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Inference of Macromolecular Assemblies from Crystalline State
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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
Hermann, R. B. (1972) · The Journal of Physical Chemistry · doi:10.1021/j100663a023 · Cited by 700
Research works printed but not linked: 107
- Fermi, 1984, The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution, J. Mol. Biol., 175, 159, 10.1016/0022-2836(84)90472-8 · DOI · Paper page
- Svergun, 2002, Advances in structure analysis using small-angle scattering in solution, Curr. Opin. Struct. Biol., 12, 654, 10.1016/S0959-440X(02)00363-9 · DOI
- Berman, 2000, The Protein Data Bank, Nucleic Acids Res., 28, 235, 10.1093/nar/28.1.235 · DOI · Paper page
- Ponstingl, 2000, Discriminating between homodimeric and monomeric proteins in the crystalline state, Proteins: Struct. Funct. Genet., 41, 47, 10.1002/1097-0134(20001001)41:1<47::AID-PROT80>3.0.CO;2-8 · DOI
- Henrick, 1998, PQS: a protein quaternary structure file server, Trends Biochem. Sci., 23, 358, 10.1016/S0968-0004(98)01253-5 · DOI · Paper page
- Ponstingl, 2003, Automatic inference of protein quaternary structure from crystals, J. Appl. Crystallogr., 36, 1116, 10.1107/S0021889803012421 · DOI
- Argos, 1988, An investigation of protein subunit and domain interfaces, Protein Eng., 2, 101, 10.1093/protein/2.2.101 · DOI
- Janin, 1990, The structure of protein–protein recognition sites, J. Biol. Chem., 265, 16027, 10.1016/S0021-9258(17)46181-3 · DOI · Paper page
- Jones, 1995, Protein-protein interactions: a review of protein dimer structures, Prog. Biophys. Mol. Biol., 63, 31, 10.1016/0079-6107(94)00008-W · DOI
- Miller, 1989, The structure of interfaces between subunits ofdimeric and tetrameric proteins, Protein Eng., 3, 77, 10.1093/protein/3.2.77 · DOI
- Padlan, 1990, On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands, Proteins: Struct. Funct. Genet., 7, 112, 10.1002/prot.340070203 · DOI
- Glaser, 2006, A method for localizing ligand binding pockets in protein structures, Proteins: Struct. Funct. Genet., 62, 479, 10.1002/prot.20769 · DOI
- Gutteridge, 2005, Understanding nature's catalytic toolkit, Trends Biochem. Sci., 30, 622, 10.1016/j.tibs.2005.09.006 · DOI
- Gutteridge, 2003, Using a neural network and spatial clustering to predict the location of active sites in enzymes, J. Mol. Biol., 330, 719, 10.1016/S0022-2836(03)00515-1 · DOI
- Tsai, 1996, Protein-protein interfaces: architectures and interactions in protein–protein interfaces and in protein cores. Their similarities and differences, Crit. Rev. Biochem. Mol. Biol., 31, 127, 10.3109/10409239609106582 · DOI
- Lo Conte, 1999, The atomic structure of protein–protein recognition sites, J. Mol. Biol., 285, 2177, 10.1006/jmbi.1998.2439 · DOI
- Chakrabarti, 2002, Dissecting protein–protein recognition sites, Proteins: Struct. Funct. Genet., 47, 334, 10.1002/prot.10085 · DOI · Paper page
- Keskin, 2004, A new, structurally nonredundant, diverse data set of protein interfaces and its implications, Protein Sci., 13, 1043, 10.1110/ps.03484604 · DOI
- Ogmen, 2005, PRISM: protein interactions by structural matching, Nucleic Acids Res., 33, W331, 10.1093/nar/gki585 · DOI
- Preiβner, 1998, Dictionary of interfaces in proteins (DIP). Data bank of complementary molecular surface patches, J. Mol. Biol., 280, 535, 10.1006/jmbi.1998.1878 · DOI
- Gong, 2005, A protein domain interaction interface database: InterPare, BMC Bioinformatics, 6, 207, 10.1186/1471-2105-6-207 · DOI
- Baker, 1984, Hydrogen bonding in globular proteins, Prog. Biophys. Mol. Biol., 44, 97, 10.1016/0079-6107(84)90007-5 · DOI
