Announcing the worldwide Protein Data Bank

The Protein Data Bank

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

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[30] Macromolecular crystallographic information file

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The effect of a thieno[2,3-b]pyridine PLC-γ inhibitor on the proliferation, morphology, migration and cell cycle of breast cancer cells

Leung, E. Y., Hung, J. M., Barker, D. L. A., & Reynisson, J. (2013) · MedChemComm · doi:10.1039/c3md00290j · Cited by 44

Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links

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ADAN: a database for prediction of protein–protein interaction of modular domains mediated by linear motifs

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3-Amino-thieno[2,3-b]pyridines as microtubule-destabilising agents: Molecular modelling and biological evaluation in the sea urchin embryo and human cancer cells

Eurtivong, C., Semenov, V. V., Semenova, M. N., Konyushkin, L. D., Atamanenko, O. P., Reynisson, J., & Kiselyov, A. S. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.11.041 · Cited by 43

Broad Analysis of Vicinal Disulfides: Occurrences, Conformations with Cis or with Trans Peptides, and Functional Roles Including Sugar Binding

Richardson, J. S., Videau, L. L., Williams, C. J., & Richardson, D. C. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.017 · Cited by 43

Model validation: local diagnosis, correction and when to quit

Richardson, J. S., Williams, C. J., Hintze, B. J., Chen, V. B., Prisant, M. G., Videau, L. L., & Richardson, D. C. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317009834 · Cited by 43

Molecular docking revealed the binding of nucleotide/side inhibitors to Zika viral polymerase solved structures

Elfiky, A. A., & Ismail, A. M. (2018) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2018.1454981 · Cited by 43

Impact of structural biologists and the Protein Data Bank on small-molecule drug discovery and development

Burley, S. K. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100559 · Cited by 45

The Protein Circular Dichroism Data Bank, A Web-Based Site for Access to Circular Dichroism Spectroscopic Data

Whitmore, L., Woollett, B., Miles, A. J., Janes, R. W., & Wallace, B. A. (2010) · Structure · doi:10.1016/j.str.2010.08.008 · Cited by 43

Reverse Micelles in Integral Membrane Protein Structural Biology by Solution NMR Spectroscopy

Kielec, J. M., Valentine, K. G., Babu, C. R., & Wand, A. J. (2009) · Structure · doi:10.1016/j.str.2009.01.004 · Cited by 43

Insights into Positive and Negative Requirements for Protein–Protein Interactions by Crystallographic Analysis of the β-Lactamase Inhibitory Proteins BLIP, BLIP-I, and BLP

Gretes, M. C., Lim, D., de Castro, L., Jensen, S. E., Kang, S. G., Lee, K. J., & Strynadka, N. C. J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.058 · Cited by 43

A Coarse-Grained Approach to Protein Design: Learning from Design to Understand Folding

Ivan Coluzza, B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020853 · Cited by 42

Proteogenomic convergence for understanding cancer pathways and networks

Boja, E. S., & Rodriguez, H. (2014) · Clinical Proteomics · doi:10.1186/1559-0275-11-22 · Cited by 42

How do SMA-linked mutations of SMN1 lead to structural/functional deficiency of the SMA protein?

Li, W. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178519 · Cited by 42

Acknowledging Errors: Advanced Molecular Replacement with Phaser

McCoy, A. J. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7000-1_18 · Cited by 42

Therapeutic Lowering of C-Reactive Protein

Jimenez, R. V., & Szalai, A. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.619564 · Cited by 42

Innovative Teacher Education with the Augmented Reality Device Microsoft HoloLens—Results of an Exploratory Study and Pedagogical Considerations

Wyss, C., Bührer, W., Furrer, F., Degonda, A., & Hiss, J. A. (2021) · Multimodal Technologies and Interaction · doi:10.3390/mti5080045 · Cited by 42

Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble

Audagnotto, M., Czechtizky, W., Maria, L. D., Käck, H., Papoian, G. A., Tornberg, L., Tyrchan, C., & Ulander, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-13714-z · Cited by 44

DNSN-1 recruits GINS for CMG helicase assembly during DNA replication initiation in Caenorhabditis elegans

Xia, Y., Sonneville, R., Jenkyn-Bedford, M., Ji, L., Alabert, C., Hong, Y., Yeeles, J. T. P., & Labib, K. P. M. (2023) · Science · doi:10.1126/science.adi4932 · Cited by 41

