UCSF Chimera—A visualization system for exploratory research and analysis

PROSITE: a documented database using patterns and profiles as motif descriptors

Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897

UCSF ChimeraX: Meeting modern challenges in visualization and analysis

Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267

An Integrated Genomic Analysis of Human Glioblastoma Multiforme

Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857

Core Signaling Pathways in Human Pancreatic Cancers Revealed by Global Genomic Analyses

Jones, S., Zhang, X., Parsons, D. W., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Kamiyama, H., Jimeno, A., et al. (2008) · Science · doi:10.1126/science.1164368 · Cited by 3,969

Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors

Zhang, L., Lin, D., Sun, X., Curth, U., Drosten, C., Sauerhering, L., Becker, S., Rox, K., & Hilgenfeld, R. (2020) · Science · doi:10.1126/science.abb3405 · Cited by 2,895

The Genomic Landscapes of Human Breast and Colorectal Cancers

Wood, L. D., Parsons, D. W., Jones, S., Lin, J., Sjöblom, T., Leary, R. J., Shen, D., Boca, S. M., Barber, T., Ptak, J., et al. (2007) · Science · doi:10.1126/science.1145720 · Cited by 2,833

CASTp 3.0: computed atlas of surface topography of proteins

Tian, W., Chen, C., Lei, X., Zhao, J., & Liang, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky473 · Cited by 2,389

SwissDock, a protein-small molecule docking web service based on EADock DSS

Grosdidier, A., Zoete, V., & Michielin, O. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr366 · Cited by 1,950

Mammalian nicotinic acetylcholine receptors: from structure to function

Albuquerque, E. X., Pereira, E. F. R., Alkondon, M., & Rogers, S. W. (2009) · Physiological Reviews · doi:10.1152/physrev.00015.2008 · Cited by 1,724

The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., et al. (2020) · eLife · doi:10.7554/elife.52760 · Cited by 1,676

Tryptophan metabolism as a common therapeutic target in cancer, neurodegeneration and beyond

Platten, M., Nollen, E. A. A., Röhrig, U. F., Fallarino, F., & Opitz, C. A. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0016-5 · Cited by 1,586

Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death

Rogers, C., Fernandes-Alnemri, T., Mayes, L., Alnemri, D., Cingolani, G., & Alnemri, E. S. (2017) · Nature Communications · doi:10.1038/ncomms14128 · Cited by 1,510

Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells

Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188

Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike

Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349

Benchmarking sets for molecular docking.

Huang, N., Shoichet, B. K., & Irwin, J. J. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm0608356 · Cited by 1,318

Structures of Cas9 endonucleases reveal RNA-mediated conformational activation

Jinek, M., Jiang, F., Taylor, D. W., Sternberg, S. H., Kaya, E., Ma, E., Anders, C., Hauer, M., Zhou, K., Lin, S., et al. (2014) · Science · doi:10.1126/science.1247997 · Cited by 1,230

Asgard archaea illuminate the origin of eukaryotic cellular complexity

Zaremba-Niedzwiedzka, K., Caceres, E. F., Saw, J. H., Bäckström, D., Juzokaite, L., Vancaester, E., Seitz, K. W., Anantharaman, K., Starnawski, P., Kjeldsen, K. U., et al. (2017) · Nature · doi:10.1038/nature21031 · Cited by 1,226

Distinct conformational states of SARS-CoV-2 spike protein

Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221

Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir

Yin, W., Mao, C., Luan, X., Shen, D.-D., Shen, Q., Su, H., Wang, X., Zhou, F., Zhao, W., Gao, M., et al. (2020) · Science · doi:10.1126/science.abc1560 · Cited by 1,219

Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability

Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140

Structural basis of STING binding with and phosphorylation by TBK1

Zhang, C., Shang, G., Gui, X., Zhang, X., Bai, X.-C., & Chen, Z. J. (2019) · Nature · doi:10.1038/s41586-019-1000-2 · Cited by 1,095

Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer

Pao, W., & Chmielecki, J. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2947 · Cited by 1,083

