Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Phaser crystallographic software

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Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix

Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637

Towards automated crystallographic structure refinement with phenix.refine

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The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327

HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information

Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417

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

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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

Structure of the 30S ribosomal subunit

Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035

Structural Basis of the Drug-binding Specificity of Human Serum Albumin

Ghuman, J., Zunszain, P. A., Petitpas, I., Bhattacharya, A. A., Otagiri, M., & Curry, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.075 · Cited by 1,941

Crystal structure of the ribosome at 5.5 Å resolution

Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688

Structural mechanism for statin inhibition of HMG-CoA reductase

Istvan, E. S., & Deisenhofer, J. (2001) · Science · doi:10.1126/science.1059344 · Cited by 1,644

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

Carter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

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

The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition

Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355

Crystal Structure of a Ternary FGF-FGFR-Heparin Complex Reveals a Dual Role for Heparin in FGFR Binding and Dimerization

Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · Cited by 1,199

Structure of TPR Domain–Peptide Complexes

Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188

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

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution

Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184

Structural basis of water-specific transport through the AQP1 water channel

Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166

Recognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit

Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162

Protein 3D Structure Computed from Evolutionary Sequence Variation

Marks, D. S., Colwell, L. J., Sheridan, R., Hopf, T. A., Pagnani, A., Zecchina, R., & Sander, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028766 · Cited by 1,144

Helical Assembly in the MyD88-IRAK4-IRAK2 Complex in TLR/IL-1R Signalling

Lin, S.-C., Lo, Y.-C., & Wu, H. (2010) · Nature · doi:10.1038/nature09121 · Cited by 1,111

Crystal structure of opsin in its G-protein-interacting conformation

Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059

The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure

Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049

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

Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979

Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

Bruner, S. D., Norman, D. P. G., & Verdine, G. L. (2000) · Nature · doi:10.1038/35002510 · Cited by 972

The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit

Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951

Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model

Wang, S., Sun, S., Li, Z., Zhang, R., & Xu, J. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005324 · Cited by 931

Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II

Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881

Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands

Kitov, P. I., Sadowska, J. M., Mulvey, G., Armstrong, G. D., Ling, H., Pannu, N. S., Read, R. J., & Bundle, D. R. (2000) · Nature · doi:10.1038/35001095 · Cited by 869

Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand

Rochel, N., Wurtz, J. M., Mitschler, A., Klaholz, B., & Moras, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80413-x · Cited by 842

Structure of a c-Cbl–UbcH7 Complex

Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839

Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition

Bledsoe, R. K., Montana, V. G., Stanley, T. B., Delves, C. J., Apolito, C. J., McKee, D. D., Consler, T. G., Parks, D. J., Stewart, E. L., Willson, T. M., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00817-6 · Cited by 818

Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

McLellan, J. S., Pancera, M., Carrico, C., Gorman, J., Julien, J.-P., Khayat, R., Louder, R., Pejchal, R., Sastry, M., Dai, K., et al. (2011) · Nature · doi:10.1038/nature10696 · Cited by 830

The structural basis of the activation of Ras by Sos

Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., & Kuriyan, J. (1998) · Nature · doi:10.1038/28548 · Cited by 799

Advances in protein structure prediction and design

Kuhlman, B., & Bradley, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0163-x · Cited by 806

Designing a 20-residue protein

Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Zhou, T., Xu, L., Dey, B., Hessell, A. J., Van Ryk, D., Xiang, S.-H., Yang, X., Zhang, M.-Y., Zwick, M. B., Arthos, J., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751

Energetic optimization of ion conduction rate by the K+ selectivity filter

Morais-Cabral, J. H., Zhou, Y., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102000 · Cited by 761

Accurate assessment of mass, models and resolution by small-angle scattering

Rambo, R. P., & Tainer, J. A. (2013) · Nature · doi:10.1038/nature12070 · Cited by 750

