Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory

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

THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method

Kumar, S., Rosenberg, J. M., Bouzida, D., Swendsen, R. H., & Kollman, P. A. (1992) · Journal of Computational Chemistry · doi:10.1002/jcc.540130812 · Cited by 6,808

The MARTINI Force Field: Coarse Grained Model for Biomolecular Simulations

Marrink, ‪. J., Risselada, H. J., Yefimov, S., Tieleman, D. P., & de Vries, A. H. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071097f · Cited by 5,641

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Global Optimization by Basin-Hopping and the Lowest Energy Structures of Lennard-Jones Clusters Containing up to 110 Atoms

Wales, D. J., & Doye, J. P. K. (1997) · The Journal of Physical Chemistry A · doi:10.1021/jp970984n · Cited by 3,030

High‐Temperature Equation of State by a Perturbation Method. I. Nonpolar Gases

Zwanzig, R. (1954) · The Journal of Chemical Physics · doi:10.1063/1.1740409 · Cited by 2,923

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

Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel

Long, S. B., Campbell, E. B., & MacKinnon, R. (2005) · Science · doi:10.1126/science.1116269 · Cited by 2,159

Solid-state nanopores

Dekker, C. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.27 · Cited by 1,940

Aβ Oligomers – a decade of discovery

Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938

The calculation of the potential of mean force using computer simulations

Roux, B. (1995) · Computer Physics Communications · doi:10.1016/0010-4655(95)00053-i · Cited by 1,755

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

Refined Structure of the Nicotinic Acetylcholine Receptor at 4Å Resolution

Unwin, P. N. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.031 · Cited by 1,677

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559

The crystal structure of a voltage-gated sodium channel

Payandeh, J., Scheuer, T., Zheng, N., & Catterall, W. A. (2011) · Nature · doi:10.1038/nature10238 · Cited by 1,453

Simulation of activation free energies in molecular systems

Neria, E., Fischer, S., & Karplus, M. (1996) · The Journal of Chemical Physics · doi:10.1063/1.472061 · Cited by 1,325

X-ray structure of a protein-conducting channel

van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,236

Neurosteroids: endogenous regulators of the GABAA receptor

Belelli, D., & Lambert, J. J. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1703 · Cited by 1,159

Principles of activation and permeation in an anion-selective Cys-loop receptor

Hibbs, R. E., & Gouaux, E. (2011) · Nature · doi:10.1038/nature10139 · Cited by 1,016

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.

Rapoport, T. A. (2007) · Nature · doi:10.1038/nature06384 · Cited by 977

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

Liu, W., Chun, E., Thompson, A. A., Chubukov, P., Xu, F., Katritch, V., Han, G. W., Roth, C., Heitman, L. H., IJzerman, A. P., et al. (2012) · Science · doi:10.1126/science.1219218 · Cited by 952

A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

Hanson, M. A., Cherezov, V., Griffith, M. T., Roth, C., Jaakola, V., Chien, E. Y. T., Velasquez, J., Kühn, P., & Stevens, R. C. (2008) · Structure · doi:10.1016/j.str.2008.05.001 · Cited by 935

Cholesterol and the Golgi Apparatus

Bretscher, M. S., & Munro, S. (1993) · Science · doi:10.1126/science.8362242 · Cited by 821

Endogenous neurosteroids regulate GABAA receptors through two discrete transmembrane sites

Hosie, A. M., Wilkins, M. E., da Silva, H. M. A., & Smart, T. G. (2006) · Nature · doi:10.1038/nature05324 · Cited by 752

G protein-coupled receptors: novel targets for drug discovery in cancer

Lappano, R., & Maggiolini, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3320 · Cited by 742

Imaging α-Hemolysin with Molecular Dynamics: Ionic Conductance, Osmotic Permeability, and the Electrostatic Potential Map

Aksimentiev, A., & Schulten, K. J. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.058727 · Cited by 692

X-ray structure of a prokaryotic pentameric ligand-gated ion channel

Hilf, R. J. C., & Dutzler, R. (2008) · Nature · doi:10.1038/nature06717 · Cited by 665

Structural basis for the function and inhibition of an influenza virus proton channel

Stouffer, A. L., Acharya, R., Salom, D., Levine, A. S., Costanzo, L. D., Soto, C. S., Tereshko, V. A., Nanda, V., Stayrook, S. E., & DeGrado, W. F. (2008) · Nature · doi:10.1038/nature06528 · Cited by 646

PIP 2 Is a Necessary Cofactor for Ion Channel Function: How and Why?