High-throughput expression and purification of membrane proteins

Mancia, F., & Love, J. D. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.03.021 · Cited by 42

Linking publication, gene and protein data

Kersey, P. J., & Apweiler, R. (2006) · Nature Cell Biology · doi:10.1038/ncb1495 · Cited by 42

Updated Virophage Taxonomy and Distinction from Polinton-like Viruses

Roux, S., Fischer, M., Hackl, T., Katz, L. A., Schulz, F., & Yutin, N. (2023) · Biomolecules · doi:10.3390/biom13020204 · Cited by 41

Modern machine‐learning for binding affinity estimation of protein–ligand complexes: Progress, opportunities, and challenges

Harren, T., Gutermuth, T., Grebner, C., Heßler, G., & Rarey, M. (2024) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1716 · Cited by 46

Therapeutic targeting of TGF ‐β in lung cancer

Aftabi, S., Behrooz, A. B., Cordani, M., Rahiman, N., Sadeghdoust, M., Aligolighasemabadi, F., Pistorius, S., Alavizadeh, S. H., Taefehshokr, N., & Ghavami, S. (2024) · FEBS Journal · doi:10.1111/febs.17234 · Cited by 42

Structural and Mutational Studies on the Unusual Substrate Specificity of meso‐Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum

Liu, W., Li, Z., Huang, C., Guo, R., Zhao, L., Zhang, D., Chen, X., Wu, Q., & Zhu, D. (2013) · ChemBioChem · doi:10.1002/cbic.201300691 · Cited by 41

Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism

Cho, H. J., Cho, H. Y., Kim, K. J., Kim, M. H., Kim, S. W., & Kang, B. S. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.04.007 · Cited by 41

4D solid-state NMR for protein structure determination

Huber, M., Böckmann, A., Hiller, S., & Meier, B. H. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp23872a · Cited by 41

3D QSAR and docking study of flavone derivatives as potent inhibitors of influenza H1N1 virus neuraminidase

Gao, L., Zu, M., Wu, S., Liu, A., & Du, G. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.07.071 · Cited by 41

SAXS Data Alone can Generate High-Quality Models of Protein-Protein Complexes

Schindler, C., de Vries, S. J., Sasse, A., & Zacharias, M. (2016) · Structure · doi:10.1016/j.str.2016.06.007 · Cited by 41

Identification of the cognate peptide-MHC target of T cell receptors using molecular modeling and force field scoring

Lanzarotti, E., Marcatili, P., & Nielsen, M. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.12.019 · Cited by 38

Oligomannose Glycopeptide Conjugates Elicit Antibodies Targeting the Glycan Core Rather than Its Extremities

Nguyen, D. N. P., Xu, B., Stanfield, R. L., Bailey, J. K., Horiya, S., Temme, J. S., Leon, D. R., LaBranche, C. C., Montefiori, D. C., Costello, C. E., et al. (2019) · ACS Central Science · doi:10.1021/acscentsci.8b00588 · Cited by 41

Peptide science: A “rule model” for new generations of peptidomimetics

Reese, H. R., Shanahan, C. C., Proulx, C., & Menegatti, S. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2019.10.045 · Cited by 41

Haruspex: A Neural Network for the Automatic Identification of Oligonucleotides and Protein Secondary Structure in Cryo‐Electron Microscopy Maps

Mostosi, P., Schindelin, H., Kollmannsberger, P., & Thorn, A. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202000421 · Cited by 41

Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future

Burley, S. K., Berman, H. M., Chiu, W., Dai, W., Flatt, J. W., Hudson, B. P., Kaelber, J. T., Khare, S. D., Kulczyk, A., Lawson, C. L., et al. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01013-w · Cited by 44

Curation of complex, context-dependent immunological data

Vita, R., Vaughan, K. C., Zarebski, L. M., Salimi, N., Fleri, W., Grey, H. M., Sathiamurthy, M., Mokili, J. L., Bui, H., Bourne, P. E., et al. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-341 · Cited by 41

Class II-selective histone deacetylase inhibitors. Part 2: Alignment-independent GRIND 3-D QSAR, homology and docking studies

Ragno, R., Simeoni, S., Rotili, D., Caroli, A., Botta, G., Brosch, G., Massa, S., & Mai, A. (2007) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2007.05.004 · Cited by 41

Hydrogen-bond stabilization in oxyanion holes: grand jeté to three dimensions

Simón, L., & Goodman, J. M. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob06717j · Cited by 41

