MOLREP: an Automated Program for Molecular Replacement

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

The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1

Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y.-S., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,288

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

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

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

An orally available non-nucleotide STING agonist with antitumor activity

Pan, B.-S., Perera, S. A., Piesvaux, J. A., Presland, J. P., Schroeder, G. K., Cumming, J. N., Trotter, B. W., Altman, M. D., Buevich, A. V., Cash, B., et al. (2020) · Science · doi:10.1126/science.aba6098 · Cited by 694

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

Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis

Pepys, M. B., Herbert, J., Hutchinson, W. L., Tennent, G. A., Lachmann, H. J., Gallimore, J. R., Lovat, L. B., Bartfai, T., Alanine, A., Hertel, C., et al. (2002) · Nature · doi:10.1038/417254a · Cited by 540

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

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 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

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

Atomic-level modelling of the HIV capsid

Pornillos, O., Ganser-Pornillos, B. K., & Yeager, M. (2011) · Nature · doi:10.1038/nature09640 · Cited by 372

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

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

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

Crystal Structures of Membrane Transporter MmpL3, an Anti-TB Drug Target

Zhang, B., Li, J., Yang, X., Wu, L., Zhang, J., Yang, Y., Zhao, Y., Zhang, L., Yang, X., Yang, X., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.003 · Cited by 263

Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1

Williams, R. S., Lee, M. S., Hau, D. D., & Glover, J. N. M. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb776 · Cited by 230

The Crystal Structure of Desulfovibrio vulgaris Dissimilatory Sulfite Reductase Bound to DsrC Provides Novel Insights into the Mechanism of Sulfate Respiration

Oliveira, T. F., Vonrhein, C., Matias, P. M., Venceslau, S. S., Pereira, I. A. C., & Archer, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805643200 · Cited by 190

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

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

The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis

Lemieux, M. J., Fischer, S. J., Cherney, M. M., Bateman, K. S., & James, M. N. G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609981104 · Cited by 147

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

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

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

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

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

A Structural Solution for the DNA Polymerase λ-Dependent Repair of DNA Gaps with Minimal Homology

Garcia-Diaz, M., Bebenek, K., Krahn, J. M., Blanco, L., Kunkel, T. A., & Pedersen, L. C. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00061-9 · Cited by 126

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

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

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

Structural basis for kinesin-1:cargo recognition

Pernigo, S., Lamprecht, A., Steiner, R. A., & Dodding, M. P. (2013) · Science · doi:10.1126/science.1234264 · Cited by 117

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

Crystal structure of the Rous sarcoma virus intasome

Yin, Z., Shi, K., Banerjee, S., Pandey, K. K., Bera, S., Grandgenett, D. P., & Aihara, H. (2016) · Nature · doi:10.1038/nature16950 · Cited by 95

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

Molecular Basis of Gain-of-Function LEOPARD Syndrome-Associated SHP2 Mutations

Yu, Z.-H., Zhang, R.-Y., Walls, C. D., Chen, L., Zhang, S., Wu, L., Liu, S., & Zhang, Z.-Y. (2014) · Biochemistry · doi:10.1021/bi5002695 · Cited by 87

Structural basis for the acyl chain selectivity and mechanism of UDP- N -acetylglucosamine acyltransferase

Williams, A. H., & Raetz, C. R. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705833104 · Cited by 84

Pentameric Assembly of Potassium Channel Tetramerization Domain-Containing Protein 5

Dementieva, I. S., Tereshko, V., McCrossan, Z. A., Solomaha, E., Araki, D., Xu, C., Grigorieff, N., & Goldstein, S. A. N. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.030 · Cited by 79

Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Grigg, J. C., Cheung, J., Heinrichs, D. E., & Murphy, M. E. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172924 · Cited by 71

Two Structures of Alliinase from Alliium sativum L.: Apo Form and Ternary Complex with Aminoacrylate Reaction Intermediate Covalently Bound to the PLP Cofactor

Shimon, L. J. W., Rabinkov, A., Shin, I., Miron, T., Mirelman, D., Wilchek, M., & Frolow, F. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.041 · Cited by 69

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Ilari, A., Alaleona, F., Tria, G., Petrarca, P., Battistoni, A., Zamparelli, C., Verzili, D., Falconi, M., & Chiancone, E. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.010 · Cited by 55

Insights into the Phosphoregulation of β‐Secretase Sorting Signal by the VHS Domain of GGA1

Shiba, T., Kametaka, S., Kawasaki, M., Shibata, M., Waguri, S., Uchiyama, Y., & Wakatsuki, S. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.00188.x · Cited by 56

High-Resolution Crystal Structure of the Subclass B3 Metallo-β-Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with Sulfonamides

Docquier, J.-D., Benvenuti, M., Calderone, V., Stoczko, M., Menciassi, N., Rossolini, G. M., & Mangani, S. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00409-10 · Cited by 51

Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state

Matsumoto, T., Kinoshita, T., Kirii, Y., Yokota, K., Hamada, K., & Tada, T. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.071 · Cited by 49

Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins

(2022) · doi:10.1038/s41467-022-31564-1 · Cited by 45

Crystal Structures and RNA-binding Properties of the RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein L

Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40

Structure-Based Discovery of M-89 as a Highly Potent Inhibitor of the Menin-Mixed Lineage Leukemia (Menin-MLL) Protein–Protein Interaction

Aguilar, A., Zheng, K., Xu, T., Xu, S., Huang, L., Fernandez-Salas, E., Liu, L., Bernard, D., Harvey, K. P., Foster, C., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00021 · Cited by 39

The ultra-high affinity transport proteins of ubiquitous marine bacteria

Clifton, B. E., Alcolombri, U., Uechi, G.-I., Jackson, C. J., & Laurino, P. (2024) · Nature · doi:10.1038/s41586-024-07924-w · Cited by 37

Affinity maturation, humanization, and co-crystallization of a rabbit anti-human ROR2 monoclonal antibody for therapeutic applications

Goydel, R. S., Weber, J., Peng, H., Qi, J., Soden, J., Freeth, J., Park, H., & Rader, C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012791 · Cited by 34

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Wong, C. T., Xu, Y., Gupta, A., Garnett, J. A., Matthews, S. J., & Hare, S. A. (2015) · Nature Communications · doi:10.1038/ncomms10172 · Cited by 30

Comparative Structural and Thermal Stability Studies of Cuc m 2.0101, Art v 4.0101 and Other Allergenic Profilins

Kapingidza, A. B., Pye, S. E., Hyduke, N., Dolamore, C., Pote, S., Schlachter, C. R., Commins, S. P., Kowal, K., & Chruszcz, M. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.07.004 · Cited by 30

De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Tetreau, G., Sawaya, M. R., De Zitter, E., Andreeva, E. A., Banneville, A.-S., Schibrowsky, N. A., Coquelle, N., Brewster, A. S., Grünbein, M. L., Kovacs, G. N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31746-x · Cited by 28

Crystal structure of the dog allergen Can f 6 and structure-based implications of its cross-reactivity with the cat allergen Fel d 4

Yamamoto, K., Ishibashi, O., Sugiura, K., Ubatani, M., Sakaguchi, M., Nakatsuji, M., Shimamoto, S., Noda, M., Uchiyama, S., Fukutomi, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-38134-w · Cited by 27

Structure and function of Aspergillus niger laccase McoG

Ferraroni, M., Westphal, A. H., Borsari, M., Tamayo-Ramos, J. A., Briganti, F., Graaff, L. H. D., & Berkel, W. J. H. V. (2017) · Biocatalysis · doi:10.1515/boca-2017-0001 · Cited by 26

Discovery of archaeal Fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins

Moi, D., Nishio, S., Li, X., Valansi, C., Langleib, M., Brukman, N. G., Flyak, K., Dessimoz, C., de Sanctis, D., Tunyasuvunakool, K., et al. (2021) · doi:10.1101/2021.10.13.464100 · Cited by 23

Mechanistic insights explain the transforming potential of the T507K substitution in the protein-tyrosine phosphatase SHP2

Zhang, R.-Y., Yu, Z.-H., Chen, L., Walls, C. D., Zhang, S., Wu, L., & Zhang, Z.-Y. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010274 · Cited by 22

DNA-binding mechanism and evolution of replication protein A

(2023) · doi:10.1038/s41467-023-38048-w · Cited by 22

AlphaFold Protein Structure Database for Sequence-Independent Molecular Replacement

Chai, L., Zhu, P., Chai, J., Pang, C., Andi, B., McSweeney, S., Shanklin, J., & Liu, Q. (2021) · Crystals · doi:10.3390/cryst11101227 · Cited by 15

Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4

Matsumoto, T., Kinoshita, T., Kirii, Y., Tada, T., & Yamano, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.066 · Cited by 15

DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces

(2024) · doi:10.1093/nar/gkae452 · Cited by 12

Structural aspects of fungal allergens

Crameri, R. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-014-0458-0 · Cited by 10

Designing novel solenoid proteins with in silico evolution

(2025) · doi:10.1038/s42004-025-01817-3 · Cited by 10

DNA Wrapping by a tetrameric bacterial histone

(2025) · doi:10.1038/s41467-025-67425-w · Cited by 7

Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus

Burmeister, W. P., Boutin, L., Balestra, A. C., Gröger, H., Ballandras-Colas, A., Hutin, S., Kraft, C., Grimm, C., Böttcher, B., Fischer, U., et al. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011652 · Cited by 3

Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding

Bimai, O., Banerjee, I., Rozman Grinberg, I., Huang, P., Hultgren, L., Ekström, S., Lundin, D., Sjöberg, B.-M., & Logan, D. T. (2024) · eLife · doi:10.7554/elife.89292 · Cited by 3

Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding

(2024) · doi:10.7554/elife.89292.4 · Cited by 1

Activity modulation in anaerobic ribonucleotide reductases: nucleotide binding to the ATP-cone allosterically mediates substrate binding to the active site

Bimaï, O., Banerjee, I., Grinberg, I. R., Huang, P., Hultgren, L., Ekström, S., Lundin, D., Sjöberg, B.-M., & Logan, D. T. (2023) · doi:10.1101/2023.06.20.545753 · Cited by 1