The relation between the divergence of sequence and structure in proteins.

The protein data bank: A computer-based archival file for macromolecular structures

Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,574

The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution

Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90472-8 · Cited by 770

The Protein Data Bank

Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., RODGERS, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11885.x · Cited by 763

Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.

Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C., & Kraut, J. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33497-5 · Cited by 746

How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins

Lesk, A. M., & Chothia, C. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90373-3 · Cited by 712

Structure and refinement of oxymyoglobin at 1·6 Å resolution

Phillips, S. E. V. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90262-4 · Cited by 643

Conformation change of cytochrome c

Takano, T., & Dickerson, R. E. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90529-5 · Cited by 557

Structure of oxidized poplar plastocyanin at 1·6 Å resolution

Guss, J. M., & Freeman, H. C. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80064-3 · Cited by 507

Structure of bovine pancreatic trypsin inhibitor

Wlodawer, A., WALTER, J., Huber, R., & Sjölin, L. (1984) · Journal of Molecular Biology · doi:10.1016/s0022-2836(84)80006-6 · Cited by 478

Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution

Marquart, M., Deisenhofer, J., Huber, R., & Palm, W. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90252-1 · Cited by 457

The Relationship Between Sequence and Interaction Divergence in Proteins

Aloy, P., Ceulemans, H., Stark, A., & Russell, R. B. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.006 · Cited by 309

Multiple alignment using hidden Markov models.

Eddy, S. R. (1995) · PubMed · Cited by 307

The Protein Folding Problem

Chan, H. S., & Dill, K. A. (1993) · Physics Today · doi:10.1063/1.881371 · Cited by 309

Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences

Lemesle-Varloot, L., Henrissat, B., Gaboriaud, C., Bissery, V., Morgat, A., & Mornon, J. (1990) · Biochimie · doi:10.1016/0300-9084(90)90120-6 · Cited by 298

Protein fold recognition by prediction-based threading

Rost, B., Schneider, R., & Sander, C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1101 · Cited by 298

Comparative modeling for protein structure prediction

Ginalski, K. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.02.003 · Cited by 296

Derivation of rules for comparative protein modeling from a database of protein structure alignments

Šali, A., & Overington, J. P. (1994) · Protein Science · doi:10.1002/pro.5560030923 · Cited by 299

The Eukaryotic Translation Initiation Factor 4E Controls Lettuce Susceptibility to the PotyvirusLettuce mosaic virus

Nicaise, V., German‐Retana, S., Sanjuán, R., Dubrana, M.-P., Mazier, M., Maisonneuve, B., Candresse, T., Caranta, C., & Gall, O. L. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.017855 · Cited by 291

PLECKSTRIN HOMOLOGY DOMAINS: A Common Fold with Diverse Functions

Rebecchi, M. J., & Scarlata, S. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.503 · Cited by 291

MIB: Metal Ion-Binding Site Prediction and Docking Server

Lin, Y., Cheng, C.-W., Chung-Shiuan, S., Hwang, J., Yu, C.-S., & Lu, C. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00407 · Cited by 289

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

Holmgren, A., & Bränden, C.-L. (1989) · Nature · doi:10.1038/342248a0 · Cited by 289

Mathematical Elegance with Biochemical Realism: The Covarion Model of Molecular Evolution

Penny, D., McComish, B. J., Charleston, M. A., & Hendy, M. D. (2001) · Journal of Molecular Evolution · doi:10.1007/s002390010258 · Cited by 287

Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein

Hamburger, Z. A., Brown, M. S., Isberg, R. R., & Bjorkman, P. J. (1999) · Science · doi:10.1126/science.286.5438.291 · Cited by 287

The high‐resolution X‐ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis

Bode, W., Papamokos, E., & Müsil, D. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13566.x · Cited by 288

Refined structure of baboon α-lactalbumin at 1.7 Å resolution

Acharya, K. R., Stuart, D. I., Walker, N. P. C., Lewis, M. P., & Phillips, D. C. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90091-0 · Cited by 286

Assessing the Impact of Secondary Structure and Solvent Accessibility on Protein Evolution

Goldman, N., Thorne, J. L., & Jones, D. T. (1998) · Genetics · doi:10.1093/genetics/149.1.445 · Cited by 281

ModeRNA: a tool for comparative modeling of RNA 3D structure

Rother, M. B., Rother, K. M., Puton, T., & Bujnicki, J. M. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1320 · Cited by 276

Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM

Sengupta, J., Nilsson, J., Gursky, R. P., Spahn, C. M. T., Nissen, P., & Frank, J. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb822 · Cited by 275

Structural Evolution of the Protein Kinase-Like Superfamily

Scheeff, E. D., & Bourne, P. E. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0010049 · Cited by 286

What is the probability of a chance prediction of a protein structure with an rmsd of 6 A?