ZifBASE: a database of zinc finger proteins and associated resources

Mannu, J., Muthukumaran, J., Chandrasekar, S., Chawla, K., Punetha, A., & Sundar, D. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-421 · Cited by 41

Evolutionary-inspired probabilistic search for enhancing sampling of local minima in the protein energy surface

Olson, B., & Shehu, A. (2012) · Proteome Science · doi:10.1186/1477-5956-10-s1-s5 · Cited by 40

tLyp–1: A peptide suitable to target NRP–1 receptor

Larue, L., Kenzhebayeva, B., Al-Thiabat, M. G., Jouan–Hureaux, V., Gazzali, A. M., Wahab, H. A., Boura, C., Yeligbayeva, G., Nakan, U., Frochot, C., et al. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106200 · Cited by 41

Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex

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From protein sequences to 3D-structures and beyond: the example of the UniProt Knowledgebase

Hinz, U. G. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0229-6 · Cited by 40

NRG-CING: integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB

Doreleijers, J. F., Vranken, W., Schulte, C., Markley, J. L., Ulrich, E. L., Vriend, G., & Vuister, G. W. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1134 · Cited by 40

Crystallographic education in the 21st century

Gražulis, S., Sarjeant, A. A. N., Moeck, P., Stone‐Sundberg, J. L., Snyder, T. J., Kaminsky, W., Oliver, A. G., Stern, C. L., Dawe, L. N., Rychkov, D. A., et al. (2015) · Journal of Applied Crystallography · doi:10.1107/s1600576715016830 · Cited by 40

Multiple Surface Regions on the Niemann-Pick C2 Protein Facilitate Intracellular Cholesterol Transport

McCauliff, L. A., Xu, Z., Li, R., Kodukula, S., Ko, D. C., Scott, M. P., Kahn, P. C., & Storch, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.667469 · Cited by 42

Aminoadamantanes containing monoterpene-derived fragments as potent tyrosyl-DNA phosphodiesterase 1 inhibitors

Ponomarev, K. Y., Суслов, Е. В., Zakharenko, A. L., Zakharova, O. D., Rogachev, A. D., Викторовна, К. Д., Zafar, A., Reynisson, J., Nefedov, A. A., Volcho, K. P., et al. (2017) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2017.12.005 · Cited by 40

Metabolic and Epigenetic Action Mechanisms of Antidiabetic Medicinal Plants

Shanak, S., Saad, B., & Zaid, H. (2019) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2019/3583067 · Cited by 42

Open-access data: A cornerstone for artificial intelligence approaches to protein structure prediction

Burley, S. K., & Berman, H. M. (2021) · Structure · doi:10.1016/j.str.2021.04.010 · Cited by 44

Regulatory interplay between pap operons in uropathogenic Escherichia coli

Totsika, M., Beatson, S. A., Holden, N. J., & Gally, D. L. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.06098.x · Cited by 40

Unraveling the molecular mechanisms of nitrogenase conformational protection against oxygen in diazotrophic bacteria

Lery, L. M. S., Bitar, M., Costa, M. G. S., Rössle, S. C., & Bisch, P. M. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-s5-s7 · Cited by 39

Deep Confident Steps to New Pockets: Strategies for Docking GeneralizationPreprint

Corso, G., Deng, A., Fry, B. N., Polizzi, N. F., Barzilay, R., & Jaakkola, T. (2024) · PubMed · doi:10.48550/arxiv.2402.18396 · Cited by 79

MOSAIC: A Data Model and File Formats for Molecular Simulations

Hinsen, K. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci400599y · Cited by 39

Promoting a structural view of biology for varied audiences: an overview of RCSB PDB resources and experiences

Dutta, S., Zardecki, C., Goodsell, D. S., & Berman, H. M. (2010) · Journal of Applied Crystallography · doi:10.1107/s002188981002371x · Cited by 39

Xanomeline displays concomitant orthosteric and allosteric binding modes at the M4 mAChR

Burger, W. A. C., Pham, V., Vuckovic, Z., Powers, A. S., Mobbs, J. I., Laloudakis, Y. D., Glukhova, A., Wootten, D. L., Tobin, A. B., Sexton, P. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41199-5 · Cited by 39

RCSB Protein Data Bank: Delivering integrative structures alongside experimental structures and computed structure models

