Normal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins

VMD: visual molecular dynamics

Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617

Scalable molecular dynamics with NAMD

Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914

Calcium's Role in Mechanotransduction during Muscle Development

Benavides Damm, T., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,502

Principal Component Analysis

Jolliffe, I. (2005) · Encyclopedia of Statistics in Behavioral Science · doi:10.1002/0470013192.bsa501 · Cited by 14,310

Classical Mechanics

Goldstein, H. (1951) · UCLA - Biblioteca de Ciencias y Tecnologia Felix Morales Bueno · Cited by 10,004

On the nature of allosteric transitions: A plausible model

Monod, J., Wyman, J., & Changeux, J.-P. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 8,825

Glutamate neurotoxicity and diseases of the nervous system

CHOI, D. (1988) · Neuron · doi:10.1016/0896-6273(88)90162-6 · Cited by 7,972

The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity

Doyle, D. A., Cabral, J. M., 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 6,807

Principal Component Analysis

Chiang, L. H., Russell, E. L., & Braatz, R. D. (2001) · Advanced Textbooks in Control and Signal Processing · doi:10.1007/978-1-4471-0347-9_4 · Cited by 6,594

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637

ABC Transporters: From Microorganisms to Man

Higgins, C. F. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.000435 · Cited by 3,985

DrugBank: a comprehensive resource for in silico drug discovery and exploration

Wishart, D. S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj067 · Cited by 3,892

How many drug targets are there?

Overington, J. P., Al-Lazikani, B., & Hopkins, A. L. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2199 · Cited by 3,505

Essential dynamics of proteins

Amadei, A., Linssen, A. B. M., & Berendsen, H. J. C. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170408 · Cited by 3,492

High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H.-J., Kuhn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,264

The Energy Landscapes and Motions of Proteins

Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250

PANTHER: A Library of Protein Families and Subfamilies Indexed by Function

Thomas, P. D., Campbell, M. J., Kejariwal, A., Mi, H., Karlak, B., Daverman, R., Diemer, K., Muruganujan, A., & Narechania, A. (2003) · Genome Research · doi:10.1101/gr.772403 · Cited by 2,944

The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints

Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941

Dynamic personalities of proteins

Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545

Coarse Grained Model for Semiquantitative Lipid Simulations

Marrink, S. J., de Vries, A. H., & Mark, A. E. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp036508g · Cited by 2,257

The Feynman Lectures on Physics

(2013) · Choice Reviews Online · doi:10.5860/choice.50-6817 · Cited by 1,866

HOLE: A program for the analysis of the pore dimensions of ion channel structural models

Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A., & Sansom, M. S. P. (1996) · Journal of Molecular Graphics · doi:10.1016/s0263-7855(97)00009-x · Cited by 1,793

The 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist

Jaakola, V.-P., Griffith, M. T., Hanson, M. A., Cherezov, V., Chien, E. Y. T., Lane, J. R., IJzerman, A. P., & Stevens, R. C. (2008) · Science · doi:10.1126/science.1164772 · Cited by 1,781

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B., & Sixma, T. K. (2001) · Nature · doi:10.1038/35077011 · Cited by 1,759

Epilepsy and Exacerbation of Brain Injury in Mice Lacking the Glutamate Transporter GLT-1

Tanaka, K., Watase, K., Manabe, T., Yamada, K., Watanabe, M., Takahashi, K., Iwama, H., Nishikawa, T., Ichihara, N., Kikuchi, T., et al. (1997) · Science · doi:10.1126/science.276.5319.1699 · Cited by 1,752

Refined Structure of the Nicotinic Acetylcholine Receptor at 4Å Resolution

Unwin, N. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.031 · Cited by 1,659

Anisotropy of Fluctuation Dynamics of Proteins with an Elastic Network Model

Atilgan, A. R., Durell, S. R., Jernigan, R. L., Demirel, M. C., Keskin, O., & Bahar, I. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76033-x · Cited by 1,637

Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis

Tirion, M. M. (1996) · Physical Review Letters · doi:10.1103/physrevlett.77.1905 · Cited by 1,615

Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential

Bahar, I., Atilgan, A. R., & Erman, B. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00024-2 · Cited by 1,375

Structure of a β1-adrenergic G-protein-coupled receptor

Warne, T., Serrano-Vega, M. J., Baker, J. G., Moukhametzianov, R., Edwards, P. C., Henderson, R., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2008) · Nature · doi:10.1038/nature07101 · Cited by 1,344

