Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

Phaser crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Towards automated crystallographic structure refinement with phenix.refine

Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511

Molecular basis of agonism and antagonism in the oestrogen receptor

Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355

The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

Yun, C.-H., Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K.-K., Meyerson, M., & Eck, M. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709662105 · Cited by 2,118

Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253

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

Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma

Krauthammer, M., Kong, Y., Ha, B. H., Evans, P., Bacchiocchi, A., McCusker, J. P., Cheng, E., Davis, M. J., Goh, G., Choi, M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2359 · Cited by 1,191

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192

Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota

Hehemann, J.-H., Correc, G., Barbeyron, T., Helbert, W., Czjzek, M., & Michel, G. (2010) · Nature · doi:10.1038/nature08937 · Cited by 1,117

The MCL1 inhibitor S63845 is tolerable and effective in diverse cancer models

Kotschy, A., Szlavik, Z., Murray, J., Davidson, J., Maragno, A. L., Le Toumelin-Braizat, G., Chanrion, M., Kelly, G. L., Gong, J.-N., Moujalled, D. M., et al. (2016) · Nature · doi:10.1038/nature19830 · Cited by 1,047

Ultra-large library docking for discovering new chemotypes

Lyu, J., Wang, S., Balius, T. E., Singh, I., Levit, A., Moroz, Y. S., O’Meara, M. J., Che, T., Algaa, E., Tolmachova, K., et al. (2019) · Nature · doi:10.1038/s41586-019-0917-9 · Cited by 998

Crystal Structure of Agaricus bisporus Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone

Ismaya, W. T., Rozeboom, H. J., Weijn, A., Mes, J. J., Fusetti, F., Wichers, H. J., & Dijkstra, B. W. (2011) · Biochemistry · doi:10.1021/bi200395t · Cited by 872

The target landscape of clinical kinase drugs

Klaeger, S., Heinzlmeir, S., Wilhelm, M., Polzer, H., Vick, B., Koenig, P.-A., Reinecke, M., Ruprecht, B., Petzoldt, S., Meng, C., et al. (2017) · Science · doi:10.1126/science.aan4368 · Cited by 854

Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis

Anastasiou, D., Yu, Y., Israelsen, W. J., Jiang, J.-K., Boxer, M. B., Hong, B. S., Tempel, W., Dimov, S., Shen, M., Jha, A., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1060 · Cited by 816

Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA

Chandra, V., Huang, P., Hamuro, Y., Raghuram, S., Wang, Y., Burris, T. P., & Rastinejad, F. (2008) · Nature · doi:10.1038/nature07413 · Cited by 808

Structural Basis for Sorting Mechanism of p62 in Selective Autophagy

Ichimura, Y., Kumanomidou, T., Sou, Y.-S., Mizushima, T., Ezaki, J., Ueno, T., Kominami, E., Yamane, T., Tanaka, K., & Komatsu, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802182200 · Cited by 803

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

Yuzwa, S. A., Macauley, M. S., Heinonen, J. E., Shan, X., Dennis, R. J., He, Y., Whitworth, G. E., Stubbs, K. A., McEachern, E. J., Davies, G. J., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.96 · Cited by 717

Insights into DNA recombination from the structure of a RAD51–BRCA2 complex

Pellegrini, L., Yu, D. S., Lo, T., Anand, S., Lee, M., Blundell, T. L., & Venkitaraman, A. R. (2002) · Nature · doi:10.1038/nature01230 · Cited by 704

Retroviral intasome assembly and inhibition of DNA strand transfer

Hare, S., Gupta, S. S., Valkov, E., Engelman, A., & Cherepanov, P. (2010) · Nature · doi:10.1038/nature08784 · Cited by 678

Targeting C-reactive protein for the treatment of cardiovascular disease.