- Janin, 1988, Surface, subunit interfaces and interior of oligomeric proteins, J. Mol. Biol., 204, 155, 10.1016/0022-2836(88)90606-7 · DOI
- Horton, 1992, Calculation of the free energy of association for protein complexes, Protein Sci., 1, 169, 10.1002/pro.5560010117 · DOI
- Janin, 1995, Protein–protein interaction at crystal contacts, Proteins: Struct. Funct. Genet., 23, 580, 10.1002/prot.340230413 · DOI · Paper page
- Amidon, 1975, Solubility of nonelectrolytes in polar solvents. V. Estimation of the solubility of aliphatic monofunctional compounds in water using a molecular surface area approach, J. Phys. Chem., 79, 2239, 10.1021/j100588a008 · DOI
- Floris, 1989, Evaluation of the dispersion contribution to the solvation energy. A simple computational model in the continuum approximation, J. Comp. Chem., 10, 616, 10.1002/jcc.540100504 · DOI
- Born, 1920, Volumes and heats of hydration of ions, Z. Phys., 1, 45, 10.1007/BF01881023 · DOI · Paper page
- You, 1995, Conformation and hydrogen ion titration of proteins: a continuum electrostatic model with conformational flexibility, Biophys. J., 69, 1721, 10.1016/S0006-3495(95)80042-1 · DOI
- McDonald, 1994, Satisfying hydrogen bonding potential in proteins, J. Mol. Biol., 238, 777, 10.1006/jmbi.1994.1334 · DOI
- Bahadur, 2003, Dissecting subunit interfaces in homodimeric proteins, Proteins: Struct. Funct. Genet., 53, 708, 10.1002/prot.10461 · DOI
- Xu, 1997, Hydrogen bonds and salt bridges across protein–protein interfaces, Protein Eng., 10, 999, 10.1093/protein/10.9.999 · DOI · Paper page
- Pace, 1996, Forces contributing to the conformational stability of proteins, FASEB J., 10, 75, 10.1096/fasebj.10.1.8566551 · DOI
- Fersht, 1987, The hydrogen bond in molecular recognition, Trends Biochem. Sci., 12, 3214, 10.1016/0968-0004(87)90146-0 · DOI
- Horovitz, 1990, Strength and co-operativity of contributions of surface salt bridges to protein stability, J. Mol. Biol., 216, 1031, 10.1016/S0022-2836(99)80018-7 · DOI
- Akke, 1990, Protein stability and electrostatic interactions between solvent exposed charged side chains, Proteins: Struct. Funct. Genet., 8, 23, 10.1002/prot.340080106 · DOI
- Betz, 1993, Disulphide bonds and the stability of globular proteins, Protein Sci., 2, 1551, 10.1002/pro.5560021002 · DOI · Paper page
- Clarke, 1993, Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation, Biochemistry, 32, 4322, 10.1021/bi00067a022 · DOI · Paper page
- Zauhar, 1985, A new method for computing the macromolecular electric potential, J. Mol. Biol., 186, 815, 10.1016/0022-2836(85)90399-7 · DOI · Paper page
- Gilson, 1987, Calculating the electrostatic potential of molecules in solution: method and error assessment, J. Comp. Chem., 9, 327, 10.1002/jcc.540090407 · DOI
- Davis, 1989, Solving the finite difference linearized Poisson–Boltzmann equation: a comparison of relaxation and conjugated gradient methods, J. Comp. Chem., 10, 386, 10.1002/jcc.540100313 · DOI
- Davis, 1990, Electrostatics in biomolecular structure and dynamics, Chem. Rev., 90, 509, 10.1021/cr00101a005 · DOI · Paper page
- Sharp, 1990, Electrostatic interactions in macromolecules: theory and applications, Annu. Rev. Biophys. Biophys. Chem., 19, 301, 10.1146/annurev.bb.19.060190.001505 · DOI
- Still, 1990, Semianalytical treatment of solvation for molecular mechanics and dynamics, J. Am. Chem. Soc., 112, 6127, 10.1021/ja00172a038 · DOI
- Nicholls, 1991, A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson–Boltzmann equation, J. Comp. Chem., 12, 435, 10.1002/jcc.540120405 · DOI