Crystal structure and mechanism of a calcium-gated potassium channel

Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/417515a · Cited by 1,332

Structure and gating mechanism of the acetylcholine receptor pore

Miyazawa, A., Fujiyoshi, Y., & Unwin, N. (2003) · Nature · doi:10.1038/nature01748 · Cited by 1,270

The open pore conformation of potassium channels

Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/417523a · Cited by 1,197

Heterotrimeric G protein activation by G-protein-coupled receptors

Oldham, W. M., & Hamm, H. E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2299 · Cited by 1,184

Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., & Khorana, H. G. (1996) · Science · doi:10.1126/science.274.5288.768 · Cited by 1,179

Climatic Impact of Tropical Lowland Deforestation on Nearby Montane Cloud Forests

Lawton, R. O., Nair, U. S., Pielke, R. A., & Welch, R. M. (2001) · Science · doi:10.1126/science.1062459 · Cited by 1,169

Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

Frauenfelder, H., Petsko, G. A., & Tsernoglou, D. (1979) · Nature · doi:10.1038/280558a0 · Cited by 1,149

ION CHANNELS IN EXCITABLE MEMBRANES

Hucho, F. (1978) · Transport by proteins · doi:10.1515/9783111710013-017 · Cited by 1,136

Molecular Basis of Mechanotransduction in Living Cells

Hamill, O. P., & Martinac, B. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.685 · Cited by 1,134

Intrinsic dynamics of an enzyme underlies catalysis

Eisenmesser, E. Z., Millet, O., Labeikovsky, W., Korzhnev, D. M., Wolf-Watz, M., Bosco, D. A., Skalicky, J. J., Kay, L. E., & Kern, D. (2005) · Nature · doi:10.1038/nature04105 · Cited by 1,101

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Henzler-Wildman, K. A., Lei, M., Thai, V., Kerns, S. J., Karplus, M., & Kern, D. (2007) · Nature · doi:10.1038/nature06407 · Cited by 1,064

Crystal structure of opsin in its G-protein-interacting conformation

Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059

Principles of Selective Ion Transport in Channels and Pumps

Gouaux, E., & MacKinnon, R. (2005) · Science · doi:10.1126/science.1113666 · Cited by 1,059

The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure

Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049

Computer simulation of protein folding

Levitt, M., & Warshel, A. (1975) · Nature · doi:10.1038/253694a0 · Cited by 1,045

Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

Lange, O. F., Lakomek, N.-A., Farès, C., Schröder, G. F., Walter, K. F. A., Becker, S., Meiler, J., Grubmüller, H., Griesinger, C., & de Groot, B. L. (2008) · Science · doi:10.1126/science.1157092 · Cited by 1,044

The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism

Locher, K. P., Lee, A. T., & Rees, D. C. (2002) · Science · doi:10.1126/science.1071142 · Cited by 1,023

Acetylcholine receptor channel imaged in the open state

Unwin, N. (1995) · Nature · doi:10.1038/373037a0 · Cited by 999

Conformational Substates in Proteins

Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 993

Structure of the MscL Homolog from Mycobacterium tuberculosis : A Gated Mechanosensitive Ion Channel

Chang, G., Spencer, R. H., Lee, A. T., Barclay, M. T., & Rees, D. C. (1998) · Science · doi:10.1126/science.282.5397.2220 · Cited by 990

Control of the Selectivity of the Aquaporin Water Channel Family by Global Orientational Tuning

Tajkhorshid, E., Nollert, P., Jensen, M. Ø., Miercke, L. J. W., O'Connell, J., Stroud, R. M., & Schulten, K. (2002) · Science · doi:10.1126/science.1067778 · Cited by 914

Crystal structure of the ligand-free G-protein-coupled receptor opsin

Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H.-W., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 903

Water Permeation Across Biological Membranes: Mechanism and Dynamics of Aquaporin-1 and GlpF

de Groot, B. L., & Grubmüller, H. (2001) · Science · doi:10.1126/science.1066115 · Cited by 900

Conformational change of proteins arising from normal mode calculations

Tama, F., & Sanejouand, Y.-H. (2001) · Protein Engineering, Design and Selection · doi:10.1093/protein/14.1.1 · Cited by 891

Intrinsic motions along an enzymatic reaction trajectory

Henzler-Wildman, K. A., Thai, V., Lei, M., Ott, M., Wolf-Watz, M., Fenn, T., Pozharski, E., Wilson, M. A., Petsko, G. A., Karplus, M., et al. (2007) · Nature · doi:10.1038/nature06410 · Cited by 887