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735

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

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733

Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710

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

Mammalian Microsomal Cytochrome P450 Monooxygenase

Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696

Protein structure prediction from sequence variation

Marks, D. S., Hopf, T. A., & Sander, C. (2012) · Nature Biotechnology · doi:10.1038/nbt.2419 · Cited by 622

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

Crystal structure of metarhodopsin II

Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663

Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form

Ogle, J. M., Murphy, F. V., Tarry, M. J., & Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)01086-3 · Cited by 663

The unfolded protein response signals through high-order assembly of Ire1

Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., Stroud, R. M., & Walter, P. (2009) · Nature · doi:10.1038/nature07661 · Cited by 656

High-affinity binders selected from designed ankyrin repeat protein libraries

Binz, H. K., Amstutz, P., Kohl, A., Stumpp, M. T., Briand, C., Forrer, P., Grütter, M. G., & Plückthun, A. (2004) · Nature Biotechnology · doi:10.1038/nbt962 · Cited by 656

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

Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis

Nowotny, M., Gaidamakov, S. A., Crouch, R. J., & Yang, W. (2005) · Cell · doi:10.1016/j.cell.2005.04.024 · Cited by 620

Crystal Structure of a Y-Family DNA Polymerase in Action

Ling, H., Boudsocq, F., Woodgate, R., & Yang, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00515-3 · Cited by 610

Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER

Smart, O. S., Womack, T. O., Flensburg, C., Keller, P., Paciorek, W., Sharff, A., Vonrhein, C., & Bricogne, G. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911056058 · Cited by 612

The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy

Xie, Q., Bu, W., Bhatia, S., Hare, J., Somasundaram, T., Azzi, A., & Chapman, M. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162250899 · Cited by 612

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612

Crystal structure of the outer membrane active transporter FepA from Escherichia coli.

Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591

Structural basis for AMP binding to mammalian AMP-activated protein kinase

Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., Walker, P. A., Haire, L., Eccleston, J. F., Davis, C. T., et al. (2007) · Nature · doi:10.1038/nature06161 · Cited by 591

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

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

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

X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA

Nair, S. K., & Burley, S. K. (2003) · Cell · doi:10.1016/s0092-8674(02)01284-9 · Cited by 551

Transmembrane Signaling across the Ligand-Gated FhuA Receptor

Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., & Moras, D. (1998) · Cell · doi:10.1016/s0092-8674(00)81700-6 · Cited by 540

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

Structure and lipid transport mechanism of a StAR-related domain

Tsujishita (2000) · Nature Structural Biology · doi:10.1038/75192 · Cited by 535

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1829 · Cited by 527

Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements

Korostelev, A., Trakhanov, S., Laurberg, M., & Noller, H. F. (2006) · Cell · doi:10.1016/j.cell.2006.08.032 · Cited by 498

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

Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone

Sack, J. S., Kish, K. F., Wang, C., Attar, R. M., Kiefer, S. E., An, Y., Wu, G. Y., Scheffler, J. E., Salvati, M. E., Krystek, S. R., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081565498 · Cited by 491

Anticancer Chemosensitization and Radiosensitization by the Novel Poly(ADP-ribose) Polymerase-1 Inhibitor AG14361

Calabrese, C. R., Almassy, R., Barton, S., Batey, M. A., Calvert, A. H., Canan-Koch, S., Durkacz, B. W., Hostomsky, Z., Kumpf, R. A., Kyle, S., et al. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh005 · Cited by 487

Cooperative binding of two acetylation marks on a histone tail by a single bromodomain

Morinière, J., Rousseaux, S., Steuerwald, U., Soler-López, M., Curtet, S., Vitte, A.-L., Govin, J., Gaucher, J., Sadoul, K., Hart, D. J., et al. (2009) · Nature · doi:10.1038/nature08397 · Cited by 469

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 the Protein Phosphatase 2A Holoenzyme

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

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