno
- Baum, Daniel
- Brannigan, Grace
- Buchete, Nicolae-Viorel
- Delemotte, Lucie
- Friedman, Ran
- Gkeka, Paraskevi
- Hege, Hans-Christian
- Hénin, Jérôme
- Kasimova, Marina A.
- Kolocouris, Antonios
- Klein, Michael L.
- Khalid, Syma
- Lemieux, M. Joanne
- Lindow, Norbert
- Selent, Jana
- Tarek, Mounir
- Tofoleanu, Florentina
- Vanni, Stefano
- Wales, David J.
- Smith, Jeremy C.
- Bondar, Ana-Nicoleta
- Venue
- The Journal of Membrane Biology
- Published
- 2015-06-11
- Volume
- 248
- Issue
- 4
- Pages
- 611-640
- ISSN
- 0022-2631 (ISSN-L)
- 1432-1424
- PMC
- PMC4515176
- OpenAlex
- W2103496068
- Cited by
- 235
- References
- 282
- Citations by year
- 2026: 11 · 2025: 23 · 2024: 36 · 2023: 37 · 2022: 18 · 2021: 28 · 2020: 27 · 2019: 15 · 2018: 18 · 2017: 12 · 2016: 10
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- The Journal of Membrane Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RECERCAT (Consorci de Serveis Universitaris de Catalunya) (acceptedVersion, other-oa)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- HAL (submittedVersion, public-domain)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Figshare (submittedVersion)
- Repositori digital de la UPF (Universitat Pompeu Fabra) (submittedVersion)
- Funders
- National Science Foundation (1052477, RC2GM093307, 0840513)
- National Institutes of Health
- University of California, Irvine
- Australian Research Council (DP120103548)
- European Regional Development Fund
- National Cancer Institute (2010-1)
- National Institute of General Medical Sciences (P01GM55876-14A1, P01GM055876, RC2GM093307)
- Division of Chemistry (CHE-0840513)
- FP7 Ideas: European Research Council (268888)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- membrane proteins, membrane protein structure, membrane protein dynamics, membrane protein function, membrane transporters, cell surface receptors, protein-lipid interactions, computational biophysics
- MeSH terms
- Animals, Humans, Models, Biological, Models, Chemical, Structure-Activity Relationship, Protein Structure, Tertiary, Membrane Transport Proteins
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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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