Structural Symmetry and Protein Function

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681 · see citing works

Dynamic instability of microtubule growth

Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337 · see citing works

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits *

Koshland, D. E., Némethy, G., & Filmer, D. (1966) · Biochemistry · doi:10.1021/bi00865a047 · Cited by 3,019 · see citing works

Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Abrahams, J. P., Leslie, A. G. W., Lutter, R., & Walker, J. E. (1994) · Nature · doi:10.1038/370621a0 · Cited by 3,004 · see citing works

Principles of protein-protein interactions

Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684 · see citing works

Physical Principles in the Construction of Regular VirusesPreprint

Caspar, D. L. D., & Klug, A. (1962) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1962.027.001.005 · Cited by 2,524 · see citing works

Structure of 20S proteasome from yeast at 2.4Å resolution

Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265 · see citing works

Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex

de Vos, A. M., Ultsch, M. H., & Kossiakoff, A. A. (1992) · Science · doi:10.1126/science.1549776 · Cited by 2,259 · see citing works

Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor

Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914 · see citing works

Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution

Löwe, J., Stock, D., Jap, B. K., Zwickl, P., Baumeister, W. P., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,527 · see citing works

FERRITIN: STRUCTURE, GENE REGULATION, AND CELLULAR FUNCTION IN ANIMALS, PLANTS, AND MICROORGANISMS

Theil, E. C. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.001445 · Cited by 1,337 · see citing works

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

Xu, Z. S., Horwich, A. L., & Sigler, P. B. (1997) · Nature · doi:10.1038/41944 · Cited by 1,244 · see citing works

Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity

Labeit, S., & Kolmerer, B. (1995) · Science · doi:10.1126/science.270.5234.293 · Cited by 1,242 · see citing works

Enthalpy–entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous properly of water

Lumry, R. W., & Rajender, S. (1970) · Biopolymers · doi:10.1002/bip.1970.360091002 · Cited by 1,224 · see citing works

The binding change mechanism for ATP synthase — Some probabilities and possibilities

Boyer, P. D. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90063-l · Cited by 1,038 · see citing works

Principles of protein–protein recognition

Chothia, C., & Janin, J. (1975) · Nature · doi:10.1038/256705a0 · Cited by 1,014 · see citing works

Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA

Krishna, T. S. R., Kong, X., Gary, S. L., Burgers, P., & Kuriyan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90014-0 · Cited by 902 · see citing works

Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology by

Blundell, T. L., Dodson, G. G., Hodgkin, D. C., & Mercola, D. (1972) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60143-6 · Cited by 836 · see citing works

How crowded is the cytoplasm?

Fulton, A. B. (1982) · Cell · doi:10.1016/0092-8674(82)90231-8 · Cited by 830 · see citing works

STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASE

Wlodawer, A., & Erickson, J. W. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002551 · Cited by 828 · see citing works

3D domain swapping: A mechanism for oligomer assembly

Bennett, M. J., Schlunegger, M. P., & Eisenberg, D. S. (1995) · Protein Science · doi:10.1002/pro.5560041202 · Cited by 765 · see citing works

Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp

Kong, X., Onrust, R., O’Donnell, M. E., & Kuriyan, J. (1992) · Cell · doi:10.1016/0092-8674(92)90445-i · Cited by 754 · see citing works

Structure of Small Viruses

Crick, F. H. C., & Watson, J. D. (1956) · Nature · doi:10.1038/177473a0 · Cited by 725 · see citing works

Tomato bushy stunt virus at 2.9 Å resolution

Harrison, S. C., Olson, A. J., Schutt, C. E., Winkler, F. K., & Bricogne, G. (1978) · Nature · doi:10.1038/276368a0 · Cited by 673 · see citing works

Assembly and Analysis of Conical Models for the HIV-1 Core

Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T., & Sundquist, W. I. (1999) · Science · doi:10.1126/science.283.5398.80 · Cited by 671 · see citing works

Mechanisms of cooperativity and allosteric regulation in proteins

Perutz, M. F. (1989) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500003826 · Cited by 648 · see citing works

Structure of simian virus 40 at 3.8-Å resolution

Liddington, R., Yan, Y., Moulai, J., Sahli, R., Benjamin, T. L., & Harrison, S. C. (1991) · Nature · doi:10.1038/354278a0 · Cited by 642 · see citing works

The atomic structure of the bluetongue virus core

Grimes, J. M., Burroughs, J. N., Gouet, P., Diprose, J. M., Malby, R. L., Zientara, S., Mertens, P., & Stuart, D. I. (1998) · Nature · doi:10.1038/26694 · Cited by 593 · see citing works

Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli

Sixma, T. K., Pronk, S. E., Kalk, K. H., et al. (1991) · Nature · doi:10.1038/351371a0 · Cited by 554 · see citing works

Mechanisms of cooperativity and allosteric regulation in proteins

Perutz, M. F. (1990) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(90)90139-j · Cited by 508 · see citing works

Structure of Rhombohedral 2 Zinc Insulin Crystals

ADAMS, M. J., BLUNDELL, T. L., DODSON, E. J., DODSON, G. G., VIJAYAN, M., BAKER, E. N., HARDING, M. M., HODGKIN, D. C., RIMMER, B., & SHEAT, S. (1969) · Nature · doi:10.1038/224491a0 · Cited by 503 · see citing works

Errors and alternatives in reading the universal genetic code

Parker, J. (1989) · Microbiological Reviews · doi:10.1128/mr.53.3.273-298.1989 · Cited by 457 · see citing works

From signal to pseudopod

Stossel, T. P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51454-x · Cited by 456 · see citing works

The influence of polyvalency on the binding properties of antibodies

Crothers, D. M., & Metzger, H. (1972) · Immunochemistry · doi:10.1016/0019-2791(72)90097-3 · Cited by 398 · see citing works

Structure-function relationships in dihydrolipoamide acyltransferases.

Reed, L. J., & Hackert, M. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38795-2 · Cited by 381 · see citing works

The Three-dimensional Crystal Structure of Cholera Toxin

Zhang, R., Scott, D. L., Westbrook, M. L., et al. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0456 · Cited by 352 · see citing works

STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Moras, D., Olsen, K., Sabesan, M. N., et al. (1975) · Worldwide Protein Data Bank · doi:10.2210/pdb1gpd/pdb · Cited by 330 · see citing works

Inside a living cell

Goodsell, D. S. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90083-8 · Cited by 328 · see citing works

Properties and metabolism of the aqueous cytoplasm and its boundaries

Clegg, J. S. (1984) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1984.246.2.r133 · Cited by 321 · see citing works

Quasi-equivalent viruses: a paradigm for protein assemblies 1 1Edited by T. Richmond

Johnson, J. E., & Speir, J. A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1068 · Cited by 315 · see citing works

How Proteins Recognize the TATA Box

Juo, Z. S., Chiu, T. K., Leiberman, P. M., et al. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0456 · Cited by 304 · see citing works

TRANSLATIONAL ACCURACY AND THE FITNESS OF BACTERIA

Kurland, C. G. (1992) · Annual Review of Genetics · doi:10.1146/annurev.ge.26.120192.000333 · Cited by 304 · see citing works

Human β-tryptase is a ring-like tetramer with active sites facing a central pore

Pereira, P. J. B., Bergner, A., Macedo‐Ribeiro, S., Huber, R., Matschiner, G., Fritz, H., Sommerhoff, C. P., & Bode, W. (1998) · Nature · doi:10.1038/32703 · Cited by 301 · see citing works

Quaternary Structure of Proteins

Klotz, I. M., Langebman, N. R., & Dahnall, D. W. (1970) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.39.070170.000325 · Cited by 298 · see citing works

The allosteric transition of glycogen phosphorylase

Barford, D., & Johnson, L. N. (1989) · Nature · doi:10.1038/340609a0 · Cited by 296 · see citing works

Modular organization of actin crosslinking proteins

Matsudalra, P. T. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90039-x · Cited by 281 · see citing works

Symmetry mismatch and DNA packaging in large bacteriophages.

Hendrix, R. W. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.10.4779 · Cited by 277 · see citing works

Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase

Moras, D., Olsen, K., Sabesan, M. N., et al. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40703-5 · Cited by 269 · see citing works

The response of T4 lysozyme to large‐to‐small substitutions within the core and its relation to the hydrophobic effect

Xu, J., Baase, W. A., Baldwin, E. P., & Matthews, B. W. (1998) · Protein Science · doi:10.1002/pro.5560070117 · Cited by 229 · see citing works

Morphology of protein–protein interfaces

Larsen, T. A., Olson, A. J., & Goodsell, D. S. (1998) · Structure · doi:10.1016/s0969-2126(98)00044-6 · Cited by 228 · see citing works

Computer Simulations of the Diffusion of a Substrate to an Active Site of an Enzyme