Reva, B., Finkelstein, A., & Skolnick, J. (1998) · Folding & design · doi:10.1016/s1359-0278(98)00019-4 · Cited by 261

Structure-based inhibitor design by using protein models for the development of antiparasitic agents.

Ring, C. S., Sun, E., McKerrow, J. H., Lee, G., Rosenthal, P. J., Kuntz, I. D., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3583 · Cited by 269

The Protein Model Portal—a comprehensive resource for protein structure and model information

Haas, J., Roth, S., Arnold, K., Kiefer, F., Schmidt, T., Bordoli, L., & Schwede, T. F. (2013) · Database · doi:10.1093/database/bat031 · Cited by 268

Rift valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases

Müller, R., Poch, O., Delarue, M. H., Bishop, D. H. L., & Bouloy, M. (1994) · Journal of General Virology · doi:10.1099/0022-1317-75-6-1345 · Cited by 267

Homology modeling a fast tool for drug discovery: Current perspectives

Vyas, V. K., Ukawala, R. D., Chintha, C., & Ghate, M. D. (2012) · Indian Journal of Pharmaceutical Sciences · doi:10.4103/0250-474x.102537 · Cited by 280

On the Evolution of Structure in Aminoacyl-tRNA Synthetases

O’Donoghue, P., & Luthey-Schulten, Z. A. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.550-573.2003 · Cited by 273

Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species.

Komiya, H., Yeates, T. O., Rees, D. C., Allen, J. P., & Fehér, G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.9012 · Cited by 265

Template-Based Protein Structure Modeling

Fiser, A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-842-3_6 · Cited by 264

The bacterial porin superfamily: sequence alignment and structure prediction

Jeanteur, D., Lakey, J. H., & Pattus, F. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb02145.x · Cited by 263

An algorithm for determining the conformation of polypeptide segments in proteins by systematic search

Moult, J., & James, M. N. G. (1986) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340010207 · Cited by 258

Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human C u,Z n superoxide dismutase

Fisher, C. L., Cabelli, D. E., Hallewell, R. A., Beroza, P., Lo, T. P., Getzoff, E. D., & Tainer, J. A. (1997) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199709)29:1 · Cited by 32

Three-Dimensional Structure Of Antibodies

Alzari, P. M., Lascombe, M., & Poljak, R. J. (1988) · Annual Review of Immunology · doi:10.1146/annurev.iy.06.040188.003011 · Cited by 257

Threading analysis suggests that the obese gene product may be a helical cytokine

Madej, T., Boguski, M. S., & Bryant, S. H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00977-h · Cited by 254

Differences in Active Site Gorge Dimensions of Cholinesterases Revealed by Binding of Inhibitors to Human Butyrylcholinesterase

Saxena, A., Redman, A. M. G., Jiang, X., Lockridge, O., & Doctor, B. P. (1997) · Biochemistry · doi:10.1021/bi971425+ · Cited by 251

Phaser.MRage : automated molecular replacement

Bunkòczi, G., Echols, N., McCoy, A. J., Oeffner, R. D., Adams, P. D., & Read, R. J. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913022750 · Cited by 247

Crystal Structure of Thermostable Family 5 Endocellulase E1 from Acidothermus cellulolyticus in Complex with Cellotetraose,

Sakon, J., Adney, W. S., Himmel, M. E., Thomas, S. R., & Karplus, P. A. (1996) · Biochemistry · doi:10.1021/bi9604439 · Cited by 243

Knowledge‐based protein modelling and design

Blundell, T. L., CARNEY, D., Gardner, S. P., Hayes, F. R. F., Howlin, B. J., Hubbard, T., Overington, J. P., SINGH, D. A., Sibanda, B. L., & Sutcliffe, M. J. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13917.x · Cited by 245

Structure and Biology of Stinging Insect Venom Allergens

King, T. P., & Spangfort, M. D. (2000) · International Archives of Allergy and Immunology · doi:10.1159/000024440 · Cited by 244

Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins

Fox, K. M., & Karplus, P. A. (1994) · Structure · doi:10.1016/s0969-2126(94)00111-1 · Cited by 244

Do aligned sequences share the same fold?