Suh, B.-C., & Hille, B. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125859 · Cited by 646

Protein Translocation Across the Bacterial Cytoplasmic Membrane

Driessen, A. J. M., & Nouwen, N. P. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.160747 · Cited by 635

Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2

Hansen, S. B., Tao, X., & MacKinnon, R. (2011) · Nature · doi:10.1038/nature10370 · Cited by 632

Crystal structure of a heterotetrameric NMDA receptor ion channel

Karakaş, E., & Furukawa, H. (2014) · Science · doi:10.1126/science.1251915 · Cited by 623

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Cady, S. D., Schmidt‐Rohr, K., Wang, J., Soto, C. S., DeGrado, W. F., & Hong, M. (2010) · Nature · doi:10.1038/nature08722 · Cited by 619

Mechanism of Voltage Gating in Potassium Channels

Jensen, M. Ø., Jogini, V., Borhani, D. W., Leffler, A. E., Dror, R. O., & Shaw, D. E. (2012) · Science · doi:10.1126/science.1216533 · Cited by 606

Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands

Noskov, S. Y., Bernèche, S., & Roux, B. (2004) · Nature · doi:10.1038/nature02943 · Cited by 598

Curvature, Lipid Packing, and Electrostatics of Membrane Organelles: Defining Cellular Territories in Determining Specificity

Bigay, J., & Antonny, B. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.10.009 · Cited by 588

Globular amyloid β‐peptide 1−42 oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559

Statistical Mechanical Theory of Transport Processes. VII. The Coefficient of Thermal Conductivity of Monatomic Liquids

Zwanzig, R. W., Kirkwood, J. G., Oppenheim, I., & Alder, B. J. (1954) · The Journal of Chemical Physics · doi:10.1063/1.1740193 · Cited by 553

Crystal structure of the channelrhodopsin light-gated cation channel

KATO, H. E., Zhang, F., Yizhar, O., Ramakrishnan, C., Nishizawa, T., Hirata, K., Ito, J., Aita, Y., Tsukazaki, T., Hayashi, S., et al. (2012) · Nature · doi:10.1038/nature10870 · Cited by 543

Negative Conductance Caused by Entry of Sodium and Cesium Ions into the Potassium Channels of Squid Axons

Bezanilla, F., & Armstrong, C. M. (1972) · The Journal of General Physiology · doi:10.1085/jgp.60.5.588 · Cited by 542

Crystal structure of a voltage-gated sodium channel in two potentially inactivated states

Payandeh, J., El-Din, T. M. G., Scheuer, T., Zheng, N., & Catterall, W. A. (2012) · Nature · doi:10.1038/nature11077 · Cited by 488

Structural mechanism of C-type inactivation in K+ channels

Cuello, L. G., Jogini, V., Cortés, D. M., & Perozo, E. (2010) · Nature · doi:10.1038/nature09153 · Cited by 486

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

Gonzales, E. B., Kawate, T., & Gouaux, E. (2009) · Nature · doi:10.1038/nature08218 · Cited by 472

The molecular basis of electroporation

Tieleman, D. P. (2004) · BMC Biochemistry · doi:10.1186/1471-2091-5-10 · Cited by 460

Structure of a complex of the ATPase SecA and the protein-translocation channel.

Zimmer, J., Nam, Y., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07335 · Cited by 459

Crystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and Sodium

Whorton, M. R., & MacKinnon, R. (2011) · Cell · doi:10.1016/j.cell.2011.07.046 · Cited by 451

A partially folded structure of amyloid-beta(1–40) in an aqueous environment

Vivekanandan, S., Brender, J., Lee, S. Y., & Ramamoorthy, A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.06.133 · Cited by 439

Critical Scaling of Shear Viscosity at the Jamming Transition

Olsson, P., & Teitel, S. (2007) · Physical Review Letters · doi:10.1103/physrevlett.99.178001 · Cited by 430

Crystal Structure of the Human K2P TRAAK, a Lipid- and Mechano-Sensitive K + Ion Channel

Brohawn, S. G., del Mármol, J. I., & MacKinnon, R. (2012) · Science · doi:10.1126/science.1213808 · Cited by 422

Modulation of rhodopsin function by properties of the membrane bilayer

Brown, M. F. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90180-5 · Cited by 422

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

Discrete path sampling

Wales, D. J. (2002) · Molecular Physics · doi:10.1080/00268970210162691 · Cited by 399

Crystal structure of a rhomboid family intramembrane protease

Wang, Y., Zhang, Y., & Ha, Y. (2006) · Nature · doi:10.1038/nature05255 · Cited by 368

Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore

Movileanu, L., Howorka, S., Braha, O., & Bayley, H. (2000) · Nature Biotechnology · doi:10.1038/80295 · Cited by 366

Virtual Screening in Drug Discovery - A Computational Perspective

Reddy, A. S., Pati, S. P., Kumar, P. P., Pradeep, H., & Sastry, G. N. (2007) · Current Protein and Peptide Science · doi:10.2174/138920307781369427 · Cited by 350

Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide.

Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., & Butler, P. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7283 · Cited by 343

Ion Channels as Therapeutic Targets: A Drug Discovery Perspective

Bagal, S. K., Brown, A. D., Cox, P. J., Omoto, K., Owen, R. M., Pryde, D. C., Sidders, B. S., Skerratt, S. E., Stevens, E. B., Storer, R. I., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3011433 · Cited by 320

Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice

Martins, I. C., Kuperstein, I., Wilkinson, H. R., Maes, E., Vanbrabant, M., Jonckheere, W., Gelder, P. V., Hartmann, D., D’Hooge, R., Strooper, B. D., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601953 · Cited by 318

Unfolding of Proteins and Long Transient Conformations Detected by Single Nanopore Recording

Oukhaled, A., Mathé, J., Biance, A., Bacri, L., Betton, J., Lairez, D., Pelta, J., & Auvray, L. (2007) · Physical Review Letters · doi:10.1103/physrevlett.98.158101 · Cited by 315

Phosphoinositides regulate ion channels

Hille, B., Dickson, E. J., Kruse, M., Vivas, O., & Suh, B.-C. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.09.010 · Cited by 312

A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

Vanni, S., Hirose, H., Barelli, H., Antonny, B., & Gautier, R. (2014) · Nature Communications · doi:10.1038/ncomms5916 · Cited by 309

Regulation of receptor function by cholesterol

Bürger, K., Gimpl, G., & Fahrenholz, F. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000643 · Cited by 302

A role for direct interactions in the modulation of rhodopsin by ω-3 polyunsaturated lipids

Grossfield, A. M., Feller, S. E., & Pitman, M. C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508352103 · Cited by 298

Lipids as Modulators of Proteolytic Activity of BACE

Kalvodova, L., Kahya, N., Schwille, P., Ehehalt, R., Verkade, P., Drechsel, D. N., & Simons, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504484200 · Cited by 297

Jamming of frictional spheres and random loose packing

Silbert, L. E. (2010) · Soft Matter · doi:10.1039/c001973a · Cited by 293

Anomalous dynamics of forced translocation

Kantor, Y., & Mehran Kardar, A. (2004) · Physical Review E · doi:10.1103/physreve.69.021806 · Cited by 287

Discrete Ba2+ block as a probe of ion occupancy and pore structure in the high-conductance Ca2+ -activated K+ channel.

Neyton, J., & Miller, C. (1988) · The Journal of General Physiology · doi:10.1085/jgp.92.5.569 · Cited by 283

Interpreting the Aggregation Kinetics of Amyloid Peptides

Pellarin, R., & Caflisch, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.033 · Cited by 259

Effective energy function for proteins in lipid membranes

Lazaridis, T. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10410 · Cited by 251

Uncovering the intimate relationship between lipids, cholesterol and GPCR activation

Oates, J., & Watts, A. G. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.09.007 · Cited by 247

Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry

Wu, Z., Yan, N., Feng, L., Oberstein, A., Yan, H., Baker, R. P., Gu, L., Jeffrey, P. D., Urban, S., & Shi, Y. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1179 · Cited by 245

Electroporation of the E. coli and S. Aureus Membranes: Molecular Dynamics Simulations of Complex Bacterial Membranes

Piggot, T. J., Holdbrook, D. A., & Khalid, S. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp207013v · Cited by 243

Potential Energy and Free Energy Landscapes

Wales, D. J., & Bogdan, T. V. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp0680544 · Cited by 242

Dynamics of Unfolded Protein Transport through an Aerolysin Pore

Pastoriza‐Gallego, M., Rabah, L., Gibrat, G., Thiébot, B., van der Goot, F. G., Auvray, L., Betton, J., & Pelta, J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1073245 · Cited by 240

Structure of the transmembrane region of the M2 protein H+ channel

Wang, J., Kim, S., Kovacs, F., & Cross, T. A. (2001) · Protein Science · doi:10.1110/ps.17901 · Cited by 234

Neurosteroid binding sites on GABAA receptors

Hosie, A. M., Wilkins, M. E., & Smart, T. G. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.03.011 · Cited by 224

Conformational transition of Sec machinery inferred from bacterial SecYE structures

Tsukazaki, T., Mori, H., Fukai, S., Ishitani, R., Mori, T., Dohmae, N., Perederina, A. A., Sugita, Y., Vassylyev, D. G., Ito, K., et al. (2008) · Nature · doi:10.1038/nature07421 · Cited by 219

Amphipathic Lipid Packing Sensor Motifs: Probing Bilayer Defects with Hydrophobic Residues

Vanni, S., Vamparys, L., Gautier, R., Drin, G., Etchebest, C., Fuchs, P., & Antonny, B. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.3837 · Cited by 206

How Translocons Select Transmembrane Helices

White, S. H., & von HEIJNE, G. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125904 · Cited by 204

Molecular Dynamics Simulations of Phosphatidylcholine Membranes: A Comparative Force Field Study

Piggot, T. J., Piñeiro, Á., & Khalid, S. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct3003157 · Cited by 195

Influence of the membrane potential on the free energy of an intrinsic protein

Roux, B. T. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78327-9 · Cited by 190