Superoxide dismutases and superoxide reductases

Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073

Molecular Architecture of the SARS-CoV-2 Virus

Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060

Potently neutralizing and protective human antibodies against SARS-CoV-2

Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041

Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition

Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016

Comprehensive Evaluation of Ten Docking Programs on a Diverse Set of Protein-Ligand Complexes: The Prediction Accuracy of Sampling Power and Scoring Power

Wang, Z., Sun, H., Yao, X., Li, D., Xu, L., Li, Y., Tian, S., & Hou, T. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp01555g · Cited by 946

Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies

Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795

DNA Excited-State Dynamics: From Single Bases to the Double Helix

Middleton, C. T., de La Harpe, K., Su, C., Law, Y. K., Crespo-Hernández, C. E., & Kohler, B. (2009) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.59.032607.093719 · Cited by 827

Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome

Sharif, H., Wang, L., Wang, W. L., Magupalli, V. G., Andreeva, L., Qiao, Q., Hauenstein, A. V., Wu, Z., Núñez, G., Mao, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1295-z · Cited by 824

Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations

Pugh, T. J., Weeraratne, S. D., Archer, T. C., Pomeranz Krummel, D. A., Auclair, D., Bochicchio, J., Carneiro, M. O., Carter, S. L., Cibulskis, K., Erlich, R. L., et al. (2012) · Nature · doi:10.1038/nature11329 · Cited by 750

Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors

Jardine, J., Julien, J.-P., Menis, S., Ota, T., Kalyuzhniy, O., McGuire, A., Sok, D., Huang, P.-S., MacPherson, S., Jones, M., et al. (2013) · Science · doi:10.1126/science.1234150 · Cited by 770

Pre-fusion structure of a human coronavirus spike protein

Kirchdoerfer, R. N., Cottrell, C. A., Wang, N., Pallesen, J., Yassine, H. M., Turner, H. L., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2016) · Nature · doi:10.1038/nature17200 · Cited by 765

A structural biology community assessment of AlphaFold2 applications

Akdel, M., Pires, D. E. V., Pardo, E. P., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00849-w · Cited by 675

De novo design of picomolar SARS-CoV-2 miniprotein inhibitors

Cao, L., Goreshnik, I., Coventry, B., Case, J. B., Miller, L., Kozodoy, L., Chen, R. E., Carter, L., Walls, A. C., Park, Y.-J., et al. (2020) · Science · doi:10.1126/science.abd9909 · Cited by 742

Patches of Disorganization in the Neocortex of Children with Autism

Stoner, R., Chow, M. L., Boyle, M. P., Sunkin, S. M., Mouton, P. R., Roy, S., Wynshaw-Boris, A., Colamarino, S. A., Lein, E. S., & Courchesne, E. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1307491 · Cited by 722

V3D enables real-time 3D visualization and quantitative analysis of large-scale biological image data sets

Peng, H., Ruan, Z., Long, F., Simpson, J. H., & Myers, E. W. (2010) · Nature Biotechnology · doi:10.1038/nbt.1612 · Cited by 707

SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex

Mannar, D., Saville, J. W., Zhu, X., Srivastava, S. S., Berezuk, A. M., Tuttle, K. S., Marquez, A. C., Sekirov, I., & Subramaniam, S. (2022) · Science · doi:10.1126/science.abn7760 · Cited by 630

Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling

Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661

Structure of the mechanically activated ion channel Piezo1

Saotome, K., Murthy, S. E., Kefauver, J. M., Whitwam, T., Patapoutian, A., & Ward, A. B. (2018) · Nature · doi:10.1038/nature25453 · Cited by 649

Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization

Wang, P., Casner, R. G., Nair, M. S., Wang, M., Yu, J., Cerutti, G., Liu, L., Kwong, P. D., Huang, Y., Shapiro, L., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.007 · Cited by 636

The Fragile X Syndrome Protein Represses Activity-Dependent Translation through CYFIP1, a New 4E-BP

Napoli, I., Mercaldo, V., Boyl, P. P., Eleuteri, B., Zalfa, F., De Rubeis, S., Di Marino, D., Mohr, E., Massimi, M., Falconi, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.031 · Cited by 609

Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms

Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510

Structure and mechanogating mechanism of the Piezo1 channel

Zhao, Q., Zhou, H., Chi, S., Wang, Y., Wang, J., Geng, J., Wu, K., Liu, W., Zhang, T., Dong, M.-Q., et al. (2018) · Nature · doi:10.1038/nature25743 · Cited by 628

Natural Products as Platforms To Overcome Antibiotic Resistance

Rossiter, S. E., Fletcher, M. H., & Wuest, W. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00283 · Cited by 622

Structural basis for androgen specificity and oestrogen synthesis in human aromatase

Ghosh, D., Griswold, J., Erman, M., & Pangborn, W. (2009) · Nature · doi:10.1038/nature07614 · Cited by 618

Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582

SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity

Motozono, C., Toyoda, M., Zahradnik, J., Saito, A., Nasser, H., Tan, T. S., Ngare, I., Kimura, I., Uriu, K., Kosugi, Y., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.006 · Cited by 586

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement

McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535

Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism

Reitman, Z. J., & Yan, H. (2010) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djq187 · Cited by 562

Computed structures of core eukaryotic protein complexes

Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542

Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40

Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548

A practical guide to large-scale docking

Bender, B. J., Gahbauer, S., Luttens, A., Lyu, J., Webb, C. M., Stein, R. M., Fink, E. A., Balius, T. E., Carlsson, J., Irwin, J. J., et al. (2021) · Nature Protocols · doi:10.1038/s41596-021-00597-z · Cited by 546

Histone deacetylase 6 structure and molecular basis of catalysis and inhibition

Hai, Y., & Christianson, D. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2134 · Cited by 521

Identification of Novel Mobilized Colistin Resistance Gene mcr-9 in a Multidrug-Resistant, Colistin-Susceptible Salmonella enterica Serotype Typhimurium Isolate

Carroll, L. M., Gaballa, A., Guldimann, C., Sullivan, G., Henderson, L. O., & Wiedmann, M. (2019) · mBio · doi:10.1128/mbio.00853-19 · Cited by 506

Crystal structure of the human σ1 receptor

Schmidt, H. R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., & Kruse, A. C. (2016) · Nature · doi:10.1038/nature17391 · Cited by 482

Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor

Kim, K., Che, T., Panova, O., DiBerto, J. F., Lyu, J., Krumm, B. E., Wacker, D., Robertson, M. J., Seven, A. B., Nichols, D. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.024 · Cited by 481

Structure of the yeast F 1 F o -ATP synthase dimer and its role in shaping the mitochondrial cristae

Davies, K. M., Anselmi, C., Wittig, I., Faraldo-Gómez, J. D., & Kühlbrandt, W. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204593109 · Cited by 473

SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern

McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412

Using Whole-Exome Sequencing to Identify Inherited Causes of Autism

Yu, T. W., Chahrour, M. H., Coulter, M. E., Jiralerspong, S., Okamura-Ikeda, K., Ataman, B., Schmitz-Abe, K., Harmin, D. A., Adli, M., Malik, A. N., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.002 · Cited by 442

Structure-based membrane dome mechanism for Piezo mechanosensitivity

Guo, Y. R., & MacKinnon, R. (2017) · eLife · doi:10.7554/elife.33660 · Cited by 446

Structural analyses of Candida albicans sterol 14α-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis

Hargrove, T. Y., Friggeri, L., Wawrzak, Z., Qi, A., Hoekstra, W. J., Schotzinger, R. J., York, J. D., Guengerich, F. P., & Lepesheva, G. I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778308 · Cited by 444

The antigenic anatomy of SARS-CoV-2 receptor binding domain

Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371

Structure of activated transcription complex Pol II–DSIF–PAF–SPT6

Vos, S. M., Farnung, L., Boehning, M., Wigge, C., Linden, A., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0440-4 · Cited by 432

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A. (2016) · Science · doi:10.1126/science.aaf5023 · Cited by 424

The structure of the dynactin complex and its interaction with dynein

Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P. (2015) · Science · doi:10.1126/science.aaa4080 · Cited by 421

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2

Jiao, L., & Liu, X. (2015) · Science · doi:10.1126/science.aac4383 · Cited by 402

Retinoic acid receptors: From molecular mechanisms to cancer therapy

di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403

Overcoming mutation-based resistance to antiandrogens with rational drug design

Balbas, M. D., Evans, M. J., Hosfield, D. J., Wongvipat, J., Arora, V. K., Watson, P. A., Chen, Y., Greene, G. L., Shen, Y., & Sawyers, C. L. (2013) · eLife · doi:10.7554/elife.00499 · Cited by 397

Boosting docking-based virtual screening with deep learning.