Abagyan, R. A., & Batalov, S. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1287 · Cited by 244

On the Accuracy of Homology Modeling and Sequence Alignment Methods Applied to Membrane Proteins

Forrest, L. R., Tang, C. L., & Honig, B. H. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.082313 · Cited by 243

PROMALS3D: Multiple Protein Sequence Alignment Enhanced with Evolutionary and Three-Dimensional Structural Information

Pei, J., & Grishin, N. V. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-646-7_17 · Cited by 241

How frequent are correlated changes in families of protein sequences?

Neher, E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.98 · Cited by 240

Structural basis of inhibition of CDK–cyclin complexes by INK4 inhibitorsPreprint

Jeffrey, P. D., Tong, L., & Pavletich, N. P. (2000) · Genes & Development · doi:10.1101/gad.851100 · Cited by 239

Mechanism and Catalytic Site Atlas (M-CSA): a database of enzyme reaction mechanisms and active sites

Ribeiro, A. J. M., Holliday, G. L., Furnham, N., Tyzack, J. D., Ferris, K., & Thornton, J. M. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1012 · Cited by 237

Comparative Protein Structure Modeling: Introduction and Practical Examples with Modeller

Sánchez, R., & Šali, A. (2003) · Humana Press eBooks · doi:10.1385/1-59259-368-2:97 · Cited by 238

The architecture of parallel β-helices and related folds

Jenkins, J. A., & Pickersgill, R. W. (2001) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(01)00013-x · Cited by 240

Structural and functional constraints in the evolution of protein families

Worth, C. L., Gong, S., & Blundell, T. L. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2762 · Cited by 232

Prediction of protein side-chain conformation by packing optimization

Lee, C. J., & Subbiah, S. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90550-p · Cited by 227

Viruses of archaea: Structural, functional, environmental and evolutionary genomics

Krupovìč, M., Cvirkaitė‐Krupovič, V., Iranzo, J., Prangishvili, D. A., & Koonin, E. V. (2017) · Virus Research · doi:10.1016/j.virusres.2017.11.025 · Cited by 227

Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy.

Rayment, I., Holden, H. M., Sellers, J. R., Fananapazir, L., & Epstein, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3864 · Cited by 220

Protein function annotation by homology-based inference

Loewenstein, Y., Raimondo, D., Redfern, O., Watson, J., Frishman, D., Michal Linial, B., Orengo, C. A., Thornton, J. M., & Tramontano, A. L. (2009) · Genome biology · doi:10.1186/gb-2009-10-2-207 · Cited by 221

Isoprenyl diphosphate synthases: Protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure

Chen, A., Poulter, C. D., & Kroon, P. A. (1994) · Protein Science · doi:10.1002/pro.5560030408 · Cited by 219

Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction

Overington, J. P., Johnson, M. S., Šali, A., & Blundell, T. L. (1990) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1990.0077 · Cited by 218

Matt: Local Flexibility Aids Protein Multiple Structure Alignment

Menke, M. E., Berger, B., & Cowen, L. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0040010 · Cited by 213

A phylogenomic data-driven exploration of viral origins and evolution

Nasir, A., & Caetano‐Anollés, G. (2015) · Science Advances · doi:10.1126/sciadv.1500527 · Cited by 220

Stereoselective hydrolysis catalyzed by related beta-1,4-glucanases and beta-1,4-xylanases.

Gebler, J. C., Gilkes, N. R., Claeyssens, M., Wilson, D. B., Béguin, P., Wakarchuk, W. W., Kilburn, D. G., Miller, R. C., Warren, R. A. J., & Withers, S. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42313-7 · Cited by 213

STRAP: editor for STRuctural Alignments of Proteins

Gille, C., & Frömmel, C. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.4.377 · Cited by 211

Machine Learning-Guided Protein Engineering

Kouba, P., Kohout, P., Haddadi, F., Bushuiev, A., Samusevich, R., Sedlář, J., Damborský, J., Pluskal, T., Šivic, J., & Mazurenko, S. (2023) · ACS Catalysis · doi:10.1021/acscatal.3c02743 · Cited by 218

A structural motif in the variant surface glycoproteins of Trypanosoma brucei

Blum, M. L., Down, J. A., Gurnett, A. M., Carrington, M., Turner, M. J., & Wiley, D. C. (1993) · Nature · doi:10.1038/362603a0 · Cited by 213