Pepys, M. B., Hirschfield, G. M., Tennent, G. A., Ruth Gallimore, J., Kahan, M. C., Bellotti, V., Hawkins, P. N., Myers, R. M., Smith, M. D., Polara, A., et al. (2006) · Nature · doi:10.1038/nature04672 · Cited by 672

Molecular Architecture and Functional Model of the Endocytic AP2 Complex

Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R., & Owen, D. J. (2002) · Cell · doi:10.1016/s0092-8674(02)00735-3 · Cited by 648

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

Structural Evidence for Ligand Specificity in the Binding Domain of the Human Androgen Receptor

Matias, P. M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Macedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004571200 · Cited by 608

Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604

Structural, Biochemical, and Clinical Characterization of Epidermal Growth Factor Receptor (EGFR) Exon 20 Insertion Mutations in Lung Cancer

Yasuda, H., Park, E., Yun, C.-H., Sng, N. J., Lucena-Araujo, A. R., Yeo, W.-L., Huberman, M. S., Cohen, D. W., Nakayama, S., Ishioka, K., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007205 · Cited by 571

A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models

Chan-Penebre, E., Kuplast, K. G., Majer, C. R., Boriack-Sjodin, P. A., Wigle, T. J., Johnston, L. D., Rioux, N., Munchhof, M. J., Jin, L., Jacques, S. L., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1810 · Cited by 569

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

Morton, W. M., Ayscough, K. R., & McLaughlin, P. J. (2000) · Nature Cell Biology · doi:10.1038/35014075 · Cited by 523

X-Ray Structures of the Hexameric Building Block of the HIV Capsid

Pornillos, O., Ganser-Pornillos, B. K., Kelly, B. N., Hua, Y., Whitby, F. G., Stout, C. D., Sundquist, W. I., Hill, C. P., & Yeager, M. (2009) · Cell · doi:10.1016/j.cell.2009.04.063 · Cited by 523

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513

Structure and control of the actin regulatory WAVE complex

Chen, Z., Borek, D., Padrick, S. B., Gomez, T. S., Metlagel, Z., Ismail, A. M., Umetani, J., Billadeau, D. D., Otwinowski, Z., & Rosen, M. K. (2010) · Nature · doi:10.1038/nature09623 · Cited by 500

Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491

Hachimoji DNA and RNA: A genetic system with eight building blocks.

Hoshika, S., Leal, N. A., Kim, M.-J., Kim, M.-S., Karalkar, N. B., Kim, H.-J., Bates, A. M., Watkins, N. E., SantaLucia, H. A., Meyer, A. J., et al. (2019) · Science · doi:10.1126/science.aat0971 · Cited by 494

Structural insight into filament formation by mammalian septins

Sirajuddin, M., Farkasovsky, M., Hauer, F., Kühlmann, D., Macara, I. G., Weyand, M., Stark, H., & Wittinghofer, A. (2007) · Nature · doi:10.1038/nature06052 · Cited by 481

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

A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment

Hyer, M. L., Milhollen, M. A., Ciavarri, J., Fleming, P., Traore, T., Sappal, D., Huck, J., Shi, J., Gavin, J., Brownell, J., et al. (2018) · Nature Medicine · doi:10.1038/nm.4474 · Cited by 447

The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation

Fischer, E. S., Scrima, A., Böhm, K., Matsumoto, S., Lingaraju, G. M., Faty, M., Yasuda, T., Cavadini, S., Wakasugi, M., Hanaoka, F., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.035 · Cited by 460

Structural Analysis Reveals that Toll-like Receptor 7 Is a Dual Receptor for Guanosine and Single-Stranded RNA

Zhang, Z., Ohto, U., Shibata, T., Krayukhina, E., Taoka, M., Yamauchi, Y., Tanji, H., Isobe, T., Uchiyama, S., Miyake, K., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.09.011 · Cited by 461

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.

(2000) · Nature Structural Biology · doi:10.1038/80981 · Cited by 448

Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex

Scrima, A., Koníčková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., & Thomä, N. H. (2008) · Cell · doi:10.1016/j.cell.2008.10.045 · Cited by 441

Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Liu, S., Widom, J., Kemp, C. W., Crews, C. M., & Clardy, J. (1998) · Science · doi:10.1126/science.282.5392.1324 · Cited by 440

Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser

Redecke, L., Nass, K., DePonte, D. P., White, T. A., Rehders, D., Barty, A., Stellato, F., Liang, M., Barends, T. R. M., Boutet, S., et al. (2013) · Science · doi:10.1126/science.1229663 · Cited by 440

