NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957

Jasmonate perception by inositol-phosphate-potentiated COI1–JAZ co-receptor

Sheard, L. B., Tan, X., Mao, H., Withers, J., Ben-Nissan, G., Hinds, T. R., Kobayashi, Y., Hsu, F.-F., Sharon, M., Browse, J., et al. (2010) · Nature · doi:10.1038/nature09430 · Cited by 1,497

Molecular Interplay of the Noncoding RNA ANRIL and Methylated Histone H3 Lysine 27 by Polycomb CBX7 in Transcriptional Silencing of INK4a

Yap, K. L., Li, S., Muñoz-Cabello, A. M., Raguz, S., Zeng, L., Mujtaba, S., Gil, J., Walsh, M. J., & Zhou, M.-M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.021 · Cited by 1,391

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains

Martin, E. W., Holehouse, A. S., Peran, I., Farag, M., Incicco, J. J., Bremer, A., Grace, C. R., Soranno, A., Pappu, R. V., & Mittag, T. (2020) · Science · doi:10.1126/science.aaw8653 · Cited by 1,147

Reducing the Environmental Sensitivity of Yellow Fluorescent Protein

Griesbeck, O., Baird, G. S., Campbell, R. E., Zacharias, D. A., & Tsien, R. Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102815200 · Cited by 1,023

Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives

Spruijt, C. G., Gnerlich, F., Smits, A. H., Pfaffeneder, T., Jansen, P. W. T. C., Bauer, C., Münzel, M., Wagner, M., Müller, M., Khan, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.004 · Cited by 973

Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations

Hunter, J. C., Manandhar, A., Carrasco, M. A., Gurbani, D., Gondi, S., & Westover, K. D. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0203 · Cited by 786

Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model

Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759

A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors

Melcher, K., Ng, L.-M., Zhou, X. E., Soon, F.-F., Xu, Y., Suino-Powell, K. M., Park, S.-Y., Weiner, J. J., Fujii, H., Chinnusamy, V., et al. (2009) · Nature · doi:10.1038/nature08613 · Cited by 731

Gating the Selectivity Filter in ClC Chloride Channels

Dutzler, R., Campbell, E. B., & MacKinnon, R. (2003) · Science · doi:10.1126/science.1082708 · Cited by 727

Structural basis of a shared antibody response to SARS-CoV-2

Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589

Chitin-Induced Dimerization Activates a Plant Immune Receptor

Liu, T., Liu, Z., Song, C., Hu, Y., Han, Z., She, J., Fan, F., Wang, J., Jin, C., Chang, J., et al. (2012) · Science · doi:10.1126/science.1218867 · Cited by 680

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor

Bowers, E. M., Yan, G., Mukherjee, C., Orry, A., Wang, L., Holbert, M. A., Crump, N. T., Hazzalin, C. A., Liszczak, G., Yuan, H., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.006 · Cited by 666

Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element

De Guzman, R. N., Wu, Z. R., Stalling, C. C., Pappalardo, L., Borer, P. N., & Summers, M. F. (1998) · Science · doi:10.1126/science.279.5349.384 · Cited by 659

Extreme disorder in an ultrahigh-affinity protein complex

Borgia, A., Borgia, M. B., Bugge, K., Kissling, V. M., Heidarsson, P. O., Fernandes, C. B., Sottini, A., Soranno, A., Buholzer, K. J., Nettels, D., et al. (2018) · Nature · doi:10.1038/nature25762 · Cited by 653

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652

Mitochondrial metabolism promotes adaptation to proteotoxic stress

Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645

Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol

Edlich, F., Banerjee, S., Suzuki, M., Cleland, M. M., Arnoult, D., Wang, C., Neutzner, A., Tjandra, N., & Youle, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.02.034 · Cited by 630

De novo protein design by deep network hallucination

Anishchenko, I., Chidyausiku, T. M., Ovchinnikov, S., Pellock, S. J., & Baker, D. (2020) · doi:10.1101/2020.07.22.211482 · Cited by 629

The fibronectin type III domain as a scaffold for novel binding proteins

Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585

The RNA-binding protein KSRP promotes the biogenesis of a subset of microRNAs

Trabucchi, M., Briata, P., Garcia-Mayoral, M., Haase, A. D., Filipowicz, W., Ramos, A., Gherzi, R., & Rosenfeld, M. G. (2009) · Nature · doi:10.1038/nature08025 · Cited by 607

