Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Structures of D 14 and D 14 L in the strigolactone and karrikin signaling pathways

Kagiyama, M., Hirano, Y., Mori, T., Kim, S., Kyozuka, J., Seto, Y., Yamaguchi, S., & Hakoshima, T. (2013) · Genes to Cells · doi:10.1111/gtc.12025 · Cited by 240

Axitinib effectively inhibits BCR-ABL1(T315I) with a distinct binding conformation

Pemovska, T., Johnson, E., Kontro, M., Repasky, G. A., Chen, J., Wells, P., Cronin, C. N., McTigue, M., Kallioniemi, O., Porkka, K., et al. (2015) · Nature · doi:10.1038/nature14119 · Cited by 234

Anti-obesity effects of GIPR antagonists alone and in combination with GLP-1R agonists in preclinical models

Killion, E. A., Wang, J., Yie, J., Shi, S. D.-H., Bates, D., Min, X., Komorowski, R., Hager, T., Deng, L., Atangan, L., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aat3392 · Cited by 237

Long-acting MIC-1/GDF15 molecules to treat obesity: Evidence from mice to monkeys

Xiong, Y., Walker, K., Min, X., Hale, C., Tran, T., Komorowski, R., Yang, J., Davda, J., Nuanmanee, N., Kemp, D., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aan8732 · Cited by 236

Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates

Hewitson, K. S., Liénard, B. M. R., McDonough, M. A., Clifton, I. J., Butler, D., Soares, A. S., Oldham, N. J., McNeill, L. A., & Schofield, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608337200 · Cited by 235

Discovery and characterization of highly potent and selective allosteric USP7 inhibitors

Gavory, G., O'Dowd, C. R., Helm, M. D., Flasz, J., Arkoudis, E., Dossang, A., Hughes, C., Cassidy, E., McClelland, K., Odrzywol, E., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2528 · Cited by 224

Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor

Blair, D. E., Schüttelkopf, A. W., MacRae, J. I., & van Aalten, D. M. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504339102 · Cited by 230

Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin

Byres, E., Paton, A. W., Paton, J. C., Löfling, J. C., Smith, D. F., Wilce, M. C. J., Talbot, U. M., Chong, D. C., Yu, H., Huang, S., et al. (2008) · Nature · doi:10.1038/nature07428 · Cited by 233

FtsA forms actin‐like protofilaments

Szwedziak, P., Wang, Q., Freund, S. M., & Löwe, J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.76 · Cited by 233

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

Ubiquitin Recognition by the Human TSG101 Protein

Sundquist, W. I., Schubert, H. L., Kelly, B. N., Hill, G. C., Holton, J. M., & Hill, C. P. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00129-7 · Cited by 223

Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins

Zanier, K., Charbonnier, S., Sidi, A. O. M. O., McEwen, A. G., Ferrario, M. G., Poussin-Courmontagne, P., Cura, V., Brimer, N., Babah, K. O., Ansari, T., et al. (2013) · Science · doi:10.1126/science.1229934 · Cited by 222

The EED protein–protein interaction inhibitor A-395 inactivates the PRC2 complex

He, Y., Selvaraju, S., Curtin, M. L., Jakob, C. G., Zhu, H., Comess, K. M., Shaw, B., The, J., Lima-Fernandes, E., Szewczyk, M. M., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2306 · Cited by 224

Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d

Brotherton, D. H., Dhanaraj, V., Wick, S., Brizuela, L., Domaille, P. J., Volyanik, E., Xu, X., Parisini, E., Smith, B. O., Archer, S. J., et al. (1998) · Nature · doi:10.1038/26164 · Cited by 210

The Potent BACE1 Inhibitor LY2886721 Elicits Robust Central Aβ Pharmacodynamic Responses in Mice, Dogs, and Humans

May, P. C., Willis, B. A., Lowe, S. L., Dean, R. A., Monk, S. A., Cocke, P. J., Audia, J. E., Boggs, L. N., Borders, A. R., Brier, R. A., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4129-14.2015 · Cited by 206