Sharp, K. A., Fine, R., & Honig, B. H. (1987) · Science · doi:10.1126/science.3589666 · Cited by 222 · see citing works

Microtubule Dynamics and Kinetochore Function in Mitosis

Mitchison, T. J. (1988) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.04.110188.002523 · Cited by 208 · see citing works

Structure of tomato bushy stunt virus IV

Olson, A. J., Bricogne, G., & Harrison, S. C. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80314-3 · Cited by 203 · see citing works

Change of waveform in bacterial flagella: The role of mechanics at the molecular level

Calldine, C. R. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90285-1 · Cited by 188 · see citing works

Symmetry and the energy landscapes of biomolecules

Wolynes, P. G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14249 · Cited by 187 · see citing works

Physical cluster mechanics: Statistical thermodynamics and nucleation theory for monatomic systems

Hoare, M. R., & Pal, P. (1975) · Advances In Physics · doi:10.1080/00018737500101481 · Cited by 184 · see citing works

Symmetry through the Eyes of a Chemist

Hargittai, I., & Hargittai, M. (1995) · Springer eBooks · doi:10.1007/b102498 · Cited by 159 · see citing works

Half-Site Reactivit

Seydoux, F. J., Malhotra, O. P., Bernhard, S. A., et al. (1974) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409237409105448 · Cited by 152 · see citing works

Heavy riboflavin synthase from Bacillus subtilis

Ladenstein, R., Schneider, M., Huber, R., et al. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90128-3 · Cited by 146 · see citing works

Three‐dimensional structure of the rotavirus haemagglutinin VP4 by cryo‐electron microscopy and difference map analysis.

Yeager, M. J., Berriman, J. A., Baker, T. S., et al. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06349.x · Cited by 140 · see citing works

Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition

Mattevi, A., Valentini, G., Rizzi, M., et al. (1995) · Structure · doi:10.1016/s0969-2126(01)00207-6 · Cited by 138 · see citing works

At Sixes and Sevens: Characterization of the Symmetry Mismatch of the ClpAP Chaperone-Assisted Protease

Beuron, F., Maurizi, M. R., Belnap, D. M., et al. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4039 · Cited by 136 · see citing works

Symmetry and Function of Biological Systems at the Macromolecular Level

Richards, F. F. (1970) · PubMed Central · Cited by 130 · see citing works

Deep-etch views of clathrin assemblies

Heuser, J., & Kirchhausen, T. L. (1985) · Journal of Ultrastructure Research · doi:10.1016/0889-1605(85)90123-5 · Cited by 129 · see citing works

Bacterial flagellar filaments and their component flagellins

Wilson, D. R., & Beveridge, T. J. (1993) · Canadian Journal of Microbiology · doi:10.1139/m93-066 · Cited by 113 · see citing works

Symmetry, stability, and dynamics of multidomain and multicomponent protein systems

Blundell, T. L., & Srinivasan, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14243 · Cited by 109 · see citing works

Mechanism and evolution of protein dimerization

Nussinov, R., Xu, D., & Tsai, C. (1998) · Protein Science · doi:10.1002/pro.5560070301 · Cited by 107 · see citing works

Soluble proteins: Size, shape and function

Goodsell, D. S., & Olson, A. J. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90153-e · Cited by 103 · see citing works

T and R states in the crystals of bacterial L–lactate dehydrogenase reveal the mechanism for allosteric control

Iwata, S., Kamata, K., Yoshida, S., Minowa, T., & Ohta, T. (1994) · Nature Structural Biology · doi:10.1038/nsb0394-176 · Cited by 96 · see citing works

THE REACTION WITH RED CELLS OF 7S RABBIT ANTIBODY, ITS SUB-UNITS AND THEIR RECOMBINANTS.

Greenbury, C. L., Moore, D. H., & Nunn, L. A. C. (1965) · PubMed · Cited by 88 · see citing works

Why are enzymes so big?

Srere, P. A. (1984) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(84)90221-4 · Cited by 87 · see citing works

Ricin subunit association. Thermodynamics and the role of the disulfide bond in toxicity.