RIM proteins tether Ca2+ channels to presynaptic active zones via a direct PDZ-domain interaction

Kaeser, P. S., Deng, L., Wang, Y., Dulubova, I., Liu, X., Rizo, J., & Südhof, T. C. (2011) · Cell · doi:10.1016/j.cell.2010.12.029 · Cited by 607

Proof of principle for epitope-focused vaccine design

Correia, B. E., Bates, J. T., Loomis, R. J., Baneyx, G., Carrico, C., Jardine, J. G., Rupert, P., Correnti, C., Kalyuzhniy, O., Vittal, V., et al. (2014) · Nature · doi:10.1038/nature12966 · Cited by 555

Global analysis of protein folding using massively parallel design, synthesis, and testing

Rocklin, G. J., Chidyausiku, T. M., Goreshnik, I., Ford, A., Houliston, S., Lemak, A., Carter, L., Ravichandran, R., Mulligan, V. K., Chevalier, A., et al. (2017) · Science · doi:10.1126/science.aan0693 · Cited by 501

Predicting multiple conformations via sequence clustering and AlphaFold2

Wayment-Steele, H. K., Ojoawo, A., Otten, R., Apitz, J. M., Pitsawong, W., Hömberger, M., Ovchinnikov, S., Colwell, L., & Kern, D. (2024) · Nature · doi:10.1038/s41586-023-06832-9 · Cited by 545

Principles for designing ideal protein structures

Koga, N., Tatsumi-Koga, R., Liu, G., Xiao, R., Acton, T. B., Montelione, G. T., & Baker, D. (2012) · Nature · doi:10.1038/nature11600 · Cited by 564

Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation

Trempe, J.-F., Sauvé, V., Grenier, K., Seirafi, M., Tang, M. Y., Ménade, M., Al-Abdul-Wahid, S., Krett, J., Wong, K., Kozlov, G., et al. (2013) · Science · doi:10.1126/science.1237908 · Cited by 523

Histamine Derived from Probiotic Lactobacillus reuteri Suppresses TNF via Modulation of PKA and ERK Signaling

Thomas, C. M., Hong, T., van Pijkeren, J. P., Hemarajata, P., Trinh, D. V., Hu, W., Britton, R. A., Kalkum, M., & Versalovic, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031951 · Cited by 491

AG-221, a First-in-Class Therapy Targeting Acute Myeloid Leukemia Harboring Oncogenic IDH2 Mutations

Yen, K., Travins, J., Wang, F., David, M. D., Artin, E., Straley, K., Padyana, A., Gross, S., DeLaBarre, B., Tobin, E., et al. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-1034 · Cited by 471

Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis

Itoh, T., Koshiba, S., Kigawa, T., Kikuchi, A., Yokoyama, S., & Takenawa, T. (2001) · Science · doi:10.1126/science.291.5506.1047 · Cited by 469

The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol

Barrett, P. J., Song, Y., Van Horn, W. D., Hustedt, E. J., Schafer, J. M., Hadziselimovic, A., Beel, A. J., & Sanders, C. R. (2012) · Science · doi:10.1126/science.1219988 · Cited by 467

Graphene quantum dots prevent α-synucleinopathy in Parkinson’s disease

Kim, D., Yoo, J. M., Hwang, H., Lee, J., Lee, S. H., Yun, S. P., Park, M. J., Lee, M., Choi, S., Kwon, S. H., et al. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0179-y · Cited by 455

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

Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability

Lauffer, B. E. L., Mintzer, R., Fong, R., Mukund, S., Tam, C., Zilberleyb, I., Flicke, B., Ritscher, A., Fedorowicz, G., Vallero, R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490706 · Cited by 429

Chloride sensing by WNK1 involves inhibition of autophosphorylation

Piala, A. T., Moon, T. M., Akella, R., He, H., Cobb, M. H., & Goldsmith, E. J. (2014) · Science Signaling · doi:10.1126/scisignal.2005050 · Cited by 418

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

Munc13 mediates the transition from the closed syntaxin–Munc18 complex to the SNARE complex

Ma, C., Li, W., Xu, Y., & Rizo, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2047 · Cited by 363

E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages

Christensen, D. E., Brzovic, P. S., & Klevit, R. E. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1295 · Cited by 351