Structural Characterisation Reveals Mechanism of IL-13-Neutralising Monoclonal Antibody Tralokinumab as Inhibition of Binding to IL-13Rα1 and IL-13Rα2

Popovic, B., Breed, J., Rees, D. G., Gardener, M. J., Vinall, L. M. K., Kemp, B., Spooner, J., Keen, J., Minter, R., Uddin, F., et al. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.12.005 · Cited by 198

Molecular basis for SNX‐BAR‐mediated assembly of distinct endosomal sorting tubules

van Weering, J. R. T., Sessions, R. B., Traer, C. J., Kloer, D. P., Bhatia, V. K., Stamou, D., Carlsson, S. R., Hurley, J. H., & Cullen, P. J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.283 · Cited by 200

Structure of a Lipid Droplet Protein

Hickenbottom, S. J., Kimmel, A. R., Londos, C., & Hurley, J. H. (2004) · Structure · doi:10.1016/j.str.2004.04.021 · 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

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190

Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch

Ren, A., Rajashankar, K. R., & Patel, D. J. (2012) · Nature · doi:10.1038/nature11152 · Cited by 189

CR8, a potent and selective, roscovitine-derived inhibitor of cyclin-dependent kinases

Bettayeb, K., Oumata, N., Echalier, A., Ferandin, Y., Endicott, J. A., Galons, H., & Meijer, L. (2008) · Oncogene · doi:10.1038/onc.2008.191 · Cited by 184

The methanogenic CO 2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters

Wagner, T., Ermler, U., & Shima, S. (2016) · Science · doi:10.1126/science.aaf9284 · Cited by 184

RAC1 P29S is a spontaneously activating cancer-associated GTPase

Davis, M. J., Ha, B. H., Holman, E. C., Halaban, R., Schlessinger, J., & Boggon, T. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220895110 · Cited by 180

Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains

Barthelemy, P. A., Raab, H., Appleton, B. A., Bond, C. J., Wu, P., Wiesmann, C., & Sidhu, S. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708536200 · Cited by 179

Structures of human Patched and its complex with native palmitoylated sonic hedgehog

Qi, X., Schmiege, P., Coutavas, E., Wang, J., & Li, X. (2018) · Nature · doi:10.1038/s41586-018-0308-7 · Cited by 178

Structural Basis of Signaling Blockade by Anti-IL-13 Antibody Lebrikizumab

Ultsch, M., Bevers, J., Nakamura, G., Vandlen, R., Kelley, R. F., Wu, L. C., & Eigenbrot, C. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.01.024 · Cited by 174

Design of a Janus Kinase 3 (JAK3) Specific Inhibitor 1-((2 S,5 R)-5-((7 H-Pyrrolo[2,3-d]pyrimidin-4-yl)amino)-2-methylpiperidin-1-yl)prop-2-en-1-one (PF-06651600) Allowing for the Interrogation of JAK3 Signaling in Humans

Thorarensen, A., Dowty, M. E., Banker, M. E., Juba, B., Jussif, J., Lin, T., Vincent, F., Czerwinski, R. M., Casimiro-Garcia, A., Unwalla, R., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01694 · Cited by 176

Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery

Oberoi, J., Fairall, L., Watson, P. J., Yang, J.-C., Czimmerer, Z., Kampmann, T., Goult, B. T., Greenwood, J. A., Gooch, J. T., Kallenberger, B. C., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1983 · Cited by 165

Haem recognition by a Staphylococcus aureus NEAT domain

Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05502.x · Cited by 166

A Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75

Hare, S., Shun, M.-C., Gupta, S. S., Valkov, E., Engelman, A., & Cherepanov, P. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000259 · Cited by 166

Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3

Kamadurai, H. B., Qiu, Y., Deng, A., Harrison, J. S., MacDonald, C., Actis, M., Rodrigues, P., Miller, D. J., Souphron, J., Lewis, S. M., et al. (2013) · eLife · doi:10.7554/elife.00828 · Cited by 165

A molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex

Clairfeuille, T., Mas, C., Chan, A. S. M., Yang, Z., Tello-Lafoz, M., Chandra, M., Widagdo, J., Kerr, M. C., Paul, B., Mérida, I., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3290 · Cited by 164

Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus

Beasley, F. C., Vinés, E. D., Grigg, J. C., Zheng, Q., Liu, S., Lajoie, G. A., Murphy, M. E. P., & Heinrichs, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06698.x · Cited by 163

Molecular Dynamics—Solvated Interaction Energy Studies of Protein–Protein Interactions: The MP1–p14 Scaffolding Complex

Cui, Q., Sulea, T., Schrag, J. D., Munger, C., Hung, M.-N., Naïm, M., Cygler, M., & Purisima, E. O. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.035 · Cited by 162

3′‐Processing and strand transfer catalysed by retroviral integrase in crystallo

Hare, S., Maertens, G. N., & Cherepanov, P. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.118 · Cited by 153

Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer’s disease

Zhang, Z., Obianyo, O., Dall, E., Du, Y., Fu, H., Liu, X., Kang, S. S., Song, M., Yu, S.-P., Cabrele, C., et al. (2017) · Nature Communications · doi:10.1038/ncomms14740 · Cited by 146

Crystal Structure and Deletion Analysis Show that the Accessory Subunit of Mammalian DNA Polymerase γ, PolγB, Functions as a Homodimer

Carrodeguas, J. A., Theis, K., Bogenhagen, D. F., & Kisker, C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00153-8 · Cited by 150

Structural basis and regulation of the reductive stress response

Manford, A. G., Mena, E. L., Shih, K. Y., Gee, C. L., McMinimy, R., Martínez-González, B., Sherriff, R., Lew, B., Zoltek, M., Rodríguez-Pérez, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.002 · Cited by 152

Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation

Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149

Reversible Sequestration of Active Site Cysteines in a 2Fe-2S-bridged Dimer Provides a Mechanism for Glutaredoxin 2 Regulation in Human Mitochondria

Johansson, C., Kavanagh, K. L., Gileadi, O., & Oppermann, U. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608179200 · Cited by 147

Principles for computational design of binding antibodies

Baran, D., Pszolla, M. G., Lapidoth, G. D., Norn, C., Dym, O., Unger, T., Albeck, S., Tyka, M. D., & Fleishman, S. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707171114 · Cited by 136

The IsdG‐family of haem oxygenases degrades haem to a novel chromophore

Reniere, M. L., Ukpabi, G. N., Harry, S. R., Stec, D. F., Krull, R., Wright, D. W., Bachmann, B. O., Murphy, M. E., & Skaar, E. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07076.x · Cited by 139

The structural basis for tight control of PP2A methylation and function by LCMT-1

Stanevich, V., Jiang, L., Satyshur, K. A., Li, Y., Jeffrey, P. D., Li, Z., Menden, P., Semmelhack, M. F., & Xing, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.030 · Cited by 142

New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)

Müller, A., Müller, J. J., Muller, Y. A., Uhlmann, H., Bernhardt, R., & Heinemann, U. (1998) · Structure · doi:10.1016/s0969-2126(98)00031-8 · Cited by 142

Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase

Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604172200 · Cited by 143

Large FK506-binding proteins shape the pharmacology of rapamycin

März, A. M., Fabian, A.-K., Kozany, C., Bracher, A., & Hausch, F. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00678-12 · Cited by 141

Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor

Yoshikawa, S., Kukimoto-Niino, M., Parker, L., Handa, N., Terada, T., Fujimoto, T., Terazawa, Y., Wakiyama, M., Sato, M., Sano, S., et al. (2013) · Oncogene · doi:10.1038/onc.2012.21 · Cited by 138

Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design

Krajewski, W. W., Collins, R., Holmberg-Schiavone, L., Jones, T. A., Karlberg, T., & Mowbray, S. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.029 · Cited by 135

Restricted leucine zipper dimerization and specificity of DNA recognition of the melanocyte master regulator MITF

Pogenberg, V., Ögmundsdóttir, M. H., Bergsteinsdóttir, K., Schepsky, A., Phung, B., Deineko, V., Milewski, M., Steingrímsson, E., & Wilmanns, M. (2012) · Genes & Development · doi:10.1101/gad.198192.112 · Cited by 137