The Molecular Basis of Filamin Binding to Integrins and Competition with Talin

Kiema, T., Lad, Y., Jiang, P., Oxley, C. L., Baldassarre, M., Wegener, K. L., Campbell, I. D., Ylänne, J., & Calderwood, D. A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.011 · Cited by 434

Structural Basis of DNA Recognition by p53 Tetramers

Kitayner, M., Rozenberg, H., Kessler, N., Rabinovich, D., Shaulov, L., Haran, T. E., & Shakked, Z. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.015 · Cited by 408

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J. M., Delarue, M., & Corringer, P.-J. (2011) · Nature · doi:10.1038/nature09647 · Cited by 412

The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility

Kozielski, F., Sack, S., Marx, A., Thormählen, M., Schönbrunn, E., Biou, V, Thompson, A., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80489-4 · Cited by 408

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75

Cherepanov, P., Ambrosio, A. L. B., Rahman, S., Ellenberger, T., & Engelman, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506924102 · Cited by 408

Toll-like receptor 8 senses degradation products of single-stranded RNA

Tanji, H., Ohto, U., Shibata, T., Taoka, M., Yamauchi, Y., Isobe, T., Miyake, K., & Shimizu, T. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2943 · Cited by 404

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

Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX

Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391

Molecular basis for LDL receptor recognition by PCSK9

Kwon, H. J., Lagace, T. A., McNutt, M. C., Horton, J. D., & Deisenhofer, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712064105 · Cited by 389

Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens

Damo, S. M., Kehl-Fie, T. E., Sugitani, N., Holt, M. E., Rathi, S., Murphy, W. J., Zhang, Y., Betz, C., Hench, L., Fritz, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220341110 · Cited by 388

Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs

Kambach, C., Walke, S., Young, R., Avis, J. M., de la Fortelle, E., Raker, V. A., Lührmann, R., Li, J., & Nagai, K. (1999) · Cell · doi:10.1016/s0092-8674(00)80550-4 · Cited by 387

Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9

Ohto, U., Shibata, T., Tanji, H., Ishida, H., Krayukhina, E., Uchiyama, S., Miyake, K., & Shimizu, T. (2015) · Nature · doi:10.1038/nature14138 · Cited by 377

Molecular mechanism of strigolactone perception by DWARF14

Nakamura, H., Xue, Y.-L., Miyakawa, T., Hou, F., Qin, H.-M., Fukui, K., Shi, X., Ito, E., Ito, S., Park, S.-H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3613 · Cited by 378

Structural Basis of Substrate Recognition by the Multidrug Resistance Protein MRP1

Johnson, Z. L., & Chen, J. (2017) · Cell · doi:10.1016/j.cell.2017.01.041 · Cited by 375

Targeting a neoantigen derived from a common TP53 mutation

Hsiue, E. H.-C., Wright, K. M., Douglass, J., Hwang, M. S., Mog, B. J., Pearlman, A. H., Paul, S., DiNapoli, S. R., Konig, M. F., Wang, Q., et al. (2021) · Science · doi:10.1126/science.abc8697 · Cited by 367

Tau filaments from multiple cases of sporadic and inherited Alzheimer's disease adopt a common fold

Falcon, B., Zhang, W., Schweighauser, M., Murzin, A. G., Vidal, R., Garringer, H. J., Ghetti, B., Scheres, S. H. W., & Goedert, M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1914-z · Cited by 362

A Small-Molecule Antagonist of HIF2α Is Efficacious in Preclinical Models of Renal Cell Carcinoma

Wallace, E. M., Rizzi, J. P., Han, G., Wehn, P. M., Cao, Z., Du, X., Cheng, T., Czerwinski, R. M., Dixon, D. D., Goggin, B. S., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0473 · Cited by 336

Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol

Duin, E. C., Wagner, T., Shima, S., Prakash, D., Cronin, B., Yáñez-Ruiz, D. R., Duval, S., Rümbeli, R., Stemmler, R. T., Thauer, R. K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600298113 · Cited by 339

Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel–Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7