Membrane Insertion of a Potassium-Channel Voltage Sensor

Hessa, T., White, S. H., & von HEIJNE, G. (2005) · Science · doi:10.1126/science.1109176 · Cited by 188

Conical Lipids in Flat Bilayers Induce Packing Defects Similar to that Induced by Positive Curvature

Vamparys, L., Gautier, R., Vanni, S., Bennett, W. F., Tieleman, D. P., Antonny, B., Etchebest, C., & Fuchs, P. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.3836 · Cited by 188

Molecular Dynamics Simulations of Lipid Membrane Electroporation

Delemotte, L., & Tarek, M. (2012) · The Journal of Membrane Biology · doi:10.1007/s00232-012-9434-6 · Cited by 188

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

Energy landscapes: calculating pathways and rates

Wales, D. J. (2006) · International Reviews in Physical Chemistry · doi:10.1080/01442350600676921 · Cited by 186

Immobilized lipid in acetylcholine receptor-rich membranes from Torpedo marmorata.

Marsh, D., & Barrantes, F. J. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.9.4329 · Cited by 186

Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity

Urban, S., & Wolfe, M. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408306102 · Cited by 185

Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field

Freedman, K. J., Haq, S. R., Edel, J. B., Jemth, P., & Kim, M. J. (2013) · Scientific Reports · doi:10.1038/srep01638 · Cited by 184

Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes

Egea, P. F., & Stroud, R. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012556107 · Cited by 183

Deciphering ionic current signatures of DNA transport through a nanopore

Aksimentiev, A. (2010) · Nanoscale · doi:10.1039/b9nr00275h · Cited by 182

Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channels

Xu, Y., Ramu, Y., & Lü, Z. (2008) · Nature · doi:10.1038/nature06618 · Cited by 181

Mechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA pore

Thompson, A. N., Kim, I., Panosian, T. D., Iverson, T. M., Allen, T. W., & Nimigean, C. M. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1703 · Cited by 181

Structural basis for intramembrane proteolysis by rhomboid serine proteases

Shem, A. B., Fass, D., & Bibi, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609773104 · Cited by 176

Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations

Delemotte, L., Tarek, M., Klein, M. L., Amaral, C., & Treptow, W. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102724108 · Cited by 176

Thermodynamics and Kinetics of Aggregation for the GNNQQNY Peptide

Strodel, B., Whittleston, C. S., & Wales, D. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja075346p · Cited by 176

The energy landscape as a unifying theme in molecular science

Wales, D. J. (2004) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2004.1497 · Cited by 176

Structural basis for lipid modulation of nicotinic acetylcholine receptor function

Barrantes, F. J. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.06.008 · Cited by 175

Reduced Lateral Mobility of Lipids and Proteins in Crowded Membranes

Goose, J. E., & Sansom, M. S. P. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003033 · Cited by 169

Molecular Dynamics and NMR Spectroscopy Studies of E. coli Lipopolysaccharide Structure and Dynamics

Wu, E. L., Engström, O., Jo, S., Stuhlsatz, D., Yeom, M. S., Klauda, J. B., Widmalm, G., & Im, W. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.08.002 · Cited by 168

Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation.

Criado, M., Eibl, H., & Barrantes, F. J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)47283-8 · Cited by 165

Embedded cholesterol in the nicotinic acetylcholine receptor

Brannigan, G. H., Hénin, J., Law, R., Eckenhoff, R. G., & Klein, M. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803029105 · Cited by 165

Cytochrome Display on Amyloid Fibrils

Baldwin, A. J., Bader, R., Christodoulou, J., MacPhee, C. E., Dobson, C. M., & Barker, P. D. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0565673 · Cited by 163

On the Importance of Atomic Fluctuations, Protein Flexibility, and Solvent in Ion Permeation

Allen, T. W., Andersen, O. S., & Roux, B. (2004) · The Journal of General Physiology · doi:10.1085/jgp.200409111 · Cited by 162

Energy landscapes: some new horizons

Wales, D. J. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.12.011 · Cited by 159

Jamming Transition as Probed by Quasistatic Shear Flow

Heussinger, C., & Barrat, J. (2009) · Physical Review Letters · doi:10.1103/physrevlett.102.218303 · Cited by 157

Transmembrane Structures for Alzheimer’s Aβ 1−42 Oligomers

Strodel, B., Lee, J. W. L., Whittleston, C. S., & Wales, D. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103725c · Cited by 155

Effects of membrane cholesterol on the sensitivity of the GABAA receptor to GABA in acutely dissociated rat hippocampal neurones

Sooksawate, T., & Simmonds, M. A. (2001) · Neuropharmacology · doi:10.1016/s0028-3908(00)00159-3 · Cited by 153

Thermal Unfolding of Proteins Probed at the Single Molecule Level Using Nanopores