The multiscale coarse-graining method. I. A rigorous bridge between atomistic and coarse-grained models

Noid, W. G., Chu, J.-W., Ayton, G. S., Krishna, V., Izvekov, S., Voth, G. A., Das, A., & Andersen, H. C. (2008) · The Journal of Chemical Physics · doi:10.1063/1.2938860 · Cited by 875

Structural mechanism of plant aquaporin gating

Törnroth-Horsefield, S., Wang, Y., Hedfalk, K., Johanson, U., Karlsson, M., Tajkhorshid, E., Neutze, R., & Kjellbom, P. (2006) · Nature · doi:10.1038/nature04316 · Cited by 862

TCDB: the Transporter Classification Database for membrane transport protein analyses and information

Saier, M. H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj001 · Cited by 858

Flux coupling in a neuronal glutamate transporter

Zerangue, N., & Kavanaugh, M. P. (1996) · Nature · doi:10.1038/383634a0 · Cited by 846

Drugs, their targets and the nature and number of drug targets

Imming, P., Sinning, C., & Meyer, A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2132 · Cited by 839

Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.

Brooks, B., & Karplus, M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.21.6571 · Cited by 829

Protein states and proteinquakes.

Ansari, A., Berendzen, J., Bowne, S. F., Frauenfelder, H., Iben, I. E., Sauke, T. B., Shyamsunder, E., & Young, R. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.15.5000 · Cited by 828

Theoretical Studies of Protein Folding

Go, N. (1983) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.12.060183.001151 · Cited by 824

Energetics of ion conduction through the K+ channel

Bernèche, S., & Roux, B. (2001) · Nature · doi:10.1038/35102067 · Cited by 803

Identifying conformational changes with site-directed spin labeling.

Hubbell, W. L., Cafiso, D. S., & Altenbach, C. (2000) · Nature Structural Biology · doi:10.1038/78956 · Cited by 793

Molecular Recognition and Docking Algorithms

Brooijmans, N., & Kuntz, I. D. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.142532 · Cited by 788

Structure of a glutamate transporter homologue from Pyrococcus horikoshii

Yernool, D., Boudker, O., Jin, Y., & Gouaux, E. (2004) · Nature · doi:10.1038/nature03018 · Cited by 783

New Tools Provide New Insights in NMR Studies of Protein Dynamics

Mittermaier, A., & Kay, L. E. (2006) · Science · doi:10.1126/science.1124964 · Cited by 780

Gaussian Dynamics of Folded Proteins

Haliloglu, T., Bahar, I., & Erman, B. (1997) · Physical Review Letters · doi:10.1103/physrevlett.79.3090 · Cited by 772

Allosteric Mechanisms of Signal Transduction

Changeux, J.-P., & Edelstein, S. J. (2005) · Science · doi:10.1126/science.1108595 · Cited by 747

Accelerating molecular modeling applications with graphics processors

Stone, J. E., Phillips, J. C., Freddolino, L., Hardy, D. J., Trabuco, L. G., & Schulten, K. (2007) · Journal of Computational Chemistry · doi:10.1002/jcc.20829 · Cited by 739

Coarse-grained normal mode analysis in structural biology

Bahar, I., & Rader, A. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.08.007 · Cited by 731

Dynamics of a small globular protein in terms of low-frequency vibrational modes.

Go, N., Noguti, T., & Nishikawa, T. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.12.3696 · Cited by 722

Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme

Levitt, M., Sander, C., & Stern, P. S. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90230-x · Cited by 721

TTD: Therapeutic Target Database

Chen, X. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.412 · Cited by 716

Analysis of domain motions by approximate normal mode calculations

Hinsen, K. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19981115)33:3<417::aid-prot10>3.0.co;2-8 · Cited by 713

ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement

Suhre, K., & Sanejouand, Y.-H. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh368 · Cited by 691

STUDIES ON PROTEIN FOLDING, UNFOLDING AND FLUCTUATIONS BY COMPUTER SIMULATION: I. The effect of specific amino acid sequence represented by specific inter‐unit interactions

Taketomi, H., Ueda, Y., & Gō, N. (1975) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1975.tb02465.x · Cited by 674

X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation

Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J.-P., Delarue, M., & Corringer, P.-J. (2009) · Nature · doi:10.1038/nature07462 · Cited by 674

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

Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography

Okada, T., Fujiyoshi, Y., Silow, M., Navarro, J., Landau, E. M., & Shichida, Y. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082666399 · Cited by 662