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346

Drosophila PIWI associates with chromatin and interacts directly with HP1a

Brower-Toland, B., Findley, S. D., Jiang, L., Liu, L., Yin, H., Dus, M., Zhou, P., Elgin, S. C. R., & Lin, H. (2007) · Genes & Development · doi:10.1101/gad.1564307 · Cited by 350

Solution structure of the N-terminal zinc binding domain of HIV-1 integrase

Cai, M., Zheng, R., Caffrey, M., Craigie, R., Clore, G. M., & Gronenborn, A. M. (1997) · Nature Structural Biology · doi:10.1038/nsb0797-567 · Cited by 342

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

Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes

Cheever, M. L., Sato, T. K., de Beer, T., Kutateladze, T. G., Emr, S. D., & Overduin, M. (2001) · Nature Cell Biology · doi:10.1038/35083000 · Cited by 341

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318

Autoregulation of Parkin activity through its ubiquitin‐like domain

Chaugule, V. K., Burchell, L., Barber, K. R., Sidhu, A., Leslie, S. J., Shaw, G. S., & Walden, H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.204 · Cited by 339

Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d

Hudson, B. P., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb738 · Cited by 336

Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501565200 · Cited by 324

Structure of an E3:E2∼Ub Complex Reveals an Allosteric Mechanism Shared among RING/U-box Ligases

Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., & Klevit, R. E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.001 · Cited by 333

Crystal Structure of the Ectodomain of Human Transferrin Receptor

Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C. (1999) · Science · doi:10.1126/science.286.5440.779 · Cited by 315

BH3-Triggered Structural Reorganization Drives the Activation of Proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Davis, M. L., Bird, G. H., & Walensky, L. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.019 · Cited by 310

Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus

Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O., & Clubb, R. T. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101064198 · Cited by 304

Structural basis for protein antiaggregation activity of the trigger factor chaperone.

Saio, T., Guan, X., Rossi, P., Economou, A., & Kalodimos, C. G. (2014) · Science · doi:10.1126/science.1250494 · Cited by 289

A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?

Dulubova, I., Lou, X., Lu, J., Huryeva, I., Alam, A., Schneggenburger, R., Südhof, T. C., & Rizo, J. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600753 · Cited by 289

Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats

Harriman, G., Greenwood, J., Bhat, S., Huang, X., Wang, R., Paul, D., Tong, L., Saha, A. K., Westlin, W. F., Kapeller, R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520686113 · Cited by 287

Secreted amyloid-β precursor protein functions as a GABA B R1a ligand to modulate synaptic transmission

Rice, H. C., de Malmazet, D., Schreurs, A., Frere, S., Van Molle, I., Volkov, A. N., Creemers, E., Vertkin, I., Nys, J., Ranaivoson, F. M., et al. (2019) · Science · doi:10.1126/science.aao4827 · Cited by 281

Structure of the HIV-1 RNA packaging signal

Keane, S. C., Heng, X., Lu, K., Kharytonchyk, S., Ramakrishnan, V., Carter, G., Barton, S., Hosic, A., Florwick, A., Santos, J., et al. (2015) · Science · doi:10.1126/science.aaa9266 · Cited by 278

Conformational states dynamically populated by a kinase determine its function

Xie, T., Saleh, T., Rossi, P., & Kalodimos, C. G. (2020) · Science · doi:10.1126/science.abc2754 · Cited by 266

Covalently circularized nanodiscs for studying membrane proteins and viral entry

Nasr, M. L., Baptista, D., Strauss, M., Sun, Z.-Y. J., Grigoriu, S., Huser, S., Plückthun, A., Hagn, F., Walz, T., Hogle, J. M., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4079 · Cited by 262

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

Jo, H., Meinhardt, N., Wu, Y., Kulkarni, S., Hu, X., Low, K. E., Davies, P. L., DeGrado, W. F., & Greenbaum, D. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307599z · Cited by 261

Visualizing transient Watson–Crick-like mispairs in DNA and RNA duplexes

Kimsey, I. J., Petzold, K., Sathyamoorthy, B., Stein, Z. W., & Al-Hashimi, H. M. (2015) · Nature · doi:10.1038/nature14227 · 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

Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release

Nowotny, M., & Yang, W. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601076 · Cited by 250

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

Glucosylceramide synthase is an essential regulator of pathogenicity of Cryptococcus neoformans

Rittershaus, P. C. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27890 · Cited by 239