Correct Folding of Circularly Permuted Variants of a βα Barrel Enzyme in Vivo

Luger, K., Hommel, U., Herold, M., Hofsteenge, J., & Kirschner, K. (1989) · Science · doi:10.1126/science.2643160 · Cited by 210

Three-dimensional structure of a thermostable bacterial cellulase

Juy, M., Amrt, A. G., Alzari, P. M., Poljak, R. J., Claeyssens, M., Béguin, P., & Aubert, J.-P. (1992) · Nature · doi:10.1038/357089a0 · Cited by 210

Characterization of the folding degree of proteins

Estrada, E. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.5.697 · Cited by 208

The HMG-1 box protein family: classification and functional relationships

Baxevanis, A. D., & Landsman, D. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.9.1604 · Cited by 208

Ligand Specificity of Brain Lipid-binding Protein

Xu, L. Z., Sánchez, R., Šali, A., & Heintz, N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24711 · Cited by 208

Alignments grow, secondary structure prediction improves

Przybylski, D., & Rost, B. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10029 · Cited by 204

Protein Evolution with Dependence Among Codons Due to Tertiary Structure

Robinson, D. M. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msg184 · Cited by 206

Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

Lee, C., Kominos, D., Jacques, S. L., Margolis, B. L., Schlessinger, J., Shoelson, S. E., & Kuriyan, J. (1994) · Structure · doi:10.1016/s0969-2126(00)00044-7 · Cited by 205

Protein Structure Modeling with MODELLER

Webb, B., & Šali, A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0892-0_14 · Cited by 210

A variety of DNA-binding and multimeric proteins contain the histone fold motif

Baxevanis, A. D., Arents, G., Moudrianakis, E. N., & Landsman, D. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.14.2685 · Cited by 204

Combining protein evolution and secondary structure

Thorne, J. L., Goldman, N., & Jones, D. T. (1996) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a025627 · Cited by 208

Protein structure prediction by threading methods: Evaluation of current techniques

Lemer, C. M. ‐., Rooman, M. J., & Wodak, S. J. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340230308 · Cited by 205

Structure of the Mosquitocidal δ-Endotoxin CytB from sp. and Implications for Membrane Pore Formation

Li, J., Koni, P. A., & Ellar, D. J. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0152 · Cited by 208

High thermal stability is essential for tumor targeting of antibody fragments: engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment.

Willuda, J., Honegger, A., Waibel, R., Schubiger, P. A., Stahel, R. A., Zangemeister‐Wittke, U., & Plückthun, A. (1999) · PubMed · Cited by 200

A Simple Statistical Method for Estimating Type-II (Cluster-Specific) Functional Divergence of Protein Sequences

Gu, X. (2006) · Molecular Biology and Evolution · doi:10.1093/molbev/msl056 · Cited by 200

Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis

Irwin, D. C., Shin, D.-H., Zhang, Z., Barr, B. K., Sakon, J., Karplus, P. A., & Wilson, D. B. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.7.1709-1714.1998 · Cited by 200

Impact of protein conformational diversity on AlphaFold predictions

Saldaño, T., Escobedo, N., Marchetti, J., Zea, D. J., Mac Donagh, J., Velez Rueda, A. J., Gonik, E., García Melani, A., Novomisky Nechcoff, J., Salas, M. N., et al. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac202 · Cited by 196

Stability and folding of domain proteins

Jaenicke, R. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(98)00032-7 · Cited by 201

All are not equal: A benchmark of different homology modeling programs

Wallner, B., & Elofsson, A. (2005) · Protein Science · doi:10.1110/ps.041253405 · Cited by 201

Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid

Kleywegt, G. J., Bergfors, T., Senn, H., LeMotte, P. K., Gsell, B., Shud, K., & Jones, T. A. (1994) · Structure · doi:10.1016/s0969-2126(94)00125-1 · Cited by 199

Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes

Studer, R. A., Dessailly, B. H., & Orengo, C. A. (2013) · Biochemical Journal · doi:10.1042/bj20121221 · Cited by 202

Evolutionary Trace of G Protein-coupled Receptors Reveals Clusters of Residues That Determine Global and Class-specific Functions

Madabushi, S., Gross, A. K., Philippi, A., Meng, E. C., Wensel, T. G., & Lichtarge, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312671200 · Cited by 196

Yeast Protein Serine/Threonine Phosphatases: Multiple Roles and Diverse Regulation