The role of dynamics in allosteric regulation

Kern, D., & Zuiderweg, E. R. (2003) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.10.008 · Cited by 661

Emergence of Preferred Structures in a Simple Model of Protein Folding

Li, H., Helling, R., Tang, C., & Wingreen, N. (1996) · Science · doi:10.1126/science.273.5275.666 · Cited by 650

SuperTarget and Matador: resources for exploring drug-target relationships

Gunther, S., Kuhn, M., Dunkel, M., Campillos, M., Senger, C., Petsalaki, E., Ahmed, J., Urdiales, E. G., Gewiess, A., Jensen, L. J., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm862 · Cited by 647

ABC transporters: physiology, structure and mechanism – an overview

Higgins, C. F. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01193-7 · Cited by 641

Dynamically driven protein allostery

Popovych, N., Sun, S., Ebright, R. H., & Kalodimos, C. G. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1132 · Cited by 635

Statistical thermodynamics of random networks

Flory, P. J. (1976) · Proceedings of the Royal Society of London. A. Mathematical and Physical Sciences · doi:10.1098/rspa.1976.0146 · Cited by 632

G protein coupled receptor structure and activation

Kobilka, B. K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.10.021 · Cited by 623

Open channel structure of MscL and the gating mechanism of mechanosensitive channels

Perozo, E., Cortes, D. M., Sompornpisut, P., Kloda, A., & Martinac, B. (2002) · Nature · doi:10.1038/nature00992 · Cited by 614

Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs),

Teller, D. C., Okada, T., Behnke, C. A., Palczewski, K., & Stenkamp, R. E. (2001) · Biochemistry · doi:10.1021/bi0155091 · Cited by 602

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 596

Structural Rearrangements Underlying K + -Channel Activation Gating

Perozo, E., Marien, D., Cortes, & Cuello, L. G. (1999) · Science · doi:10.1126/science.285.5424.73 · Cited by 552

Protein dynamics from NMR.

Ishima, R., & Torchia, D. A. (2000) · Nature Structural Biology · doi:10.1038/78963 · Cited by 546

Quantitative dynamics and binding studies of the 20S proteasome by NMR

Sprangers, R., & Kay, L. E. (2007) · Nature · doi:10.1038/nature05512 · Cited by 527

Structures and Properties of Rubberlike Networks

Erman, B., & Mark, J. E. (1997) · Oxford University Press eBooks · doi:10.1093/oso/9780195082371.001.0001 · Cited by 526

Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel

Hilf, R. J. C., & Dutzler, R. (2009) · Nature · doi:10.1038/nature07461 · Cited by 526

Overcoming the challenges of membrane protein crystallography

Carpenter, E. P., Beis, K., Cameron, A. D., & Iwata, S. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.07.001 · Cited by 525

Recent advances in Cys-loop receptor structure and function

Sine, S. M., & Engel, A. G. (2006) · Nature · doi:10.1038/nature04708 · Cited by 521

Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins

Miyashita, O., Onuchic, J. N., & Wolynes, P. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135471100 · Cited by 514

Lead discovery using molecular docking

Shoichet, B. K., McGovern, S. L., Wei, B., & Irwin, J. J. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00339-3 · Cited by 501

Flexible ligand docking to multiple receptor conformations: a practical alternative

Totrov, M., & Abagyan, R. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.01.004 · Cited by 497

Walking on potential energy surfaces

Simons, J., Joergensen, P., Taylor, H., & Ozment, J. (1983) · The Journal of Physical Chemistry · doi:10.1021/j100238a013 · Cited by 497

Crystal structure of squid rhodopsin

Murakami, M., & Kouyama, T. (2008) · Nature · doi:10.1038/nature06925 · Cited by 488

Usefulness and Limitations of Normal Mode Analysis in Modeling Dynamics of Biomolecular Complexes

Ma, J. (2005) · Structure · doi:10.1016/j.str.2005.02.002 · Cited by 487

Building-block approach for determining low-frequency normal modes of macromolecules

Tama, F., Gadea, F. X., Marques, O., & Sanejouand, Y.-H. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001001)41:1<1::aid-prot10>3.0.co;2-p · Cited by 484

Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter

Boudker, O., Ryan, R. M., Yernool, D., Shimamoto, K., & Gouaux, E. (2007) · Nature · doi:10.1038/nature05455 · Cited by 484

Carrier-mediated cellular uptake of pharmaceutical drugs: an exception or the rule?