Lewis, M. S., & Youle, R. J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67281-3 · Cited by 86 · see citing works

Protein crystals as a model for mitochondrial matrix proteins

Srere, P. A. (1981) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(81)90003-7 · Cited by 84 · see citing works

Protein Subunits: A Table

Klotz, I. M. (1967) · Science · doi:10.1126/science.155.3763.697 · Cited by 83 · see citing works

Transition of bacterial flagella from helical to straight forms with different subunit arrangements

Kamiya, R., Asakura, S., Wakabayashi, K., et al. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90199-2 · Cited by 75 · see citing works

Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding

Yang, M., Chen, X.-P., Militello, K. T., et al. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1149 · Cited by 74 · see citing works

The Quaternary Structure of Proteins Composed of Identical Subunits

Cornish-Bowden, A. J., & Koshland, D. E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62200-8 · Cited by 72 · see citing works

Quaternary Structure of Proteins

Klotz, I. M., Darnall, D. W., & Langerman, N. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-516301-9.50009-7 · Cited by 70 · see citing works

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-.ANG. resolution and neutral pH

Gouaux, J. E., & Lipscomb, W. N. (1990) · Biochemistry · doi:10.1021/bi00454a013 · Cited by 69 · see citing works

Constraints on the assembly of spherical virus particles

Rossmann, M. G. (1984) · Virology · doi:10.1016/0042-6822(84)90267-8 · Cited by 62 · see citing works

Form determination of the heads of bacteriophages

KELLENBERGER, E. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15568.x · Cited by 60 · see citing works

Principles and Problems of Biological Growth

Crane, H. R. (2019) · Routledge eBooks · doi:10.4324/9780429314148-8 · Cited by 59 · see citing works

Protein interactions. Aggregation of globular proteins

Pauling, L. C. (1953) · Discussions of the Faraday Society · doi:10.1039/df9531300170 · Cited by 57 · see citing works

Virus Structure: General Principles

Crick, F. H. C., & Watson, J. D. G. (2008) · Novartis Foundation symposium · doi:10.1002/9780470715239.ch1 · Cited by 51 · see citing works

Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.

Sträter, N., Hakansson, K., Schnappauf, G., Braus, G. H., & Lipscomb, W. N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3330 · Cited by 49 · see citing works

Symmetry of protein oligomers formed by isologous association

Hanson, K. R. (1966) · Journal of Molecular Biology · doi:10.1016/0022-2836(66)90149-5 · Cited by 44 · see citing works

Mass and Size of Protein Molecules

Svedberg, T. (1929) · Nature · doi:10.1038/123871a0 · Cited by 43 · see citing works

Morphogenetic core of the bacteriophage T4 head. Structure of the core in polyheads

Paulson, J. R., & Laemmli, U. K. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80064-8 · Cited by 41 · see citing works

New structures of allosteric proteins revealing remarkable conformational changes

Mattevi, A., Rizzi, M., & Bolognesi, M. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80013-3 · Cited by 36 · see citing works

Symmetries throughout organic evolution

Garcı́a-Bellido, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14229 · Cited by 33 · see citing works

DNA Polymerase III: Running Rings around the Fork

Herendeen, D. R., & Kelly, T. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80069-0 · Cited by 31 · see citing works

On symmetry and function in biological systems

Monod, J. (1978) · Elsevier eBooks · doi:10.1016/b978-0-12-460482-7.50061-0 · Cited by 26 · see citing works

Intrinsic versus imposed curvature in cyclical oligomers: the portal protein of bacteriophage SPP1.

van Heel, M., Orlova, E. V., Dube, P., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00858.x · Cited by 21 · see citing works

The evolution of function in enzymes.

Koshland, D. E. (1976) · PubMed · Cited by 20 · see citing works

Kinetic co‐operativity of monomeric mnemonical enzymes

Ricard, J., & Noat, G. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb09231.x · Cited by 19 · see citing works

Enzymes with asymmetrically arranged subunits

Degani, Y., & Degani, C. (1980) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(80)90146-2 · Cited by 18 · see citing works

Protein Structure: Why have six-fold symmetry?

Kelman, Z., Finkelstein, J., & O’Donnell, M. E. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00247-8 · Cited by 16 · see citing works

Structural aspects of allostery

Evans, P. R. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90178-v · Cited by 15 · see citing works

On the influence of polyvalent ligands on membrane curvature

Hewitt, J. A. (1977) · Journal of Theoretical Biology · doi:10.1016/0022-5193(77)90282-x · Cited by 14 · see citing works

On the Structure of the Scaffolding Core of Bacteriophage T4 and Its Role in Head Length Determination

Berger, B., & Shor, P. W. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3942 · Cited by 7 · see citing works

Broadly applicable and accurate protein design by integrating structure prediction networks and diffusion generative models