- Davis, 1991, Dielectric boundary smoothing in finite difference solutions of the Poisson equation: an approach to improve accuracy and convergence, J. Comp. Chem., 12, 909, 10.1002/jcc.540120718 · DOI
- Zhou, 1993, Boundary element solution of macromolecular electrostatics: interaction energy between two proteins, Biophys. J., 65, 955, 10.1016/S0006-3495(93)81094-4 · DOI
- You, 1993, Finite element approach to the electrostatics of macromolecules with arbitrary geometries, J. Comp. Chem., 14, 484, 10.1002/jcc.540140413 · DOI
- Purisima, 1995, A simple yet accurate boundary element method for continuum dielectric calculations, J. Comp. Chem., 16, 681, 10.1002/jcc.540160604 · DOI
- Zaloj, 1998, Diffusion approach to the linear Poisson–Boltzmann equation, Chem. Phys. Lett., 284, 76, 10.1016/S0009-2614(97)01364-X · DOI
- Bashford, 2000, Generalized Born models of macromolecular solvation effects, Annu. Rev. Phys. Chem., 51, 129, 10.1146/annurev.physchem.51.1.129 · DOI · Paper page
- Chothia, 1974, Hydrophobic bonding and accessible surface areas in proteins, Nature, 248, 338, 10.1038/248338a0 · DOI · Paper page
- Eisenberg, 1986, Solvation energy in protein folding and binding, Nature, 319, 199, 10.1038/319199a0 · DOI · Paper page
- Ooi, 1987, Accessible surface areas as a measure of thermodynamic parameters of hydration of peptides, Proc. Natl Acad. Sci. USA, 84, 3086, 10.1073/pnas.84.10.3086 · DOI · Paper page
- Vila, 1991, Empirical solvation models can be used to differentiate native from near-native conformations of bovine pancreatic trypsin inhibitors, Proteins: Struct. Funct. Genet., 10, 199, 10.1002/prot.340100305 · DOI
- Wesson, 1992, Atomic solvation parameters applied to molecular dynamics of proteins in solution, Protein Sci., 1, 227, 10.1002/pro.5560010204 · DOI
- Juffer, 1995, Comparison of atomic solvation parametric sets: applicability and limitations in protein folding and binding, Protein Sci., 4, 2499, 10.1002/pro.5560041206 · DOI
- Wang, 2001, Solvation model based on weighted solvent accessible surface area, J. Phys. Chem., B, 105, 5055, 10.1021/jp0102318 · DOI
- Hou, 2002, Empirical aqueoues solvation models based on accessible surface areas with implicit electrostatics, J. Phys. Chem., B, 106, 11295, 10.1021/jp025595u · DOI
- Jackson, 1998, Rapid refinement of protein interfaces incorporating solvation: application to the docking problem, J. Mol. Biol., 276, 265, 10.1006/jmbi.1997.1519 · DOI
- Page, 1971, Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect, Proc. Natl Acad. Sci. USA, 68, 1678, 10.1073/pnas.68.8.1678 · DOI · Paper page
- Murray, 2002, The consequences of translational and rotational entropy lost by small molecules on binding to proteins, J. Comput.-Aided Mol. Des., 16, 741, 10.1023/A:1022446720849 · DOI
- Mammen, 1998, Estimating the entropic cost of self-assembly of multiparticle hydrogen-bonded aggregates based on the cyanuric acid melamine lattice, J. Org. Chem., 63, 3821, 10.1021/jo970944f · DOI
- Finkelstein, 1989, The price of lost freedom: entropy of bimolecular complex formation, Protein Eng., 3, 1, 10.1093/protein/3.1.1 · DOI
- Minh, 2005, The entropic cost of protein–protein association: a case study on Acetylcholinesterase binding to Fasciculin-2, Biophys. J., 89, L25, 10.1529/biophysj.105.069336 · DOI
- Krissinel, 2004, Common subgraph isomorphism detection by backtracking search, Softw. Pract. Exp., 34, 591, 10.1002/spe.588 · DOI
- Murakami, 2006, Inhibition of myotoxic activity of bothrops asper myotoxin II by the anti-trypanosomal drug suramin, J. Mol. Biol., 350, 416, 10.1016/j.jmb.2005.04.072 · DOI
- Schuetz, 2007, Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by Suramin, Structure, 15, 377, 10.1016/j.str.2007.02.002 · DOI · Paper page