Dobson, P. D., & Kell, D. B. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2438 · Cited by 475

Investigating protein dynamics in collective coordinate space

Kitao, A., & Go, N. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80023-2 · Cited by 475

Transmembrane Protein Structure: Spin Labeling of Bacteriorhodopsin Mutants

Altenbach, C., Marti, T., Khorana, H. G., & Hubbell, W. L. (1990) · Science · doi:10.1126/science.2160734 · Cited by 474

High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation

Altenbach, C., Kusnetzow, A. K., Ernst, O. P., Hofmann, K. P., & Hubbell, W. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802515105 · Cited by 462

Crystal structure of a photoactivated deprotonated intermediate of rhodopsin

Salom, D., Lodowski, D. T., Stenkamp, R. E., Trong, I. L., Golczak, M., Jastrzebska, B., Harris, T., Ballesteros, J. A., & Palczewski, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608022103 · Cited by 442

Vibrational Dynamics of Folded Proteins: Significance of Slow and Fast Motions in Relation to Function and Stability

Bahar, I., Atilgan, A. R., Demirel, M. C., & Erman, B. (1998) · Physical Review Letters · doi:10.1103/physrevlett.80.2733 · Cited by 441

Crystallization of membrane proteins

Ostermeier, C., & Michel, H. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80080-2 · Cited by 439

The Cavity and Pore Helices in the KcsA K + Channel: Electrostatic Stabilization of Monovalent Cations

Roux, B., & MacKinnon, R. (1999) · Science · doi:10.1126/science.285.5424.100 · Cited by 434

Allosteric Receptors after 30 Years

Changeux, J.-P., & Edelstein, S. J. (1998) · Neuron · doi:10.1016/s0896-6273(00)80616-9 · Cited by 431

Structure and dynamics of membrane proteins as studied by infrared spectroscopy

Arrondo, J. L. R., & Goñi, F. M. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00007-3 · Cited by 426

Multiscale modeling of biomolecular systems: in serial and in parallel

Ayton, G. S., Noid, W. G., & Voth, G. A. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.03.004 · Cited by 420

Watching proteins move using site-directed spin labeling

Hubbell, W. L., Mchaourab, H. S., Altenbach, C., & Lietzow, M. A. (1996) · Structure · doi:10.1016/s0969-2126(96)00085-8 · Cited by 420

Theoretical and computational models of biological ion channels

Roux, B., Allen, T., Bernèche, S., & Im, W. (2004) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583504003968 · Cited by 413

Protein Flexibility in Ligand Docking and Virtual Screening to Protein Kinases

Cavasotto, C. N., & Abagyan, R. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.003 · Cited by 412

Thermodynamic fluctuations in protein molecules.

Cooper, A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.8.2740 · Cited by 410

Mechanism of selectivity in aquaporins and aquaglyceroporins

Hub, J. S., & de Groot, B. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707662104 · Cited by 410

The hinge-bending mode in lysozyme

MCCAMMON, J. A., GELIN, B. R., KARPLUS, M., & WOLYNES, P. G. (1976) · Nature · doi:10.1038/262325a0 · Cited by 379

Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state

Tobi, D., & Bahar, I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507603102 · Cited by 379

Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking

Hubbell, W. L., Altenbach, C., Hubbell, C. M., & Khorana, H. G. (2003) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(03)63010-x · Cited by 352

Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy

Tama, F., Valle, M., Frank, J., & Brooks, C. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632476100 · Cited by 344

The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin

Frauenfelder, H., McMahon, B. H., Austin, R. H., Chu, K., & Groves, J. T. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041614298 · Cited by 340

Keynote review: Structural biology and drug discovery

Congreve, M., Murray, C. W., & Blundell, T. L. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03484-7 · Cited by 338

Sequential Binding of Agonists to the β2 Adrenoceptor

Swaminath, G., Xiang, Y., Lee, T. W., Steenhuis, J., Parnot, C., & Kobilka, B. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310888200 · Cited by 333

Large Amplitude Conformational Change in Proteins Explored with a Plastic Network Model: Adenylate Kinase

Maragakis, P., & Karplus, M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.031 · Cited by 332

Coarse-grained molecular dynamics simulations of membrane proteins and peptides

Bond, P. J., Holyoake, J., Ivetac, A., Khalid, S., & Sansom, M. S. P. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.10.004 · Cited by 327

Accommodating Protein Flexibility in Computational Drug Design,

Carlson, H. A., & McCammon, J. A. (2000) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)23192-8 · Cited by 324