Vallat, B. K., Rose, Y., Piehl, D. W., Duarte, J. M., Bittrich, S., Bi, C., Segura, J., Zalevsky, A. O., Sekharan, M. R., Webb, B., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1187 · Cited by 39

Cloning, expression and functional validation of drought inducible ascorbate peroxidase (Ec-apx1) from Eleusine coracana

Bhatt, D., Saxena, S. C., Jain, S., Dobriyal, A. K., Majee, M., & Arora, S. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-2157-z · Cited by 39

You are lost without a map: Navigating the sea of protein structures

Lamb, A. L., Kappock, T. J., & Silvaggi, N. R. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.12.021 · Cited by 45

How Community Has Shaped the Protein Data Bank

Berman, H. M., Kleywegt, G. J., Nakamura, H., & Markley, J. L. (2013) · Structure · doi:10.1016/j.str.2013.07.010 · Cited by 39

Off-lattice protein structure prediction with homologous crossover

Olson, B., Jong, K. A. D., & Shehu, A. (2013) · Genetic and Evolutionary Computation Conference (GECCO) · doi:10.1145/2463372.2463407 · Cited by 39

Multivariate Analyses of Quality Metrics for Crystal Structures in the PDB Archive

Shao, C., Yang, H., Westbrook, J., Young, J. Y., Zardecki, C., & Burley, S. K. (2017) · Structure · doi:10.1016/j.str.2017.01.013 · Cited by 40

A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora

Salomone‐Stagni, M., Bartho, J. D., Polsinelli, I., Bellini, D., Walsh, M. A., Demitri, N., & Benini, S. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.02.002 · Cited by 39

Using Entropy Maximization to Understand the Determinants of Structural Dynamics beyond Native Contact Topology

Lezon, T. R., & Bahar, İ. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000816 · Cited by 39

From evidence to inference: Probing the evolution of protein interaction networks

Ratmann, O., Wiuf, C., & Pinney, J. W. (2009) · HFSP journal · doi:10.2976/1.3167215 · Cited by 38

The human "magnesome": detecting magnesium binding sites on human proteins

Piovesan, D., Profiti, G., Martelli, P. L., & Casadio, R. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-s14-s10 · Cited by 41

Identification of chemically diverse, novel inhibitors of 17β-hydroxysteroid dehydrogenase type 3 and 5 by pharmacophore-based virtual screening

Schuster, D., Kowalik, D., Kirchmair, J., Laggner, C., Markt, P., Aebischer-Gumy, C., Ströhle, F., Möller, G., Wolber, G., Wilckens, T., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.01.016 · Cited by 39

Quantitative Comparison of Catalytic Mechanisms and Overall Reactions in Convergently Evolved Enzymes: Implications for Classification of Enzyme Function

Almonacid, D. E., Yera, E. R., Mitchell, J. B. O., & Babbitt, P. C. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000700 · Cited by 39

Identification of FAH Domain-containing Protein 1 (FAHD1) as Oxaloacetate Decarboxylase

Pircher, H., von Grafenstein, S., Diener, T., Metzger, C., Albertini, E., Taferner, A., Unterluggauer, H., Krämer, C., Liedl, K. R., & Jansen‐Dürr, P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.609305 · Cited by 39

3-D QSAR Studies on Histone Deacetylase Inhibitors. A GOLPE/GRID Approach on Different Series of Compounds

Ragno, R., Simeoni, S., Valente, S., Massa, S., & Mai, A. (2006) · Journal of Chemical Information and Modeling · doi:10.1021/ci050556b · Cited by 39

A Novel Variant in CMAH Is Associated with Blood Type AB in Ragdoll Cats

Gandolfi, B., Grahn, R. A., Gustafson, N. A., Proverbio, D., Spada, E., Adhikari, B., Cheng, J., Andrews, G. A., Lyons, L. A., & Helps, C. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154973 · Cited by 38

Titration_DB: Storage and analysis of NMR‐monitored protein pH titration curves

Farrell, D., Miranda, E. S., Webb, H. M., Georgi, N., Crowley, P. B., McIntosh, L. P., & Nielsen, J. E. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22611 · Cited by 39

LabTrove: A Lightweight, Web Based, Laboratory “Blog” as a Route towards a Marked Up Record of Work in a Bioscience Research Laboratory

Milsted, A. J., Hale, J. R., Frey, J. G., & Neylon, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067460 · Cited by 38

Probabilistic Search and Energy Guidance for Biased Decoy Sampling in Ab Initio Protein Structure Prediction

Molloy, K., Saleh, S. N., & Shehu, A. (2013) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2013.29 · Cited by 38

Fractal symmetry of protein interior: what have we learned?