- Evdokimov, 2001, Unusual molecular architecture of the Yersinia pestis Cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit, J. Mol. Biol., 312, 807, 10.1006/jmbi.2001.4973 · DOI
- Luscombe, 2000, An overview of the structures of protein–DNA complexes, Genome Biol., 1, 1, 10.1186/gb-2000-1-1-reviews001 · DOI
- Krissinel, 2004, Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions, Acta Crystallogr., D, 60, 2256, 10.1107/S0907444904026460 · DOI
- Giudice, 2003, Base pair opening within B-DNA: free energy pathways for GC and AT pairs from umbrella sampling simulations, Nucleic Acids Res., 31, 1434, 10.1093/nar/gkg239 · DOI
- Rossmann, 2004, The bacteriophage T4 DNA injection machine, Curr. Opin. Struct. Biol., 14, 171, 10.1016/j.sbi.2004.02.001 · DOI
- Rowsell, 1997, Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy, Structure, 5, 337, 10.1016/S0969-2126(97)00191-3 · DOI
- DiTusa, 2001, Thermodynamics of metal ion binding. 1. Metal ion binding by wild-type carbonic anhydrase, Biochemistry, 40, 5338, 10.1021/bi001731e · DOI
- Lubkowski, 1999, Decamers observed in the crystals of bovine pancreatic trypsin inhibitor, Acta Crystallogr., D, 55, 335, 10.1107/S0907444998011068 · DOI
- Wu, 1994, Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein, Structure, 2, 545, 10.1016/S0969-2126(00)00054-X · DOI
- Lustbader, 1993, The application of chemical studies of human chorionic gonadotropin to visualize its three-dimensional structure, Endocr. Rev., 14, 291
- Littlefield, 1999, The structural basis for the oriented assembly of a TBP/TFB/promoter complex, Biochemistry, 96, 13668
- Guo, 1997, Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse, Nature, 389, 40, 10.1038/37925 · DOI · Paper page
- Fujinaga, 1987, Rat submaxillary gland serine protease, tonin structure solution and refinement at 1.8 Å resolution, J. Mol. Biol., 195, 373, 10.1016/0022-2836(87)90658-9 · DOI
- Evdokimov, 2001, Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit, J. Mol. Biol., 312, 807, 10.1006/jmbi.2001.4973 · DOI
- Haramis, 2006, Selectivity and promiscuity in Eph receptors, Structure, 14, 169, 10.1016/j.str.2006.01.005 · DOI
- Golovin, 2004, E-MSD: an integrated data resource for bioinformatics, Nucleic Acids Res., 32, D211, 10.1093/nar/gkh078 · DOI
- Hunt, 1997, Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage, Cell, 90, 361, 10.1016/S0092-8674(00)80343-8 · DOI
- Almog, 2004, Three-dimensional structure of the R115E mutant of T4-bacteriophage 2′-deoxycytidylate deaminase, Biochemistry, 43, 13715, 10.1021/bi048928h · DOI
- Kanamaru, 2002, Structure of the cell-puncturing device of bacteriophage T4, Nature, 415, 553, 10.1038/415553a · DOI
- Van Raaij, 2001, Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre, J. Mol. Biol., 314, 1137, 10.1006/jmbi.2000.5204 · DOI
- Lariviere, 2002, A base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition-state analog, J. Mol. Biol., 324, 483, 10.1016/S0022-2836(02)01091-4 · DOI
- Leiman, 2000, Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers, J. Mol. Biol., 301, 975, 10.1006/jmbi.2000.3989 · DOI
- Thomassen, 2003, The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold, J. Mol. Biol., 331, 361, 10.1016/S0022-2836(03)00755-1 · DOI
- Kostyuchenko, 1999, The structure of bacteriophage T4 gene product 9: the trigger for tail contraction, Struct. Fold Des., 7, 1213, 10.1016/S0969-2126(00)80055-6 · DOI
- Moarefi, 2000, Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage, J. Mol. Biol., 296, 1215, 10.1006/jmbi.1999.3511 · DOI
- Papanikolopoulou, 2004, Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif, J. Mol. Biol., 342, 219, 10.1016/j.jmb.2004.07.008 · DOI