TGFβ2 and TGFβ3 isoforms drive fibrotic disease pathogenesis

Sun, T., Huang, Z., Liang, W.-C., Yin, J., Lin, W. Y., Wu, J., Vernes, J.-M., Lutman, J., Caplazi, P., Jeet, S., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe0407 · Cited by 134

Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling

de Araujo, M. E. G., Naschberger, A., Fürnrohr, B. G., Stasyk, T., Dunzendorfer-Matt, T., Lechner, S., Welti, S., Kremser, L., Shivalingaiah, G., Offterdinger, M., et al. (2017) · Science · doi:10.1126/science.aao1583 · Cited by 134

Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria

Luo, X., Fu, G., Wang, R. E., Zhu, X., Zambaldo, C., Liu, R., Liu, T., Lyu, X., Du, J., Xuan, W., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2405 · Cited by 134

Functional and structural characterization of the integrase from the prototype foamy virus

Valkov, E., Gupta, S. S., Hare, S., Helander, A., Roversi, P., McClure, M., & Cherepanov, P. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn938 · Cited by 130

Structural Basis for a Munc13–1 Homodimer to Munc13–1/RIM Heterodimer Switch

Lu, J., Machius, M., Dulubova, I., Dai, H., Südhof, T. C., Tomchick, D. R., & Rizo, J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040192 · Cited by 132

The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain

Xu, C., Bian, C., Lam, R., Dong, A., & Min, J. (2011) · Nature Communications · doi:10.1038/ncomms1237 · Cited by 130

Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity

Saul, F. A., Arié, J.-P., Vulliez-le Normand, B., Kahn, R., Betton, J.-M., & Bentley, G. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.056 · Cited by 130

Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106

Su, D., Hu, Q., Li, Q., Thompson, J. R., Cui, G., Fazly, A., Davies, B. A., Botuyan, M. V., Zhang, Z., & Mer, G. (2012) · Nature · doi:10.1038/nature10861 · Cited by 128

Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor

Booe, J. M., Walker, C. S., Barwell, J., Kuteyi, G., Simms, J., Jamaluddin, M. A., Warner, M. L., Bill, R. M., Harris, P. W., Brimble, M. A., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.018 · Cited by 122

Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains

Lundell, A., Olin, A. I., Mörgelin, M., al-Karadaghi, S., Aspberg, A., & Logan, D. T. (2004) · Structure · doi:10.1016/j.str.2004.05.021 · Cited by 127

The Rap–RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues

Scrima, A., Thomas, C., Deaconescu, D., & Wittinghofer, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.30 · Cited by 127

Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination

Sheikh, M. A., & Taylor, G. L. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06718.x · Cited by 126

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin

Ultsch, M., Li, B., Maurer, T., Mathieu, M., Adolfsson, O., Muhs, A., Pfeifer, A., Pihlgren, M., Bainbridge, T. W., Reichelt, M., et al. (2016) · Scientific Reports · doi:10.1038/srep39374 · Cited by 124

A New Class of Multimerization Selective Inhibitors of HIV-1 Integrase

Sharma, A., Slaughter, A., Jena, N., Feng, L., Kessl, J. J., Fadel, H. J., Malani, N., Male, F., Wu, L., Poeschla, E., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004171 · Cited by 124

Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control

Yang, J.-Y., Deng, X.-Y., Li, Y.-S., Ma, X.-C., Feng, J.-X., Yu, B., Chen, Y., Luo, Y.-L., Wang, X., Chen, M.-L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03544-x · Cited by 124

Crystal structure of human prion protein bound to a therapeutic antibody

Antonyuk, S. V., Trevitt, C. R., Strange, R. W., Jackson, G. S., Sangar, D., Batchelor, M., Cooper, S., Fraser, C., Jones, S., Georgiou, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809170106 · Cited by 124

The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family

Kaiser, L., Grönlund, H., Sandalova, T., Ljunggren, H.-G., van Hage-Hamsten, M., Achour, A., & Schneider, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304740200 · Cited by 122

Structural Basis for Functional Tetramerization of Lentiviral Integrase

Hare, S., Di Nunzio, F., Labeja, A., Wang, J., Engelman, A., & Cherepanov, P. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000515 · Cited by 122