Watson, J. L., Juergens, D., Bennett, N. R., Trippe, B. L., Yim, J., Eisenach, H. E., Ahern, W., Borst, A. J., Ragotte, R. J., Milles, L. F., et al. (2022) · doi:10.1101/2022.12.09.519842 · Cited by 2,369 · see citing works

De novo design of protein structure and function with RFdiffusion

Watson, J. L., Juergens, D., Bennett, N. R., Trippe, B. L., Yim, J., Eisenach, H. E., Ahern, W., Borst, A. J., Ragotte, R. J., Milles, L. F., et al. (2023) · Nature · doi:10.1038/s41586-023-06415-8 · Cited by 2,325 · see citing works

Demystifying Heparan Sulfate–Protein Interactions

Xu, D., & Esko, J. D. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035314 · Cited by 805 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

Hallucinating symmetric protein assemblies

Wicky, B. I. M., Milles, L. F., Courbet, A., Ragotte, R. J., Dauparas, J., Kinfu, E., Tipps, S., Kibler, R. D., Baek, M., DiMaio, F., et al. (2022) · Science · doi:10.1126/science.add1964 · Cited by 240 · see citing works

An atlas of protein homo-oligomerization across domains of life

Schweke, H., Pacesa, M., Levin, T., Goverde, C. A., Kumar, P., Duhoo, Y., Dornfeld, L. J., Dubreuil, B., Georgeon, S., Ovchinnikov, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.01.022 · Cited by 144 · see citing works

A hydrophobic ratchet entrenches molecular complexes

Hochberg, G. K. A., Liu, Y., Marklund, E. G., Metzger, B. P. H., Laganowsky, A., & Thornton, J. W. (2020) · Nature · doi:10.1038/s41586-020-3021-2 · Cited by 134 · see citing works

iAlign: a method for the structural comparison of protein–protein interfaces

Gao, M., & Skolnick, J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq404 · Cited by 98 · see citing works

Copper/Zinc Superoxide Dismutase in Human Skin: Current Knowledge

Altobelli, G. G., Van Noorden, S., Balato, A., & Cimini, V. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00183 · Cited by 84 · see citing works

Integrative structure modeling of macromolecular assemblies from proteomics data

Lasker, K., Phillips, J. L., Russel, D., Velázquez-Muriel, J., Schneidman-Duhovny, D., Tjioe, E., Webb, B., Schlessinger, A., & Sali, A. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r110.000067 · Cited by 71 · see citing works

Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins

Natan, E., Endoh, T., Haim-Vilmovsky, L., Flock, T., Chalancon, G., Hopper, J. T. S., Kintses, B., Horvath, P., Daruka, L., Fekete, G., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0029-5 · Cited by 56 · see citing works

Accurate prediction of protein assembly structure by combining AlphaFold and symmetrical docking

Jeppesen, M., & André, I. (2023) · Nature Communications · doi:10.1038/s41467-023-43681-6 · Cited by 44 · see citing works

Flexible backbone assembly and refinement of symmetrical homomeric complexes

Roy Burman, S. S., Yovanno, R. A., & Gray, J. J. (2019) · Structure · doi:10.1016/j.str.2019.03.014 · Cited by 18 · see citing works

Protein oligomer modeling guided by predicted interchain contacts in <scp>CASP14</scp>

Baek, M., Anishchenko, I., Park, H., Humphreys, I. R., & Baker, D. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26197 · Cited by 18 · see citing works

Toward an understanding of the sequence and structural basis of allosteric proteins

Li, X., Chen, Y., Lu, S., Huang, Z., Liu, X., Wang, Q., Shi, T., & Zhang, J. (2013) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2012.12.011 · Cited by 28 · see citing works

Analysis of tractable allosteric sites in G protein-coupled receptors

Wakefield, A., Mason, J. S., Vajda, S., & Keserű, G. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-42618-8 · Cited by 45 · see citing works

ASD v2.0: updated content and novel features focusing on allosteric regulation

Huang, Z., Mou, L., Shen, Q., Lu, S., Li, C., Liu, X., Wang, G., Li, S., Geng, L., Liu, Y., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1247 · Cited by 102 · see citing works

Allosteric sites: remote control in regulation of protein activity

Guarnera, E., & Berezovsky, I. N. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.10.004 · Cited by 149 · see citing works

Toward understanding the molecular basis for chemical allosteric modulator design

Wang, Q., Zheng, M., Huang, Z., Liu, X., Zhou, H., Chen, Y., Shi, T., & Zhang, J. (2012) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2012.07.006 · Cited by 40 · see citing works