- Leiman, 2006, Evolution of bacteriophage tails: structure of T4 gene product 10, J. Mol. Biol., 358, 912, 10.1016/j.jmb.2006.02.058 · DOI
- Leiman, 2003, Structure and location of gene product 8 in the bacteriophage T4 baseplate, J. Mol. Biol., 328, 821, 10.1016/S0022-2836(03)00366-8 · DOI
- Raaijmakers, 2001, Conformational flexibility in T4 endonuclease VII revealed by crystallography: implications for substrate binding and cleavage, J. Mol. Biol., 308, 311, 10.1006/jmbi.2001.4592 · DOI
- Raaijmakers, 1999, X-ray structure of T4 endonuclease VII: a DNA junction resolvase with a novel fold and unusual domain-swapped dimer architecture, EMBO J., 18, 1447, 10.1093/emboj/18.6.1447 · DOI
- Finnin, 1997, The activation domain of the MotA transcription factor from bacteriophage T4, EMBO J., 16, 1992, 10.1093/emboj/16.8.1992 · DOI
- Mueser, 2000, Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 Å resolution crystal structure reveals a novel alpha-helical two-domain fold, J. Mol. Biol., 296, 597, 10.1006/jmbi.1999.3438 · DOI
- Morera, 1999, T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism, J. Mol. Biol., 292, 717, 10.1006/jmbi.1999.3094 · DOI
- He, 2004, Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation, Protein Sci., 10, 2716, 10.1110/ps.04875504 · DOI
- Sickmier, 2004, The crystal structure of the UvsW helicase from bacteriophage T4, Structure, 12, 583, 10.1016/j.str.2004.02.016 · DOI
- Lariviere, 2003, Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism, J. Mol. Biol., 330, 1077, 10.1016/S0022-2836(03)00635-1 · DOI
- Morera, 2001, High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding, J. Mol. Biol., 311, 569, 10.1006/jmbi.2001.4905 · DOI
- Park, 2002, Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV, Proteins: Struct. Funct. Genet., 49, 49, 10.1002/prot.10199 · DOI
- Li, 2002, The MotA transcription factor from bacteriophage T4 contains a novel DNA-binding domain: the ‘double wing’ motif, Mol. Microbiol., 43, 1079, 10.1046/j.1365-2958.2002.02809.x · DOI
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Jia, C., Yang, X., Zhao, M.-H., Tan, Y., & Xiao, J. (2026) · Science Advances · doi:10.1126/sciadv.adz5404 · Cited by 5
Frey, A. F., Schwan, M., Weldert, A. C., Kadenbach, V., Kopp, J., Nidoieva, Z., Zimmermann, R. A., Gleue, L., Zimmer, C., Jörg, M., et al. (2025) · iScience · doi:10.1016/j.isci.2025.113300 · Cited by 5
Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism
Caveney, N. A., Tsutsumi, N., & Garcia, K. C. (2023) · eLife · doi:10.7554/elife.86784 · Cited by 5
Mahony, J., Goulet, A., van Sinderen, D., & Cambillau, C. (2023) · Viruses · doi:10.3390/v15122440 · Cited by 5
Structural basis for Salmonella infection by two Microviridae phages
Hu, W., Liu, Z., Wei, Y., Bian, Q., Lan, W., Fan, C., Song, J., Sun, Q., Zhang, X., Liu, Y., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08595-7 · Cited by 4
Dudziak, A., Pleuger, R., Schmidt, J., Hamm, F., Tendulkar, S., Jänen, K., Vetter, I. R., Singh, S., Fischböck, J., Herzog, F., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00437-w · Cited by 4
Molecular exaptation by the integrin αI domain
Hollis, J. A., Chan, M. C., Malik, H. S., & Campbell, M. G. (2025) · Science Advances · doi:10.1126/sciadv.adx9567 · Cited by 4
Curvature Generation and Engineering Principles from Shewanella oneidensis Multi-flagellin Flagellum
Lou, Q., Fan, H., Liu, Y., Miller, J. F., Huang, Y., & Zhou, Z. H. (2025) · ACS Nano · doi:10.1021/acsnano.5c02744 · Cited by 4
Degron-independent recruitment of KAT2A expands the target space of CRBN molecular glues