Cardiolipin Binds to CD1d and Stimulates CD1d-Restricted γδ T Cells in the Normal Murine Repertoire

Dieudé, M., Striegl, H., Tyznik, A. J., Wang, J., Behar, S. M., Piccirillo, C. A., Levine, J. S., Zajonc, D. M., & Rauch, J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1000921 · Cited by 121

Crystal Structure of the Heme-IsdC Complex, the Central Conduit of the Isd Iron/Heme Uptake System in Staphylococcus aureus

Sharp, K. H., Schneider, S., Cockayne, A., & Paoli, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700234200 · Cited by 120

Crystal structure of the eIF4A–PDCD4 complex

Chang, J. H., Cho, Y. H., Sohn, S. Y., Choi, J. M., Kim, A., Kim, Y. C., Jang, S. K., & Cho, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808275106 · Cited by 120

Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome

Yatskevich, S., Muir, K. W., Bellini, D., Zhang, Z., Yang, J., Tischer, T., Predin, M., Dendooven, T., McLaughlin, S. H., & Barford, D. (2022) · Science · doi:10.1126/science.abn3810 · Cited by 120

Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus

Lee, W. C., Reniere, M. L., Skaar, E. P., & Murphy, M. E. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709486200 · Cited by 117

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase

Jackson, C. J., Foo, J.-L., Tokuriki, N., Afriat, L., Carr, P. D., Kim, H.-K., Schenk, G., Tawfik, D. S., & Ollis, D. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907548106 · Cited by 119

AdcAII, a new pneumococcal Zn-binding protein homologous with ABC transporters: biochemical and structural analysis

Loisel, E., Jacquamet, L., Serre, L., Bauvois, C., Ferrer, J. L., Vernet, T., Di Guilmi, A. M., & Durmort, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.068 · Cited by 115

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

Najmudin, S., González, P. J., Trincão, J., Coelho, C., Mukhopadhyay, A., Cerqueira, N. M. F. S. A., Romão, C. C., Moura, I., Moura, J. J. G., Brondino, C. D., et al. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0359-6 · Cited by 116

Structural and Functional Organization of the ESCRT-I Trafficking Complex

Kostelansky, M. S., Sun, J., Lee, S., Kim, J., Ghirlando, R., Hierro, A., Emr, S. D., & Hurley, J. H. (2006) · Cell · doi:10.1016/j.cell.2006.01.049 · Cited by 115

Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate

Wu, X., Bradley, M. J., Cai, Y., Kümmel, D., De La Cruz, E. M., Barr, F. A., & Reinisch, K. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110415108 · Cited by 115

The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile

Demmer, J. K., Pal Chowdhury, N., Selmer, T., Ermler, U., & Buckel, W. (2017) · Nature Communications · doi:10.1038/s41467-017-01746-3 · Cited by 114

High-resolution X-ray Structures of Human Apoferritin H-chain Mutants Correlated with Their Activity and Metal-binding Sites

Toussaint, L., Bertrand, L., Hue, L., Crichton, R. R., & Declercq, J.-P. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.010 · Cited by 113

The B‐box dominates SAP‐1–SRF interactions in the structure of the ternary complex

Hassler, M., & Richmond, T. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3018 · Cited by 111

Molecular basis of MAPK-activated protein kinase 2:p38 assembly

White, A., Pargellis, C. A., Studts, J. M., Werneburg, B. G., & Farmer, B. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701679104 · Cited by 111

The C2 domain of SynGAP is essential for stimulation of the Rap GTPase reaction

Pena, V., Hothorn, M., Eberth, A., Kaschau, N., Parret, A., Gremer, L., Bonneau, F., Ahmadian, M. R., & Scheffzek, K. (2008) · The EMBO Reports · doi:10.1038/embor.2008.20 · Cited by 101

Mapping the reaction coordinates of enzymatic defluorination

Chan, P. W. Y., Yakunin, A. F., Edwards, E. A., & Pai, E. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja200277d · Cited by 107