Anisotropic network model: systematic evaluation and a new web interface

Eyal, E., Yang, L.-W., & Bahar, I. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl448 · Cited by 322

Ligand-selective receptor conformations revisited: the promise and the problem

Kenakin, T. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00167-6 · Cited by 321

Recent advances and applications of site-directed spin labeling

FANUCCI, G., & CAFISO, D. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.08.008 · Cited by 318

Agonist-induced conformational changes in the G-protein-coupling domain of the β 2 adrenergic receptor

Ghanouni, P., Steenhuis, J. J., Farrens, D. L., & Kobilka, B. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101126198 · Cited by 311

NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis

Lindahl, E., Azuara, C., Koehl, P., & Delarue, M. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl082 · Cited by 309

Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation

Bahar, I., Chennubhotla, C., & Tobi, D. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.09.011 · Cited by 306

The changing landscape of protein allostery

Swain, J. F., & Gierasch, L. M. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.01.003 · Cited by 298

Energetics of Pore Opening in a Voltage-Gated K+ Channel

Yifrach, O., & MacKinnon, R. (2002) · Cell · doi:10.1016/s0092-8674(02)01013-9 · Cited by 291

NMR studies of protein structure and dynamics

Kay, L. E. (2005) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2004.11.021 · Cited by 284

Global ribosome motions revealed with elastic network model

Wang, Y., Rader, A. J., Bahar, I., & Jernigan, R. L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.01.005 · Cited by 284

The progress of membrane protein structure determination

White, S. H. (2004) · Protein Science · doi:10.1110/ps.04712004 · Cited by 284

Simulations of Ion Permeation Through a Potassium Channel: Molecular Dynamics of KcsA in a Phospholipid Bilayer

Shrivastava, I. H., & Sansom, M. S. P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76616-1 · Cited by 283

Representing Receptor Flexibility in Ligand Docking through Relevant Normal Modes

Cavasotto, C. N., Kovacs, J. A., & Abagyan, R. A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042260c · Cited by 278

The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding

Bakan, A., & Bahar, I. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904214106 · Cited by 277

Potassium channels and their evolving gates

Jan, L. Y., & Jan, Y. N. (1994) · Nature · doi:10.1038/371119a0 · Cited by 275

Dynamics of proteins predicted by molecular dynamics simulations and analytical approaches: application to alpha-amylase inhibitor.

Doruker, P., Atılgan, A. R., & Bahar, İ. (2000) · PubMed · Cited by 275

PDB_TM: selection and membrane localization of transmembrane proteins in the protein data bank

Tusnady, G. E. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki002 · Cited by 274

Coupling between Catalytic Site and Collective Dynamics: A Requirement for Mechanochemical Activity of Enzymes

Yang, L.-W., & Bahar, I. (2005) · Structure · doi:10.1016/j.str.2005.03.015 · Cited by 273

Principal pathway coupling agonist binding to channel gating in nicotinic receptors

Lee, W. Y., & Sine, S. M. (2005) · Nature · doi:10.1038/nature04156 · Cited by 273

Conformations of Macromolecules

Tm, B., & Ptitsyn, O. B. (1966) · Medical Entomology and Zoology · Cited by 272

A Single Glycine Residue at the Entrance to the First Membrane-Spanning Domain of the γ-Aminobutyric Acid Type A Receptor β2Subunit Affects Allosteric Sensitivity to GABA and Anesthetics

Carlson, B. X., Engblom, A. C., Kristiansen, U., Schousboe, A., & Olsen, R. W. (2000) · Molecular Pharmacology · doi:10.1124/mol.57.3.474 · Cited by 271

Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel

Bouzat, C., Gumilar, F., Spitzmaul, G., Wang, H.-L., Rayes, D., Hansen, S. B., Taylor, P., & Sine, S. M. (2004) · Nature · doi:10.1038/nature02753 · Cited by 267

SYMMETRY, FORM, AND SHAPE: Guiding Principles for Robustness in Macromolecular Machines

Tama, F., & Brooks, C. L. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102010 · Cited by 266

Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli

Cruickshank, C. C., Minchin, R. F., Le Dain, A. C., & Martinac, B. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78223-7 · Cited by 262

Structural Features and Light-Dependent Changes in the Cytoplasmic Interhelical E−F Loop Region of Rhodopsin: A Site-Directed Spin-Labeling Study