Ojeda, S., Wang, M., Baek, K., Bourgeois, W., Sommerschield, A., Yue, H., Metivier, R. J., Karagiannis, P., Levitz, T. S., Xiong, Y., et al. (2026) · Science · doi:10.1126/science.aef5391 · Cited by 5
Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus
Burmeister, W. P., Boutin, L., Balestra, A. C., Gröger, H., Ballandras-Colas, A., Hutin, S., Kraft, C., Grimm, C., Böttcher, B., Fischer, U., et al. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011652 · Cited by 3
Protein Quaternary Structures in Solution are a Mixture of Multiple forms
Marciano, S., Dey, D., Listov, D., Fleishman, S. J., Sonn-Segev, A., Mertens, H., Busch, F., Kim, Y., Harvey, S. R., Wysocki, V. H., et al. (2022) · doi:10.1101/2022.03.30.486392 · Cited by 3
EGGNet, a Generalizable Geometric Deep Learning Framework for Protein Complex Pose Scoring
Wang, Z., Brand, R., Adolf-Bryfogle, J., Grewal, J., Qi, Y., Combs, S. A., Golovach, N., Alford, R., Rangwala, H., & Clark, P. M. (2024) · ACS Omega · doi:10.1021/acsomega.3c04889 · Cited by 3
Hay, I. M., Mulholland, K. E., Lai, T., Graham, S. C., Sharpe, H. J., & Deane, J. E. (2022) · eLife · doi:10.7554/elife.79855 · Cited by 3
Turvey, S., Muench, S. P., Issad, T., Fishwick, C. W. G., Kearney, M. T., & Simmons, K. J. (2024) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2024.101607 · Cited by 3
Exploring the structural assembly of rice ADP-glucose pyrophosphorylase subunits using MD simulation
Maharana, J., Hwang, S.-K., Singha, D. L., Panda, D., Singh, S., Okita, T. W., & Modi, M. K. (2024) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2024.108761 · Cited by 3
Design principles of a membrane-spanning ubiquitin ligase
Williams, C., Nocka, L. M., Hedger, G., Parashara, P., Pardon, E., Latorraca, N. R., Pusapati, G. V., Sarkar, P., Lartey, D., Gao, L., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.001 · Cited by 3
Harnessing Photosynthetic ATP for Whole-Cell Biocatalysis in the Cyanobacterium Synechocystis
Loprete, G., Traverso, E., Vascon, F., Botteri, M., Robescu, M. S., Ubiali, D., Cendron, L., Morosinotto, T., & Bergantino, E. (2025) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.5c07236 · Cited by 2
GPCRchimeraDB: A Database of Chimeric G Protein-Coupled Receptors (GPCRs) to Assist Their Design
Crauwels, C., Díaz, A., & Vranken, W. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169164 · Cited by 2
Reprogramming of bacterial virulence by lysine acetylation
Schmöker, O., Girbardt, B., Schulze, S., Palm, G. J., Berndt, L., Hoppen, J., Kara, N., Schöps, X., Al-Abdulla, R., Garz, K., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72244-8 · Cited by 2
Evolutionary Adaptation of an HP1-protein Chromodomain Integrates Chromatin and DNA Sequence Signals
Baumgartner, L., Ipsaro, J. J., Hohmann, U., Handler, D., Schleiffer, A., Duchek, P., & Brennecke, J. (2023) · doi:10.1101/2023.09.29.560096 · Cited by 2
Bi-allelic variants in WDR47 cause a complex neurodevelopmental syndrome
Bayam, E., Tilly, P., Collins, S. C., Rivera Alvarez, J., Kannan, M., Tonneau, L., Brivio, E., Rinaldi, B., Lecat, R., Schwaller, N., et al. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00178-z · Cited by 2
Le Moigne, T., Santoni, M., Jomat, L., Lemaire, S. D., Zaffagnini, M., Chéron, N., & Henri, J. (2025) · eLife · doi:10.7554/elife.87196 · Cited by 2
Hammerstad, M., Steinvik, E., & Hersleth, H.-P. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103937 · Cited by 1
“PDBePISA [69] was used to confirm that NmbA is a biological monomer, despite having two monomers in the asymmetric unit, since analysis of the protein interfaces did not reveal any specific interactions that could result in the formation of a stable quaternary structure.”