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

Chowdhury, R., Sekirnik, R., Brissett, N. C., Krojer, T., Ho, C.-H., Ng, S. S., Clifton, I. J., Ge, W., Kershaw, N. J., Fox, G. C., et al. (2014) · Nature · doi:10.1038/nature13263 · Cited by 105

c-di-AMP binds the ydaO riboswitch in two pseudo-symmetry–related pockets

Ren, A., & Patel, D. J. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1606 · Cited by 104

Tetrahydrobiopterin biosynthesis as an off-target of sulfa drugs

Haruki, H., Pedersen, M. G., Gorska, K. I., Pojer, F., & Johnsson, K. (2013) · Science · doi:10.1126/science.1232972 · Cited by 101

Selective Inhibition of the Mitochondrial Permeability Transition Pore Protects against Neurodegeneration in Experimental Multiple Sclerosis

Warne, J., Pryce, G., Hill, J. M., Shi, X., Lennerås, F., Puentes, F., Kip, M., Hilditch, L., Walker, P., Simone, M. I., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700385 · Cited by 99

Structural basis for SH3 domain‐mediated high‐affinity binding between Mona/Gads and SLP‐76

Harkiolaki, M., Lewitzky, M., Gilbert, R. J. C., Jones, E., Bourette, R. P., Mouchiroud, G., Sondermann, H., Moarefi, I., & Feller, S. M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg258 · Cited by 102

Structure and function of cohesin's Scc3/SA regulatory subunit

Roig, M. B., Löwe, J., Chan, K.-L., Beckouët, F., Metson, J., & Nasmyth, K. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.08.015 · Cited by 91

High-Affinity Small-Molecule Inhibitors of the Menin-Mixed Lineage Leukemia (MLL) Interaction Closely Mimic a Natural Protein–Protein Interaction

He, S., Senter, T. J., Pollock, J., Han, C., Upadhyay, S. K., Purohit, T., Gogliotti, R. D., Lindsley, C. W., Cierpicki, T., Stauffer, S. R., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401868d · Cited by 99

Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function

Ballandras-Colas, A., Brown, M., Cook, N. J., Dewdney, T. G., Demeler, B., Cherepanov, P., Lyumkis, D., & Engelman, A. N. (2016) · Nature · doi:10.1038/nature16955 · Cited by 98

Inhibitors of androgen receptor activation function-2 (AF2) site identified through virtual screening

Axerio-Cilies, P., Lack, N. A., Nayana, M. R. S., Chan, K. H., Yeung, A., Leblanc, E., Guns, E. S. T., Rennie, P. S., & Cherkasov, A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200532b · Cited by 97

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

Coelho, C., González, P. J., Moura, J. G., Moura, I., Trincão, J., & João Romão, M. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.016 · Cited by 97

Implications of AlphaFold 2 for crystallographic phasing by molecular replacement

McCoy, A. J., Sammito, M. D., & Read, R. J. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321012122 · Cited by 104

Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.

Banci, L., Bertini, I., Calderone, V., Della-Malva, N., Felli, I. C., Neri, S., Pavelkova, A., & Rosato, A. (2009) · Biochemical Journal · doi:10.1042/bj20090422 · Cited by 94

A Structural Rationale for Selective Stabilization of Anti-tumor Interactions of 14-3-3 proteins by Cotylenin A

Ottmann, C., Weyand, M., Sassa, T., Inoue, T., Kato, N., Wittinghofer, A., & Oecking, C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.005 · Cited by 94

Acid-Tolerant Monomeric GFP from Olindias formosa

Shinoda, H., Ma, Y., Nakashima, R., Sakurai, K., Matsuda, T., & Nagai, T. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.12.005 · Cited by 93

Insights into the bacterial transferrin receptor: the structure of transferrin-binding protein B from Actinobacillus pleuropneumoniae

Moraes, T. F., Yu, R.-H., Strynadka, N. C. J., & Schryvers, A. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.029 · Cited by 89

The Structure of the Human Centrin 2-Xeroderma Pigmentosum Group C Protein Complex

Thompson, J. R., Ryan, Z. C., Salisbury, J. L., & Kumar, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513667200 · Cited by 93