Stark, M. J. R. (1996) · Yeast · doi:10.1002/(sici)1097-0061(199612)12:16 · Cited by 201

Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation 1 1Edited by F. E. Cohen

Russell, R. B., Saqi, M. A. S., Sayle, R. A., Bates, P. A., & Sternberg, M. J. E. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1019 · Cited by 199

Novel knowledge-based mean force potential at atomic level

Melo, F., & Feytmans, E. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0868 · Cited by 196

X‐ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

Day, M. W., Hsu, B. T., Joshua‐Tor, L., Park, J., Zhou, Z. H., Adams, M. W. W., & Rees, D. C. (1992) · Protein Science · doi:10.1002/pro.5560011111 · Cited by 194

Searching for hypothetical proteins: Theory and practice based upon original data and literature

Lübec, G., Afjehi‐Sadat, L., Yang, J., & John, J. P. P. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.10.001 · Cited by 193

FAST: A novel protein structure alignment algorithm

Zhu, J., & Weng, Z. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20331 · Cited by 192

Convergent evolution of similar function in two structurally divergent enzymes

Kuriyan, J., Krishna, T. S. R., Wong, L., Guenther, B. D., Pähler, A., Williams, C. H., & Model, P. (1991) · Nature · doi:10.1038/352172a0 · Cited by 192

Natively Disordered Proteins

Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., & Dunker, A. K. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch41 · Cited by 196

Protein structures sustain evolutionary drift

Rost, B. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00059-x · Cited by 189

Identification of effector-activating residues of Gsα

Berlot, C. H., & Bourne, H. R. (1992) · Cell · doi:10.1016/0092-8674(92)90034-a · Cited by 189

X‐ray structure of nucleoside diphosphate kinase.

Dumas, C., Lascu, I., Moréra, S., Glaser, P., Fourme, R., Wallet, V., Lacombe, M., Véron, M., & Janin, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05397.x · Cited by 188

Modelling three-dimensional protein structures for applications in drug design

Schmidt, T., Bergner, A., & Schwede, T. F. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.10.027 · Cited by 192

Domain closure in mitochondrial aspartate aminotransferase

McPhalen, C. A., Vincent, M. G., Picot, D., Jansonius, J. N., Lesk, A. M., & Chothia, C. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90691-c · Cited by 186

Empirical solvation models can be used to differentiate native from near‐native conformations of bovine pancreatic trypsin inhibitor

Vila, J. A., Williams, R. L., Vásquez, M., & Scheraga, H. A. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340100305 · Cited by 184

Crystal structure of SIV matrix antigen and implications for virus assembly

Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M., & Stuart, D. I. (1995) · Nature · doi:10.1038/378743a0 · Cited by 183

Complementarity of Structure Ensembles in Protein-Protein Binding

Grünberg, R., Leckner, J., & Nilges, M. (2004) · Structure · doi:10.1016/j.str.2004.09.014 · Cited by 187

An integrated approach to the analysis and modeling of protein sequences and structures. I. Protein structural alignment and a quantitative measure for protein structural distance

Yang, A., & Honig, B. H. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3973 · Cited by 185

Evolution, energy landscapes and the paradoxes of protein folding

Wolynes, P. G. (2014) · Biochimie · doi:10.1016/j.biochi.2014.12.007 · Cited by 185

Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion

Su, X., Gastinel, L. N., Vaughn, D. E., Faye, I., Poon, P. H., & Björkman, P. J. (1998) · Science · doi:10.1126/science.281.5379.991 · Cited by 181

The response of protein structures to amino-acid sequence changes

Lesk, A. M., & Chothia, C. (1986) · Philosophical Transactions of the Royal Society of London Series A Mathematical and Physical Sciences · doi:10.1098/rsta.1986.0044 · Cited by 100

Comparison of conformational characteristics in structurally similar protein pairs

Flores, T. P., Orengo, C. A., Moss, D. S., & Thornton, J. M. (1993) · Protein Science · doi:10.1002/pro.5560021104 · Cited by 171

The Evolution of Protein StructuresPreprint

Chothia, C., & Lesk, A. M. (1987) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1987.052.01.046 · Cited by 88

Structural Features can be Unconserved in Proteins with Similar Folds

Russell, R. B., & Barton, G. J. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1733 · Cited by 163

Uncover the conserved property underlying sequence‐distant and structure‐similar proteins

Gao, J., & Li, Z. (2009) · Biopolymers · doi:10.1002/bip.21342 · Cited by 4