Payet, L., Martinho, M., Pastoriza‐Gallego, M., Betton, J., Auvray, L., Pelta, J., & Mathé, J. (2012) · Analytical Chemistry · doi:10.1021/ac300129e · Cited by 153

E. coli Outer Membrane and Interactions with OmpLA

Wu, E. L., Fleming, P. J., Yeom, M. S., Widmalm, G., Klauda, J. B., Fleming, K. G., & Im, W. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.04.024 · Cited by 153

The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis

Lemieux, M. J., Fischer, S. J., Cherney, M. M., Bateman, K. S., & James, M. N. G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609981104 · Cited by 147

Enzymatic activation of voltage-gated potassium channels

Ramu, Y., Xu, Y., & Lü, Z. (2006) · Nature · doi:10.1038/nature04880 · Cited by 143

Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate

Baker, R. P., Young, K. E., Feng, L., Shi, Y., & Urban, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700814104 · Cited by 142

Jamming, Yielding, and Rheology of Weakly Vibrated Granular Media

Dijksman, J. A., Wortel, G. H., van Dellen, L. T. H., Dauchot, O., & van Hecke, M. (2011) · Physical Review Letters · doi:10.1103/physrevlett.107.108303 · Cited by 138

The Alzheimer β‐peptide shows temperature‐dependent transitions between left‐handed 31‐helix, β‐strand and random coil secondary structures

Danielsson, J., Jarvet, J., Damberg, P., & Gräslund, A. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04812.x · Cited by 136

Amyloid Aggregation on Lipid Bilayers and Its Impact on Membrane Permeability

Friedman, R., Pellarin, R., & Caflisch, A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.036 · Cited by 135

Role of Cholesterol and Polyunsaturated Chains in Lipid−Protein Interactions: Molecular Dynamics Simulation of Rhodopsin in a Realistic Membrane Environment

Pitman, M. C., Grossfield, A. M., Suits, F., & Feller, S. E. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042715y · Cited by 133

Computational models for the prediction of polypeptide aggregation propensity

Caflisch, A. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.07.009 · Cited by 130

Membrane permeabilization by Islet Amyloid Polypeptide

Engel, M. F. M. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2009.03.008 · Cited by 129

Computational approaches to molecular recognition

Lamb, M. L., & Jorgensen, W. L. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80038-5 · Cited by 127

Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition

Ochoa, E. L. M., Dalziel, A. W., & McNamee, M. G. (1983) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(83)90379-6 · Cited by 127

Structure and Dynamics of Parallel β-Sheets, Hydrophobic Core, and Loops in Alzheimer’s Aβ Fibrils

Buchete, N., & Hummer, G. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.100404 · Cited by 127

Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation

Mereuta, L., Roy, M., Asandei, A., Lee, J. K., Park, Y., Andricioaei, I., & Luchian, T. (2014) · Scientific Reports · doi:10.1038/srep03885 · Cited by 126

Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity

Dickey, S. W., Baker, R. P., Cho, S., & Urban, S. (2013) · Cell · doi:10.1016/j.cell.2013.10.053 · Cited by 124

X-ray structures of AMPA receptor–cone snail toxin complexes illuminate activation mechanism

Chen, L., Dürr, K. L., & Gouaux, E. (2014) · Science · doi:10.1126/science.1258409 · 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

Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel

Cady, S. D., & Hong, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711500105 · Cited by 122

Catalysis of Na + permeation in the bacterial sodium channel Na V Ab

Chakrabarti, N., Ing, C. E., Payandeh, J., Zheng, N., Catterall, W. A., & Pomès, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309452110 · Cited by 118

GPCR structures in drug design, emerging opportunities with new structures

Tautermann, C. S. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.07.009 · Cited by 117

Ion conduction and conformational flexibility of a bacterial voltage-gated sodium channel

Boiteux, C., Vorobyov, I. V., & Allen, T. W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320907111 · Cited by 117

Ionic Current Blockades from DNA and RNA Molecules in the α-Hemolysin Nanopore

Butler, T. Z., Gundlach, J. H., & Troll, M. A. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.107003 · Cited by 116

Computer Simulation of the Rough Lipopolysaccharide Membrane of Pseudomonas aeruginosa

Lins, R. D., & Straatsma, T. P. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75761-x · Cited by 114

Rhomboid Protease Dynamics and Lipid Interactions

Bondar, A., del Val, C., & White, S. H. (2009) · Structure · doi:10.1016/j.str.2008.12.017 · Cited by 113

Determination of RNA Orientation during Translocation through a Biological Nanopore

Butler, T. Z., Gundlach, J. H., & Troll, M. A. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.068957 · Cited by 111

Optimization of Receptor-G Protein Coupling by Bilayer Lipid Composition II

Niu, S., Mitchell, D. C., & Litman, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105778200 · Cited by 109

In Silico Partitioning and Transmembrane Insertion of Hydrophobic Peptides under Equilibrium Conditions