Altenbach, C., Yang, K., Farrens, D. L., Farahbakhsh, Z. T., Khorana, H. G., & Hubbell, W. L. (1996) · Biochemistry · doi:10.1021/bi960849l · Cited by 258

Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations

Zheng, W., Brooks, B. R., & Thirumalai, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510426103 · Cited by 258

Dynamics of Proteins in Crystals: Comparison of Experiment with Simple Models

Kundu, S., Melton, J. S., Sorensen, D. C., & Phillips, G. N. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75203-x · Cited by 254

Atomic structure of a Na+- and K+-conducting channel

Shi, N., Ye, S., Alam, A., Chen, L., & Jiang, Y. (2006) · Nature · doi:10.1038/nature04508 · Cited by 247

Determination of Membrane Protein Structure by Rotational Resonance NMR: Bacteriorhodopsin

Creuzet, F., McDermott, A., Gebhard, R., van der Hoef, K., Spijker-Assink, M. B., Herzfeld, J., Lugtenburg, J., Levitt, M. H., & Griffin, R. G. (1991) · Science · doi:10.1126/science.1990439 · Cited by 245

Excitatory amino acid transporters: keeping up with glutamate

Amara, S. G., & Fontana, A. C. K. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(02)00018-9 · Cited by 240

Soft Docking and Multiple Receptor Conformations in Virtual Screening

Ferrari, A. M., Wei, B. Q., Costantino, L., & Shoichet, B. K. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049756p · Cited by 239

Normal mode based flexible fitting of high-resolution structure into low-resolution experimental data from cryo-EM

Tama, F., Miyashita, O., & Brooks III, C. L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.03.002 · Cited by 235

Crystallographic Analysis of Primary Visual Photochemistry

Nakamichi, H., & Okada, T. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600595 · Cited by 230

Computer simulations of membrane proteins

Ash, W. L., Zlomislic, M. R., Oloo, E. O., & Tieleman, D. P. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.04.012 · Cited by 228

Crystal Structure of a Thermally Stable Rhodopsin Mutant

Standfuss, J., Xie, G., Edwards, P. C., Burghammer, M., Oprian, D. D., & Schertler, G. F. X. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.007 · Cited by 225

Dynamics of large proteins through hierarchical levels of coarse‐grained structures

Doruker, P., Jernigan, R. L., & Bahar, I. (2002) · Journal of Computational Chemistry · doi:10.1002/jcc.1160 · Cited by 223

Combining Efficient Conformational Sampling with a Deformable Elastic Network Model Facilitates Structure Refinement at Low Resolution

Schröder, G. F., Brunger, A. T., & Levitt, M. (2007) · Structure · doi:10.1016/j.str.2007.09.021 · Cited by 220

Analysis of domain motions in large proteins

Hinsen, K., Thomas, A., & Field, M. J. (1999) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19990215)34:3<369::aid-prot9>3.0.co;2-f · Cited by 220

Detection and trapping of intermediate states priming nicotinic receptor channel opening

Mukhtasimova, N., Lee, W. Y., Wang, H.-L., & Sine, S. M. (2009) · Nature · doi:10.1038/nature07923 · Cited by 218

Flexible Multi-scale Fitting of Atomic Structures into Low-resolution Electron Density Maps with Elastic Network Normal Mode Analysis

Tama, F., Miyashita, O., & Brooks, C. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.048 · Cited by 217

Molecular dynamics simulations of membrane channels and transporters

Khalili-Araghi, F., Gumbart, J., Wen, P.-C., Sotomayor, M., Tajkhorshid, E., & Schulten, K. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.02.011 · Cited by 216

Structural Models of the MscL Gating Mechanism

Sukharev, S., Durell, S. R., & Guy, H. R. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75751-7 · Cited by 215

Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor.

Gelin, B. R., & Karplus, M. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.6.2002 · Cited by 214

Coarse-Grained MD Simulations of Membrane Protein-Bilayer Self-Assembly

Scott, K. A., Bond, P. J., Ivetac, A., Chetwynd, A. P., Khalid, S., & Sansom, M. S. P. (2008) · Structure · doi:10.1016/j.str.2008.01.014 · Cited by 207

How Well Can We Understand Large-Scale Protein Motions Using Normal Modes of Elastic Network Models?