Zoppi, V., Hughes, S. J., Maniaci, C., Testa, A., Gmaschitz, T., Wieshofer, C., Koegl, M., Riching, K. M., Daniels, D. L., Spallarossa, A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01413 · Cited by 336

N- and C-Terminal Flanking Regions Modulate Light-Induced Signal Transduction in the LOV2 Domain of the Blue Light Sensor Phototropin 1 from Avena sativa ,

Halavaty, A. S., & Moffat, K. (2007) · Biochemistry · doi:10.1021/bi701543e · Cited by 317

Engineering an allosteric transcription factor to respond to new ligands

Taylor, N. D., Garruss, A. S., Moretti, R., Chan, S., Arbing, M. A., Cascio, D., Rogers, J. K., Isaacs, F. J., Kosuri, S., Baker, D., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3696 · Cited by 328

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326

Monoacidic Inhibitors of the Kelch-like ECH-Associated Protein 1: Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein–Protein Interaction with High Cell Potency Identified by Fragment-Based Discovery

Davies, T. G., Wixted, W. E., Coyle, J. E., Griffiths-Jones, C., Hearn, K., McMenamin, R., Norton, D., Rich, S. J., Richardson, C., Saxty, G., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00228 · Cited by 322

The role of protein dynamics in the evolution of new enzyme function

Campbell, E., Kaltenbach, M., Correy, G. J., Carr, P. D., Porebski, B. T., Livingstone, E. K., Afriat-Jurnou, L., Buckle, A. M., Weik, M., Hollfelder, F., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2175 · Cited by 311

Predicting Absolute Ligand Binding Free Energies to a Simple Model Site

Mobley, D. L., Graves, A. P., Chodera, J. D., McReynolds, A. C., Shoichet, B. K., & Dill, K. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.002 · Cited by 310

Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance

Hare, S., Vos, A. M., Clayton, R. F., Thuring, J. W., Cummings, M. D., & Cherepanov, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010246107 · Cited by 305

Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling

Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P. J. G., & McMahon, H. T. (2007) · Nature · doi:10.1038/nature06173 · Cited by 304

The mechanism of retroviral integration from X-ray structures of its key intermediates

Maertens, G. N., Hare, S., & Cherepanov, P. (2010) · Nature · doi:10.1038/nature09517 · Cited by 296

Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W. (2002) · Cell · doi:10.1016/s0092-8674(02)01136-4 · Cited by 302

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284

Crystal structure of nucleotide-free dynamin

Faelber, K., Posor, Y., Gao, S., Held, M., Roske, Y., Schulze, D., Haucke, V., Noé, F., & Daumke, O. (2011) · Nature · doi:10.1038/nature10369 · Cited by 301

Artificial ligand binding within the HIF2α PAS-B domain of the HIF2 transcription factor

Scheuermann, T. H., Tomchick, D. R., Machius, M., Guo, Y., Bruick, R. K., & Gardner, K. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808092106 · Cited by 301

First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity

Sendovski, M., Kanteev, M., Ben-Yosef, V. S., Adir, N., & Fishman, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.048 · Cited by 299

Binding of the PX domain of p47phox to phosphatidylinositol 3,4‐bisphosphate and phosphatidic acid is masked by an intramolecular interaction

Karathanassis, D., Stahelin, R. V., Bravo, J., Perisic, O., Pacold, C. M., Cho, W., & Williams, R. L. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf519 · Cited by 294

Structural basis for a [4Fe–3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase

Shomura, Y., Yoon, K.-S., Nishihara, H., & Higuchi, Y. (2011) · Nature · doi:10.1038/nature10504 · Cited by 290

A Small-Molecule Inhibitor of BCL6 Kills DLBCL Cells In Vitro and In Vivo

Cerchietti, L. C., Ghetu, A. F., Zhu, X., Da Silva, G. F., Zhong, S., Matthews, M., Bunting, K. L., Polo, J. M., Farès, C., Arrowsmith, C. H., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.050 · Cited by 288

Structural basis for sialic acid–mediated self-recognition by complement factor H

Blaum, B. S., Hannan, J. P., Herbert, A. P., Kavanagh, D., Uhrín, D., & Stehle, T. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1696 · Cited by 278

Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers

Swanson, K. A., Settembre, E. C., Shaw, C. A., Dey, A. K., Rappuoli, R., Mandl, C. W., Dormitzer, P. R., & Carfi, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106536108 · Cited by 285

Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex

Esser, L., Quinn, B., Li, Y.-F., Zhang, M., Elberry, M., Yu, L., Yu, C.-A., & Xia, D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.065 · Cited by 285

Pharmacological targeting of the Wdr5-MLL interaction in C/EBPα N-terminal leukemia

Grebien, F., Vedadi, M., Getlik, M., Giambruno, R., Grover, A., Avellino, R., Skucha, A., Vittori, S., Kuznetsova, E., Smil, D., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1859 · Cited by 284

Structure of the CaMKIIδ/Calmodulin Complex Reveals the Molecular Mechanism of CaMKII Kinase Activation

Rellos, P., Pike, A. C. W., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., & Knapp, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000426 · Cited by 279

Comparison of Crystal Structures of Human Androgen Receptor Ligand-Binding Domain Complexed with Various Agonists Reveals Molecular Determinants Responsible for Binding Affinity

Pereira de Jésus‐Tran, K., Côté, P., Cantin, L., Blanchet, J., Labrie, F., & Breton, R. (2006) · Protein Science · doi:10.1110/ps.051905906 · Cited by 278

Hallucinating symmetric protein assemblies

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

Oligomycin Frames a Common Drug-Binding Site in the ATP Synthase

Symersky, J., Osowski, D., Walters, D. E., & Mueller, D. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207912109 · Cited by 269

Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus

Choi, J.-M., Hutson, A. M., Estes, M. K., & Prasad, B. V. V. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803275105 · Cited by 268

Structural and Functional Analyses of the Second-Generation Integrase Strand Transfer Inhibitor Dolutegravir (S/GSK1349572)

Hare, S., Smith, S. J., Métifiot, M., Jaxa-Chamiec, A., Pommier, Y., Hughes, S. H., & Cherepanov, P. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.073189 · Cited by 264

A Basis Set of de Novo Coiled-Coil Peptide Oligomers for Rational Protein Design and Synthetic Biology

Fletcher, J. M., Boyle, A. L., Bruning, M., Bartlett, G. J., Vincent, T. L., Zaccai, N. R., Armstrong, C. T., Bromley, E. H. C., Booth, P. J., Brady, R. L., et al. (2012) · ACS Synthetic Biology · doi:10.1021/sb300028q · Cited by 262

Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex

Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., De Francesco, R., Steinkühler, C., & Di Marco, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401047 · Cited by 256

Structure of a yeast activated spliceosome at 3.5 Å resolution

Yan, C., Wan, R., Bai, R., Huang, G., & Shi, Y. (2016) · Science · doi:10.1126/science.aag0291 · Cited by 261

Structural Insights into Neonatal Fc Receptor-based Recycling Mechanisms

Oganesyan, V., Damschroder, M. M., Cook, K. E., Li, Q., Gao, C., Wu, H., & Dall'Acqua, W. F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537563 · Cited by 259

Selective inhibitors of the FK506-binding protein 51 by induced fit

Gaali, S., Kirschner, A., Cuboni, S., Hartmann, J., Kozany, C., Balsevich, G., Namendorf, C., Fernandez-Vizarra, P., Sippel, C., Zannas, A. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1699 · Cited by 245

Discovery of a Potent Small-Molecule Antagonist of Inhibitor of Apoptosis (IAP) Proteins and Clinical Candidate for the Treatment of Cancer (GDC-0152)

Flygare, J. A., Beresini, M., Budha, N., Chan, H., Chan, I. T., Cheeti, S., Cohen, F., Deshayes, K., Doerner, K., Eckhardt, S. G., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300060k · Cited by 252

Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage

Stella, S., Alcón, P., & Montoya, G. (2017) · Nature · doi:10.1038/nature22398 · Cited by 244

Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis

Shin, O.-H., Lu, J., Rhee, J.-S., Tomchick, D. R., Pang, Z. P., Wojcik, S. M., Camacho-Perez, M., Brose, N., Machius, M., Rizo, J., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1758 · Cited by 243