Ulmschneider, J. P., Smith, J. C., White, S. H., & Ulmschneider, M. B. (2011) · Journal of the American Chemical Society · doi:10.1021/ja204042f · Cited by 109

The Role of Molecular Simulations in the Development of Inhibitors of Amyloid β-Peptide Aggregation for the Treatment of Alzheimer’s Disease

Lemkul, J. A., & Bevan, D. R. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300091a · Cited by 109

Interaction of the Acetylcholine (Nicotinic) Receptor Protein from Torpedo marmorata Electric Organ with Monolayers of Pure Lipids

Popot, J., DEMEL, R. A., Sobel, A., Deenen, L. L. M. V., & Changeux, J. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12209.x · Cited by 108

Anticonvulsant and Adverse Effects of Avermectin Analogs in Mice Are Mediated through the γ-Aminobutyric AcidA Receptor

Dawson, G. R., Wafford, K. A., Smith, A. J., Marshall, G. R., Bayley, P. J., Schaeffer, J. M., Meinke, P. T., & McKernan, R. M. (2000) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)39005-6 · Cited by 108

The structural basis for catalysis and substrate specificity of a rhomboid protease

Vinothkumar, K. R., Střı́šovský, K., Andreeva, A. E., Christova, Y., Verhelst, S. H. L., & Freeman, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.243 · Cited by 107

Equilibrium thermodynamics from basin-sampling

Bogdan, T. V., Wales, D. J., & Calvo, F. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2148958 · Cited by 105

Rearrangements of the water trimer

Walsh, T. R., & Wales, D. J. (1996) · Journal of the Chemical Society Faraday Transactions · doi:10.1039/ft9969202505 · Cited by 105

Rhodopsin Exhibits a Preference for Solvation by Polyunsaturated Docosohexaenoic Acid

Feller, S. E., Gawrisch, K., & Woolf, T. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0345874 · Cited by 104

Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy

Cady, S. D., Wang, J., Wu, Y., DeGrado, W. F., & Hong, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja102581n · Cited by 102

The lateral gate of SecYEG opens during protein translocation.

du Plessis, D. J. F., Berrelkamp, G., Nouwen, N., & Driessen, A. J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901855200 · Cited by 102

Energy landscapes for diffusion: Analysis of cage-breaking processes

de Souza, V. K., & Wales, D. J. (2008) · The Journal of Chemical Physics · doi:10.1063/1.2992128 · Cited by 101

Local anesthetic and antiepileptic drug access and binding to a bacterial voltage-gated sodium channel

Boiteux, C., Vorobyov, I. V., French, R. J., French, C. R., Yarov-Yarovoy, V. M., & Allen, T. W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408710111 · Cited by 100

Channelopathies linked to plasma membrane phosphoinositides

Logothetis, D. E., Petrou, V. I., Adney, S. K., & Mahajan, R. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0828-y · Cited by 100

Anticonvulsant and adverse effects of avermectin analogs in mice are mediated through the gamma-aminobutyric acid(A) receptor.

Dawson, G. R., Wafford, K. A., Smith, A., Marshall, G. R., Bayley, P. J., Schaeffer, J. M., Meinke, P. T., & McKernan, R. M. (2000) · PubMed · Cited by 100

Cholesterol effects on nicotinic acetylcholine receptor

Barrantes, F. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04719.x · Cited by 99

Architectural and thermodynamic principles underlying intramembrane protease function

Baker, R. P., & Urban, S. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1021 · Cited by 98

Predictions for Cholesterol Interaction Sites on the A2A Adenosine Receptor

Lee, J. Y., & Lyman, E. R. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307532d · Cited by 98

Stationary points and dynamics in high-dimensional systems

Wales, D., & Doye, J. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1625644 · Cited by 96

Structure of Rhomboid Protease in a Lipid Environment

Vinothkumar, K. R. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.029 · Cited by 95

Regulation of voltage-gated potassium channels by PI(4,5)P2

Kruse, M., Hammond, G. R. V., & Hille, B. (2012) · The Journal of General Physiology · doi:10.1085/jgp.201210806 · Cited by 95

Environment of the Gating Charges in the Kv1.2 Shaker Potassium Channel

Treptow, W. L., & Tarek, M. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.080754 · Cited by 93

Phospholipid chain immobilization and steriod rotational immobilization in acetylcholine receptor-rich membranes from torpedo marmorata

Marsh, D., Watts, A. G., & Barrantes, F. J. (1981) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(81)90516-2 · Cited by 93

Coarse-Grained Biomolecular Simulation with REACH: Realistic Extension Algorithm via Covariance Hessian

Moritsugu, K., & Smith, J. C. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.111898 · Cited by 93

How Does a Voltage Sensor Interact with a Lipid Bilayer? Simulations of a Potassium Channel Domain

Sands, Z. A., & Sansom, M. S. P. (2007) · Structure · doi:10.1016/j.str.2007.01.004 · Cited by 93