Yang, L., Song, G., & Jernigan, R. L. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.095927 · Cited by 206

The Mechanism and Pathway of pH Induced Swelling in Cowpea Chlorotic Mottle Virus

Tama, F., & Brooks, C. L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00135-3 · Cited by 205

Local peptide movement in the photoreaction intermediate of rhodopsin

Nakamichi, H., & Okada, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601765103 · Cited by 203

A Coarse-Grained Normal Mode Approach for Macromolecules:An Efficient Implementation and Application to Ca2+-ATPase

Li, G., & Cui, Q. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75257-0 · Cited by 202

Allosteric Changes in Protein Structure Computed by a Simple Mechanical Model: Hemoglobin T↔R2 Transition

Xu, C., Tobi, D., & Bahar, I. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.027 · Cited by 197

Discovery of New GPCR Biology: One Receptor Structure at a Time

Hanson, M. A., & Stevens, R. C. (2009) · Structure · doi:10.1016/j.str.2008.12.003 · Cited by 196

Exploring Global Distortions of Biological Macromolecules and Assemblies from Low-resolution Structural Information and Elastic Network Theory

Tama, F., Wriggers, W., & Brooks, C. L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00627-7 · Cited by 196

Coarse-Grained Modeling of the Actin Filament Derived from Atomistic-Scale Simulations

Chu, J.-W., & Voth, G. A. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.073924 · Cited by 193

Structure of the KcsA channel intracellular gate in the open state.

Liu, Y., Sompornpisut, P., & Perozo, E. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-883 · Cited by 192

Hinge‐bending motion in citrate synthase arising from normal mode calculations

Marques, O., & Sanejouand, Y. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340230410 · Cited by 191

Normal Mode Analysis Suggests a Quaternary Twist Model for the Nicotinic Receptor Gating Mechanism

Taly, A., Delarue, M., Grutter, T., Nilges, M., Le Novère, N., Corringer, P.-J., & Changeux, J.-P. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.050229 · Cited by 189

Structure and mechanism of ABC transporters

Locher, K. P. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.06.005 · Cited by 189

Diversity and Identity of Mechanical Properties of Icosahedral Viral Capsids Studied with Elastic Network Normal Mode Analysis

Tama, F., & Brooks, C. L. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.054 · Cited by 186

Therapeutic Targets: Progress of Their Exploration and Investigation of Their Characteristics

Zheng, C. J., Han, L. Y., Yap, C. W., Ji, Z. L., Cao, Z. W., & Chen, Y. Z. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.2.4 · Cited by 185

On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models

Delarue, M., & Dumas, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400301101 · Cited by 184

Multiscale methods for macromolecular simulations

Sherwood, P., Brooks, B. R., & Sansom, M. S. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.07.003 · Cited by 180

Four-Dimensional Docking: A Fast and Accurate Account of Discrete Receptor Flexibility in Ligand Docking

Bottegoni, G., Kufareva, I., Totrov, M., & Abagyan, R. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8009958 · Cited by 180

Allosteric modulations of the nicotinic acetylcholine receptor

Léna, C., & Changeux, J.-P. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90150-k · Cited by 180

Molecular structure of the lecithin ripple phase

de Vries, A. H., Yefimov, S., Mark, A. E., & Marrink, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408249102 · Cited by 180

Testing a Flexible-receptor Docking Algorithm in a Model Binding Site

Wei, B. Q., Weaver, L. H., Ferrari, A. M., Matthews, B. W., & Shoichet, B. K. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.015 · Cited by 179

What Makes an Aquaporin a Glycerol Channel? A Comparative Study of AqpZ and GlpF

Wang, Y., Schulten, K., & Tajkhorshid, E. (2005) · Structure · doi:10.1016/j.str.2005.05.005 · Cited by 179

Mechanisms of Cytoplasmic Hemoglobin and Myoglobin Function

Wittenberg, J. B., & Wittenberg, B. A. (1990) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.19.060190.001245 · Cited by 179

Solution NMR of supramolecular complexes: providing new insights into function

Sprangers, R., Velyvis, A., & Kay, L. E. (2007) · Nature Methods · doi:10.1038/nmeth1080 · Cited by 176

DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability

Rodrigues, C. H., Pires, D. E., & Ascher, D. B. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky300 · Cited by 1,086

Perspective: Coarse-grained models for biomolecular systems

Noid, W. G. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4818908 · Cited by 893

GPCR Dynamics: Structures in Motion

Latorraca, N. R., Venkatakrishnan, A. J., & Dror, R. O. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00177 · Cited by 835

Global dynamics of proteins: bridging between structure and function

Bahar, I., Lezon, T. R., Yang, L.-W., & Eyal, E. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131258 · Cited by 610

An introduction to NMR-based approaches for measuring protein dynamics

Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561