Asymmetric horseshoe-like assembly of peroxisomal Yeast Oxalyl-CoA synthetase
Bürgi, J., Lill, P., Giannopoulou, E.-A., Jeffries, C. M., Chojnowski, G., Raunser, S., Gatsogiannis, C., & Wilmanns, M. (2022) · doi:10.1101/2022.08.30.505785 · Cited by 1
HSV ‐1 ICP0 dimer domain adopts a novel β‐barrel fold
(2024) · doi:10.1002/prot.26673 · Cited by 1
Dodge, G. J., Anderson, A. J., He, Y., Liu, W., Viner, R., & Imperiali, B. (2023) · doi:10.1101/2023.06.16.545297 · Cited by 1
Cryo‐EM structures of multiple‐peptide resistance factor ( MprF ) from Pseudomonas aeruginosa
Jha, S., & Vinothkumar, K. R. (2026) · The FEBS Journal · doi:10.1111/febs.70519 · Cited by 1
Tetramerisation governs SALL transcription factor function in development and disease
Giuliani, S., Chhatbar, K., Wear, M., Guy, J., Mathieson, T., Burdett, H., George, L., Alston, G., Spanos, C., McHugh, T., et al. (2025) · bioRxiv · doi:10.1101/2025.10.27.684836
Lefebvre, D., Soscia, C., Schmitt, L., Goulet, A., Ize, B., & Bleves, S. (2025) · doi:10.64898/2025.12.24.696360
Development and structure-guided characterization of a novel ACE2-binding macrocyclic peptide
Benoit, R. M., Wang, J., Beyer, D., Abbas, A., Rodrigues, M. J., Wieser, M. M., Deupi, X., Müller, C., Suga, H., & Bode, J. W. (2026) · Journal of Structural Biology: X · doi:10.1016/j.yjsbx.2026.100145
“A surface area of 1142.5 Å 2 is buried at the peptide-protein interface, according to analysis with PDBePISA (Krissinel and Henrick, 2007).”
InfluentialStructural and mechanistic insights into the constitutive Themis–Grb2 complex in T cell signalling
Clancy, D. M., Sanz-Sanjuan, A., Gilis, E., Tougaard, P., Velghe, I., Van Droogenbroeck, Y., Felix, J., Bloch, Y., Cuadrado, Á. F., Merceron, R., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-73359-8
Contrasting functions of ATP hydrolysis by MDA5 and LGP2 in viral RNA sensing
Singh, R., Wu, Y., Herrero del Valle, A., Leigh, K. E., Cheng, M. T. K., Ferguson, B. J., & Modis, Y. (2023) · doi:10.1101/2023.05.25.542247
eIFiso4G editing confers high and broad-spectrum resistance against rice yellow mottle virus
Auguy, F., Chéron, S., Dossou, L., Pinel-Galzi, A., Thomas, E., Aribi, J., Celli, M. G., Cunnac, S., Hébrard, E., & Albar, L. (2026) · Peer Community Journal · doi:10.24072/pcjournal.740
The phage protein paratox is a multifunctional metabolic regulator of Streptococcus
Muna, T. H., Rutbeek, N. R., Horne, J., Lao, Y. W., Krokhin, O. V., & Prehna, G. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkae1200
Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism
Caveney, N. A., Tsutsumi, N., & Garcia, K. C. (2023) · doi:10.7554/elife.86784.2
Mukhtar, O., Dutt, R., Panda, A., Kumari, P., Singh, S. S., Paul, G., Prakash, N., Abbas, M., Islam, M. M., Arora, P., et al. (2026) · eLife · doi:10.7554/elife.110942
Lefebvre, D., Soscia, C., Schmitt, L., Goulet, A., Ize, B., & Bleves, S. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111416
Mukhtar, O., Dutt, R., Panda, A., Kumari, P., Singh, S. S., Paul, G., Prakash, N., Abbas, M., Islam, M. M., Arora, P., et al. (2026) · eLife · doi:10.7554/elife.110942.3
Metadata
- Authors
- Krissinel, E., & Henrick, K.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2007-09
- Volume
- 372
- Issue
- 3
- Pages
- 774-797
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2035503835
- Cited by
- 9,984
- References
- 2
- FWCI
- 124.87
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Funders
- Biotechnology and Biological Sciences Research Council
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.