PIP 2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

Rodríguez‐Menchaca, A. A., Adney, S. K., Tang, Q.-Y., Meng, X.-Y., Rosenhouse‐Dantsker, A., Cui, M., & Logothetis, D. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207901109 · Cited by 92

The effect of cholesterol on agonist‐induced flux in reconstituted acetylcholine receptor vesicles

Dalziel, A. W., Rollins, E. S., & McNamee, M. G. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80435-2 · Cited by 92

Structure-Guided Design of AMP Mimics That Inhibit Fructose-1,6-bisphosphatase with High Affinity and Specificity

Erion, M. D., Dang, Q., Reddy, M. R., Kasibhatla, S. R., Huang, J., Lipscomb, W. N., & van Poelje, P. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074869u · Cited by 92

Cholesterol depletion activates rapid internalization of submicron-sized acetylcholine receptor domains at the cell membrane

Borroni, V., Borroni, V., Baier, C. J., Lang, T., Bonini, I. C., White, M. M., Garbus, I., & Barrantes, F. J. (2006) · Molecular Membrane Biology · doi:10.1080/09687860600903387 · Cited by 92

Open-cap conformation of intramembrane protease GlpG

Wang, Y., & Ha, Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611080104 · Cited by 91

Nanopore Analysis of a Small 86‐Residue Protein

Stefureac, R. I., Waldner, L. L., Howard, P., & Lee, J. S. (2007) · Small · doi:10.1002/smll.200700402 · Cited by 91

Mechanism and Kinetics of Peptide Partitioning into Membranes from All-Atom Simulations of Thermostable Peptides

Ulmschneider, M. B., Doux, J. P. F., Killian, J. A., Smith, J. C., & Ulmschneider, J. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909347x · Cited by 91

Theoretical study of the water tetramer

Wales, D. J., & Walsh, T. R. (1997) · The Journal of Chemical Physics · doi:10.1063/1.473681 · Cited by 88

Quantitative Modeling of Membrane Deformations by Multihelical Membrane Proteins: Application to G-Protein Coupled Receptors

Mondal, S., Khelashvili, G., Shan, J., Andersen, O. S., & Weinstein, H. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.09.037 · Cited by 88

The rhomboid protease family: a decade of progress on function and mechanism

Urban, S., & Dickey, S. W. (2011) · Genome biology · doi:10.1186/gb-2011-12-10-231 · Cited by 88

A Predicted Binding Site for Cholesterol on the GABAA Receptor

Hénin, J., Salari, R., Murlidaran, S., & Brannigan, G. H. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.03.024 · Cited by 87

Hydrogen bond dynamics in membrane protein function

Bondar, A., & White, S. H. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.035 · Cited by 87

The force network ensemble for granular packings

Tighe, B. P., Snoeijer, J. H., Vlugt, T. J. H., & van Hecke, M. (2010) · Soft Matter · doi:10.1039/b926592a · Cited by 86

On the selective ion binding hypothesis for potassium channels

Kim, I., & Allen, T. W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110735108 · Cited by 85

Effect of ivermectin on γ-aminobutyric acid-induced chloride currents in mouse hippocampal embryonic neurones

Krůšek, J., & Zemkova, H. W. (1994) · European Journal of Pharmacology · doi:10.1016/0014-2999(94)90500-2 · Cited by 83

Calculation of Relative Binding Free Energy Differences for Fructose 1,6-Bisphosphatase Inhibitors Using the Thermodynamic Cycle Perturbation Approach

Reddy, M. R., & Erion, M. D. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0103288 · Cited by 80

Origins of ion selectivity in potassium channels from the perspective of channel block

Nimigean, C. M., & Allen, T. W. (2011) · The Journal of General Physiology · doi:10.1085/jgp.201010551 · Cited by 80

Metastability and Markov State Models in Molecular Dynamics

Schütte, C., & Sarich, M. (2013) · Courant Lecture Notes · doi:10.1090/cln/024 · Cited by 80

Energy landscapes of model polyalanines

Mortenson, P. N., Evans, D. A., & Wales, D. J. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1484389 · Cited by 79

Improving Internal Peptide Dynamics in the Coarse-Grained MARTINI Model: Toward Large-Scale Simulations of Amyloid- and Elastin-like Peptides

Seo, M., Rauscher, S., Pomès, R., & Tieleman, D. P. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct200876v · Cited by 78

The Role of L1 Loop in the Mechanism of Rhomboid Intramembrane Protease GlpG

Wang, Y., Maegawa, S., Akiyama, Y., & Ha, Y. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.014 · Cited by 78

Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology

Mohammad, M. M., & Movileanu, L. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0309-9 · Cited by 76

The free energy landscape and dynamics of met-enkephalin

Evans, D. A., & Wales, D. J. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1616515 · Cited by 76

Finite-size scaling at the jamming transition: Corrections to scaling and the correlation-length critical exponent