Pereira, J. C., Caffarena, E. R., & dos Santos, C. N. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00355 · Cited by 395

C2H2 zinc finger proteins greatly expand the human regulatory lexicon

Najafabadi, H. S., Mnaimneh, S., Schmitges, F. W., Garton, M., Lam, K. N., Yang, A., Albu, M., Weirauch, M. T., Radovani, E., Kim, P. M., et al. (2015) · Nature Biotechnology · doi:10.1038/nbt.3128 · Cited by 346

Hypoxia induces rapid changes to histone methylation and reprograms chromatin

Batie, M., Frost, J., Frost, M., Wilson, J. W., Schofield, P., & Rocha, S. (2019) · Science · doi:10.1126/science.aau5870 · Cited by 385

Transaminase Inhibition by 2-Hydroxyglutarate Impairs Glutamate Biosynthesis and Redox Homeostasis in Glioma

McBrayer, S. K., Mayers, J. R., DiNatale, G. J., Shi, D. D., Khanal, J., Chakraborty, A. A., Sarosiek, K. A., Briggs, K. J., Robbins, A. K., Sewastianik, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.038 · Cited by 368

Structure of the neurotensin receptor 1 in complex with β-arrestin 1

Huang, W., Masureel, M., Qu, Q., Janetzko, J., Inoue, A., Kato, H. E., Robertson, M. J., Nguyen, K. C., Glenn, J. S., Skiniotis, G., et al. (2020) · Nature · doi:10.1038/s41586-020-1953-1 · Cited by 373

SIRT6 is responsible for more efficient DNA double-strand break repair in long-lived species

Tian, X., Firsanov, D., Zhang, Z., Cheng, Y., Luo, L., Tombline, G., Tan, R., Simon, M., Henderson, S., Steffan, J., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.043 · Cited by 353

XPD Helicase Structures and Activities: Insights into the Cancer and Aging Phenotypes from XPD Mutations

Fan, L., Fuss, J. O., Cheng, Q. J., Arvai, A. S., Hammel, M., Roberts, V. A., Cooper, P. K., & Tainer, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.04.030 · Cited by 369

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants

Yuan, M., Huang, D., Lee, C.-C. D., Wu, N. C., Jackson, A. M., Zhu, X., Liu, H., Peng, L., van Gils, M. J., Sanders, R. W., et al. (2021) · doi:10.1101/2021.02.16.430500 · Cited by 364

Structural insight into autoinhibition and histone H3-induced activation of DNMT3A

Guo, X., Wang, L., Li, J., Ding, Z., Xiao, J., Yin, X., He, S., Shi, P., Dong, L., Li, G., et al. (2015) · Nature · doi:10.1038/nature13899 · Cited by 361

A Genomic Regulatory Element That Directs Assembly and Function of Immune-Specific AP-1–IRF Complexes

Glasmacher, E., Agrawal, S., Chang, A. B., Murphy, T. L., Zeng, W., Vander Lugt, B., Khan, A. A., Ciofani, M., Spooner, C. J., Rutz, S., et al. (2012) · Science · doi:10.1126/science.1228309 · Cited by 361

Mapping protein binding sites on the biomolecular corona of nanoparticles

Kelly, P. M., Åberg, C., Polo, E., O'Connell, A., Cookman, J., Fallon, J., Krpetić, Ž., & Dawson, K. A. (2015) · Nature Nanotechnology · doi:10.1038/nnano.2015.47 · Cited by 360

Spatiotemporal single-cell analysis of gene expression in the mouse suprachiasmatic nucleus

Wen, S., Ma, D., Zhao, M., Xie, L., Wu, Q., Gou, L., Zhu, C., Fan, Y., Wang, H., & Yan, J. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0586-x · Cited by 328