Banerji, A., & Ghosh, I. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0722-6 · Cited by 38

Glycoconjugate Data Bank:Structures an annotated glycan structure database and N-glycan primary structure verification service

Nakahara, T., Hashimoto, R., Nakagawa, H., Monde, K., Miura, N., & Nishimura, S. ‐. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm833 · Cited by 38

OpenStructure: a flexible software framework for computational structural biology

Biasini, M., Mariani, V., Haas, J., Scheuber, S., Schenk, A. D., Schwede, T. F., & Philippsen, A. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq481 · Cited by 38

A fast and automated solution for accurately resolving protein domain architectures

Yeats, C., Redfern, O., & Orengo, C. A. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq034 · Cited by 38

An integrative data analysis platform for gene set analysis and knowledge discovery in a data warehouse framework

Chen, Y. A., Tripathi, L. P., & Mizuguchi, K. (2016) · Database · doi:10.1093/database/baw009 · Cited by 38

Structural basis of reversine selectivity in inhibiting Mps1 more potently than aurora B kinase

Hiruma, Y., Koch, A., Dharadhar, S., Joosten, R. P., & Anastassis Perrakis, A. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25174 · Cited by 36

Recent developments inMrBUMP: better search-model preparation, graphical interaction with search models, and solution improvement and assessment

Keegan, R. M., McNicholas, S. J., Thomas, J. M. H., Simpkin, A. J., Šimkovic, F., Uski, V., Ballard, C. C., Winn, M., Wilson, K. S., & Rigden, D. J. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318003455 · Cited by 38

Protein structure and computational drug discovery

Nero, T. L., Parker, M. W., & Morton, C. J. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180202 · Cited by 39

GlyStruct: glycation prediction using structural properties of amino acid residues

Reddy, H. M., Sharma, A. K., Dehzangi, A., Shigemizu, D., Chandra, A. A., & Tsunoda, T. (2019) · BMC Bioinformatics · doi:10.1186/s12859-018-2547-x · Cited by 37

Interaction of ZnO Nanostructures with Proteins: In Vitro Fibrillation/Antifibrillation Studies and in Silico Molecular Docking Simulations

Giannousi, K., Geromichalos, G. D., Κακολύρη, Δ. Ν., Mourdikoudis, S., & Dendrinou-Samara, C. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00642 · Cited by 39

PlayMolecule CrypticScout: Predicting Protein Cryptic Sites Using Mixed-Solvent Molecular Simulations

Martinez-Rosell, G., Lovera, S., Sands, Z. A., & Fabritiis, G. D. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01209 · Cited by 38

A systematic analysis of the beta hairpin motif in the Protein Data Bank

DuPai, C. D., Davies, B. W., & Wilke, C. O. (2021) · Protein Science · doi:10.1002/pro.4020 · Cited by 40

Enhanced validation of small-molecule ligands and carbohydrates in the Protein Data Bank

Feng, Z., Westbrook, J., Sala, R., Smart, O. S., Bricogne, G., Matsubara, M., Yamada, I., Tsuchiya, S., Aoki-Kinoshita, K. F., Hoch, J. C., et al. (2021) · Structure · doi:10.1016/j.str.2021.02.004 · Cited by 39

New system for archiving integrative structures

Vallat, B. K., Webb, B., Fayazi, M., Voinea, S., Tangmunarunkit, H., Ganesan, S. J., Lawson, C. L., Westbrook, J., Kesselman, C., Šali, A., et al. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321010871 · Cited by 38

Protein folding problem: enigma, paradox, solution

Finkelstein, A. V., Bogatyreva, N. S., Ivankov, D. N., & Garbuzynskiy, S. O. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01000-1 · Cited by 41

Hydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPase

Elias, M. H., Liebschner, D. C., Koepke, J., Claude Lecomte, B., Guillot, B., Jelsch, C., & Chabrière, É. (2013) · BMC Research Notes · doi:10.1186/1756-0500-6-308 · Cited by 38

Agathisflavone, a natural biflavonoid that inhibits SARS-CoV-2 replication by targeting its proteases

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LYCHOS is a human hybrid of a plant-like PIN transporter and a GPCR

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