Vågberg, D., Valdez-Balderas, D., Moore, M. A., Olsson, P., & Teitel, S. (2011) · Physical Review E · doi:10.1103/physreve.83.030303 · Cited by 74

Rigorous Free Energy Calculations in Structure‐Based Drug Design

Michel, J., Foloppe, N., & Essex, J. (2010) · Molecular Informatics · doi:10.1002/minf.201000051 · Cited by 73

Probing the Effects of Membrane Cholesterol in the Torpedo californica Acetylcholine Receptor and the Novel Lipid-exposed Mutation αC418W in XenopusOocytes

Santiago, J., Guzmán, G. R., Rojas, L. V., Marti, R., Asmar-Rovira, G. A., Santana, L. F., McNamee, M. G., & Lasalde‐Dominicci, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104563200 · Cited by 73

Disaccharides Impact the Lateral Organization of Lipid Membranes

Moiset, G., López, C. A., Bartelds, R., Syga, Ł., Rijpkema, E. M. A., Cukkemane, A., Baldus, M., Poolman, B., & Marrink, ‪. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505476c · Cited by 72

Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site

Lenaeus, M. J., Burdette, D. O., Wagner, T., Focia, P. J., & Gross, A. (2014) · Biochemistry · doi:10.1021/bi500525s · Cited by 72

Targeting ion channels for drug discovery.

Clare, J. J. (2010) · PubMed · Cited by 71

Metastability and Markov State Models in Molecular Dynamics: Modeling, Analysis, Algorithmic Approaches

Schütte, C., & Sarich, M. (2013) · Cited by 71

Conformational dynamics and membrane interactions of the E. coli outer membrane protein FecA: A molecular dynamics simulation study

Piggot, T. J., Holdbrook, D. A., & Khalid, S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.08.021 · Cited by 71

The role of cholesterol on the activity and stability of neurotensin receptor 1

Oates, J., Faust, B., Attrill, H. L., Harding, P., Orwick, M., & Watts, A. G. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.04.010 · Cited by 70

Coexistence of two adamantane binding sites in the influenza A M2 ion channel

Rosenberg, M., & Casarotto, M. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002051107 · Cited by 69

Topography of Nicotinic Acetylcholine Receptor Membrane-embedded Domains

Barrantes, F. J., Antollini, S. S., Blanton, M., & PRIETO, M. J. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005246200 · Cited by 69

Allosteric regulation of rhomboid intramembrane proteolysis

Arutyunova, E. I., Panwar, P., Skiba, P. M., Gale, N., Mak, M. W., & Lemieux, M. J. (2014) · The EMBO Journal · doi:10.15252/embj.201488149 · Cited by 68

Molecular Interactions of Alzheimer's Aβ Protofilaments with Lipid Membranes

Tofoleanu, F., & Buchete, N. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.063 · Cited by 68

Influence of membrane cholesterol on modulation of the GABAA receptor by neuroactive steroids and other potentiators

Sooksawate, T., & Simmonds, M. A. (2001) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704360 · Cited by 67

Surveying a complex potential energy landscape: Overcoming broken ergodicity using basin-sampling

Wales, D. J. (2013) · Chemical Physics Letters · doi:10.1016/j.cplett.2013.07.066 · Cited by 66

Characterization of the outer membrane protein OprF of Pseudomonas aeruginosa in a lipopolysaccharide membrane by computer simulation

Straatsma, T. P., & Soares, T. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22165 · Cited by 66

Alzheimer Aβ peptide interactions with lipid membranes

Tofoleanu, F., & Buchete, N. (2012) · Prion · doi:10.4161/pri.21022 · Cited by 66

Sampling alternative conformational states of transporters and receptors with AlphaFold2

del Alamo, D., Sala, D., Mchaourab, H. S., & Meiler, J. (2022) · eLife · doi:10.7554/elife.75751 · Cited by 511

Ubiquitination 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

Molecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms

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

Introduction to the Membrane Protein Reviews: The Interplay of Structure, Dynamics, and Environment in Membrane Protein Function

Sachs, J. N., & Engelman, D. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.110105.142336 · Cited by 114

Modeling of Membrane Proteins

Latek, D., Trzaskowski, B., Niewieczerzał, S., Miszta, P., Młynarczyk, K., Dębiński, A., Puławski, W., Yuan, S., Sztyler, A., Orzeł, U., et al. (2018) · Springer series on bio- and neurosystems · doi:10.1007/978-3-319-95843-9_12 · Cited by 8

Structure and dynamics of membrane proteins

van Amerongen, H., Hemminga, M. A., & Vos, W. L. (2003)

Biophysical studies of membrane protein structure and function

Watts, A. G. (2014) · Cited by 1

Perspective on the Effect of Membrane Mimetics on Dynamic Properties of Integral Membrane Proteins

Sahu, I. D., & Lorigan, G. A. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c07324 · Cited by 3