Loss of succinate dehydrogenase activity results in dependency on pyruvate carboxylation for cellular anabolism

Lussey-Lepoutre, C., Hollinshead, K. E. R., Ludwig, C., Menara, M., Morin, A., Castro-Vega, L.-J., Parker, S. J., Janin, M., Martinelli, C., Ottolenghi, C., et al. (2015) · Nature Communications · doi:10.1038/ncomms9784 · Cited by 227

Teaching an Old Scaffold New Tricks: Monobodies Constructed Using Alternative Surfaces of the FN3 Scaffold

Koide, A., Wojcik, J., Gilbreth, R. N., Hoey, R. J., & Koide, S. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.019 · Cited by 227

Crystal Structure of Human Frataxin

Dhe-Paganon, S., Shigeta, R., Chi, Y.-I., Ristow, M., & Shoelson, S. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000407200 · Cited by 226

The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation

Bottomley (2001) · Nature Structural Biology · doi:10.1038/89675 · Cited by 224

Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

Schwarten, M., Mohrlüder, J., Ma, P., Stoldt, M., Thielmann, Y., Stangler, T., Hersch, N., Hoffmann, B., Merkel, R., & Willbold, D. (2009) · Autophagy · doi:10.4161/auto.5.5.8494 · Cited by 224

Crystal structure of an IRF‐DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences

Fujii, Y., Shimizu, T., Kusumoto, M., Kyogoku, Y., Taniguchi, T., & Hakoshima, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5028 · Cited by 223

Hepcidin Revisited, Disulfide Connectivity, Dynamics, and Structure

Jordan, J. B., Poppe, L., Haniu, M., Arvedson, T., Syed, R., Li, V., Kohno, H., Kim, H., Schnier, P. D., Harvey, T. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017764 · Cited by 214

Interaction between Aβ Peptide and α Synuclein: Molecular Mechanisms in Overlapping Pathology of Alzheimer’s and Parkinson’s in Dementia with Lewy Body Disease

Mandal, P. K., Pettegrew, J. W., Masliah, E., Hamilton, R. L., & Mandal, R. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9140-9 · Cited by 219

Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes

Eidahl, J. O., Crowe, B. L., North, J. A., McKee, C. J., Shkriabai, N., Feng, L., Plumb, M., Graham, R. L., Gorelick, R. J., Hess, S., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt074 · Cited by 207

Antiparallel EmrE exports drugs by exchanging between asymmetric structures

Morrison, E. A., DeKoster, G. T., Dutta, S., Vafabakhsh, R., Clarkson, M. W., Bahl, A., Kern, D., Ha, T., & Henzler-Wildman, K. A. (2012) · Nature · doi:10.1038/nature10703 · Cited by 215

Val66Met polymorphism of BDNF alters prodomain structure to induce neuronal growth cone retraction

Anastasia, A., Deinhardt, K., Chao, M. V., Will, N. E., Irmady, K., Lee, F. S., Hempstead, B. L., & Bracken, C. (2013) · Nature Communications · doi:10.1038/ncomms3490 · Cited by 215

A protein fold switch joins the circadian oscillator to clock output in cyanobacteria

Chang, Y.-G., Cohen, S. E., Phong, C., Myers, W. K., Kim, Y.-I., Tseng, R., Lin, J., Zhang, L., Boyd, J. S., Lee, Y., et al. (2015) · Science · doi:10.1126/science.1260031 · Cited by 212

Structures of the σ2 receptor enable docking for bioactive ligand discovery

Alon, A., Lyu, J., Braz, J. M., Tummino, T. A., Craik, V., O’Meara, M. J., Webb, C. M., Radchenko, D. S., Moroz, Y. S., Huang, X.-P., et al. (2021) · Nature · doi:10.1038/s41586-021-04175-x · Cited by 211

Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein

Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205

The Acidic Transcription Activator Gcn4 Binds the Mediator Subunit Gal11/Med15 Using a Simple Protein Interface Forming a Fuzzy Complex

Brzovic, P. S., Heikaus, C. C., Kisselev, L., Vernon, R., Herbig, E., Pacheco, D., Warfield, L., Littlefield, P., Baker, D., Klevit, R. E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.008 · Cited by 203

High-throughput prediction of protein conformational distributions with subsampled AlphaFold2