Structure of the human LAT1–4F2hc heteromeric amino acid transporter complex

Yan, R., Zhao, X., Lei, J., & Zhou, Q. (2019) · Nature · doi:10.1038/s41586-019-1011-z · Cited by 358

D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization

Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.012 · Cited by 324

AI-based structure prediction empowers integrative structural analysis of human nuclear pores

Mosalaganti, S., Obarska-Kosinska, A., Siggel, M., Taniguchi, R., Turoňová, B., Zimmerli, C. E., Buczak, K., Schmidt, F. H., Margiotta, E., Mackmull, M.-T., et al. (2022) · Science · doi:10.1126/science.abm9506 · Cited by 355

SIRT5 regulation of ammonia-induced autophagy and mitophagy

Polletta, L., Vernucci, E., Carnevale, I., Arcangeli, T., Rotili, D., Palmerio, S., Steegborn, C., Nowak, T., Schutkowski, M., Pellegrini, L., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1009778 · Cited by 350

Cartography of neurexin alternative splicing mapped by single-molecule long-read mRNA sequencing

Treutlein, B., Gokce, O., Quake, S. R., & Südhof, T. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403244111 · Cited by 348

Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis

Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Brewster, A. S., Sauter, N. K., Cohen, A. E., et al. (2015) · Nature · doi:10.1038/nature14975 · Cited by 348

Architecture of human mTOR complex 1

Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344

Binding MOAD (Mother Of All Databases)

Hu, L., Benson, M. L., Smith, R. D., Lerner, M. G., & Carlson, H. A. (2005) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20512 · Cited by 328

Experimental demonstration of highly reliable dynamic memristor for artificial neuron and neuromorphic computing

Park, S.-O., Jeong, H., Park, J., Bae, J., & Choi, S. (2022) · Nature Communications · doi:10.1038/s41467-022-30539-6 · Cited by 331

Human germinal centres engage memory and naive B cells after influenza vaccination

Turner, J. S., Zhou, J. Q., Han, J., Schmitz, A. J., Rizk, A. A., Alsoussi, W. B., Lei, T., Amor, M., McIntire, K. M., Meade, P., et al. (2020) · Nature · doi:10.1038/s41586-020-2711-0 · Cited by 304

Cryo-EM structures of the TMEM16A calcium-activated chloride channel

Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., et al. (2017) · Nature · doi:10.1038/nature25024 · Cited by 333

Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome

Dong, Y., Zhang, S., Wu, Z., Li, X., Wang, W. L., Zhu, Y., Stoilova-McPhie, S., Lu, Y., Finley, D., & Mao, Y. (2019) · Nature · doi:10.1038/s41586-018-0736-4 · Cited by 328

Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways

Ikeuchi, K., Tesina, P., Matsuo, Y., Sugiyama, T., Cheng, J., Saeki, Y., Tanaka, K., Becker, T., Beckmann, R., & Inada, T. (2019) · The EMBO Journal · doi:10.15252/embj.2018100276 · Cited by 315

Fine-Mapping the Genetic Association of the Major Histocompatibility Complex in Multiple Sclerosis: HLA and Non-HLA Effects

Patsopoulos, N. A., Barcellos, L. F., Hintzen, R. Q., Schaefer, C., van Duijn, C. M., Noble, J. A., Raj, T., IMSGC, ANZgene, Gourraud, P.-A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003926 · Cited by 312

In Silico Reconstruction of the Viral Evolutionary Lineage Yields a Potent Gene Therapy Vector

Zinn, E., Pacouret, S., Khaychuk, V., Turunen, H. T., Carvalho, L. S., Andres-Mateos, E., Shah, S., Shelke, R., Maurer, A. C., Plovie, E., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.019 · Cited by 310

Structure deformation and curvature sensing of PIEZO1 in lipid membranes

Yang, X., Lin, C., Chen, X., Li, S., Li, X., & Xiao, B. (2022) · Nature · doi:10.1038/s41586-022-04574-8 · Cited by 305

Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.

Frauenfeld, J., Gumbart, J., Sluis, E. O. V. D., Funes, S., Gartmann, M., Beatrix, B., Mielke, T., Berninghausen, O., Becker, T., Schulten, K., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2026 · Cited by 298