Monteiro da Silva, G., Cui, J. Y., Dalgarno, D. C., Lisi, G. P., & Rubenstein, B. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46715-9 · Cited by 196

Broadband homonuclear correlation spectroscopy driven by combined R2nv sequences under fast magic angle spinning for NMR structural analysis of organic and biological solids

Hou, G., Yan, S., Trébosc, J., Amoureux, J.-P., & Polenova, T. (2013) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2013.04.009 · Cited by 193

Electron crystallography of ultrathin 3D protein crystals: atomic model with charges

Yonekura, K., Kato, K., Ogasawara, M., Tomita, M., & Toyoshima, C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500724112 · Cited by 190

Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis

Starita, L. M., Pruneda, J. N., Lo, R. S., Fowler, D. M., Kim, H. J., Hiatt, J. B., Shendure, J., Brzovic, P. S., Fields, S., & Klevit, R. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303309110 · Cited by 183

Cooperativity in Transcription Factor Binding to the Coactivator CREB-binding Protein (CBP)

Goto, N. K., Zor, T., Martinez-Yamout, M., Dyson, H. J., & Wright, P. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207660200 · Cited by 177

Degradation of MEPE, DMP1, and release of SIBLING ASARM-Peptides (Minhibins): ASARM-Peptide(s) are directly responsible for defective mineralization in HYP

Martin, A., David, V., Laurence, J. S., Schwarz, P. M., Lafer, E. M., Hedge, A.-M., & Rowe, P. S. N. (2008) · Endocrinology · doi:10.1210/en.2007-1205 · Cited by 173

Chemical and structural studies provide a mechanistic basis for recognition of the MYC G-quadruplex

Calabrese, D. R., Chen, X., Leon, E. C., Gaikwad, S. M., Phyo, Z., Hewitt, W. M., Alden, S., Hilimire, T. A., He, F., Michalowski, A. M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06315-w · Cited by 172

Phase Separation-Mediated TARP/MAGUK Complex Condensation and AMPA Receptor Synaptic Transmission

Zeng, M., Díaz-Alonso, J., Ye, F., Chen, X., Xu, J., Ji, Z., Nicoll, R. A., & Zhang, M. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.001 · Cited by 171

Domain Architectures and Characterization of an RNA-binding Protein, TLS

Iko, Y., Kodama, T. S., Kasai, N., Oyama, T., Morita, E. H., Muto, T., Okumura, M., Fujii, R., Takumi, T., Tate, S.-I., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408552200 · Cited by 168

Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein

Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151

The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability

Babon, J. J., McManus, E. J., Yao, S., DeSouza, D. P., Mielke, L. A., Sprigg, N. S., Willson, T. A., Hilton, D. J., Nicola, N. A., Baca, M., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.024 · Cited by 163

Antioxidant Peptidomics Reveals Novel Skin Antioxidant System

Yang, H., Wang, X., Liu, X., Wu, J., Liu, C., Gong, W., Zhao, Z., Hong, J., Lin, D., Wang, Y., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800297-mcp200 · Cited by 156

Structural basis of adhesion‐molecule recognition by ERM proteins revealed by the crystal structure of the radixin—ICAM‐2 complex

Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S., & Hakoshima, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg039 · Cited by 155

Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006927200 · Cited by 152

Discovery and characterization of small molecules that target the GTPase Ral

Yan, C., Liu, D., Li, L., Wempe, M. F., Guin, S., Khanna, M., Meier, J., Hoffman, B., Owens, C., Wysoczynski, C. L., et al. (2014) · Nature · doi:10.1038/nature13713 · Cited by 150

Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules

Fischer, D., Mukrasch, M. D., Biernat, J., Bibow, S., Blackledge, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · Biochemistry · doi:10.1021/bi901090m · Cited by 149

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148

Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron–Sulfur Cluster Biosynthesis

Cai, K., Tonelli, M., Frederick, R. O., & Markley, J. L. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b00447 · Cited by 148

Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase

Jin, R., Junutula, J. R., Matern, H. T., Ervin, K. E., Scheller, R. H., & Brunger, A. T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600699 · Cited by 145

Structure and mutagenesis of the Dbl homology domain

Aghazadeh, B., Zhu, K., Kubiseski, T. J., Liu, G. A., Pawson, T., Zheng, Y., & Rosen, M. K. (1998) · Nature Structural Biology · doi:10.1038/4209 · Cited by 145