[20] Processing of X-ray diffraction data collected in oscillation mode

An empirical method for correcting diffractometer data for absorption effects

Walker, N. P. C., & Stuart, D. I. (1983) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767383000252 · Cited by 5,944 · see citing works

Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector

Kabsch, W. (1988) · Journal of Applied Crystallography · doi:10.1107/s0021889888007903 · Cited by 1,509 · see citing works

Automatic indexing of rotation diffraction patterns

Kabsch, W. (1988) · Journal of Applied Crystallography · doi:10.1107/s0021889887009737 · Cited by 566 · see citing works

The use of an imaging proportional counter in macromolecular crystallography

Howard, A. J., Gilliland, G. L., Finzel, B. C., Poulos, T. L., Ohlendorf, D. H., & Salemme, F. R. (1987) · Journal of Applied Crystallography · doi:10.1107/s0021889887086436 · Cited by 475 · see citing works

Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography

Messerschmidt, A., & Pflugrath, J. W. (1987) · Journal of Applied Crystallography · doi:10.1107/s002188988708662x · Cited by 392 · see citing works

[28] Software for a diffractometer with multiwire area detector

Howard, A. J., Nielsen, C., & Xuong, N. H. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)14030-9 · Cited by 259 · see citing works

X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation

Sakabe, N. (1991) · Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment · doi:10.1016/0168-9002(91)90282-u · Cited by 229 · see citing works

Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting

Rossmann, M. G. (1979) · Journal of Applied Crystallography · doi:10.1107/s0021889879012218 · Cited by 228 · see citing works

Processing and post-refinement of oscillation camera data

Rossmann, M. G., Leslie, A. G. W., Abdel‐Meguid, S., et al. (1979) · Journal of Applied Crystallography · doi:10.1107/s0021889879013273 · Cited by 142 · see citing works

A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector

Blum, M., Metcalf, P., Harrison, S. C., et al. (1987) · Journal of Applied Crystallography · doi:10.1107/s0021889887086783 · Cited by 128 · see citing works

An alternative method of solving the layer scaling equations of Hamilton, Rollett and Sparks

Fox, G. C., & Holmes, K. C. (1966) · Acta Crystallographica · doi:10.1107/s0365110x66002007 · Cited by 107 · see citing works

An analytical function for absorption correction

Katayama, C. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099968 · Cited by 101 · see citing works

Auto-indexing of oscillation images

Higashi, T. (1990) · Journal of Applied Crystallography · doi:10.1107/s0021889890002461 · Cited by 79 · see citing works

Statistical descriptors in crystallography: Report of the IUCr Subcommittee on Statistical Descriptors

Schwarzenbach, D., Abrahams, S. C., Flack, H. D., et al. (1989) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767388009596 · Cited by 75 · see citing works

Refinement of setting angles in screenless film methods

Schwager, P., Bartels, K. S., & Jones, A. (1975) · Journal of Applied Crystallography · doi:10.1107/s002188987501045x · Cited by 72 · see citing works

Synchrotron radiation and biophysics

Hasnain, S. S. (1990) · Cited by 56 · see citing works

Synchrotron Radiation and Biophysics

Kobayashi, K. (1991) · International Journal of Radiation Biology · doi:10.1080/09553009114550961 · Cited by 42 · see citing works

Oscillation photography of radiation-sensitive crystals using a synchrotron source

Rossmann, M. G., & Erickson, J. W. (1983) · Journal of Applied Crystallography · doi:10.1107/s002188988301119x · Cited by 39 · see citing works

Auto-indexing oscillation photographs

Kim, S. (1989) · Journal of Applied Crystallography · doi:10.1107/s0021889888010878 · Cited by 30 · see citing works

Determination of three-dimensional structure by multiwavelength anomalous diffraction

Smith, J. L. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90098-e · Cited by 29 · see citing works

Intensity determination by profile-fitting applied to precession photographs

Ford, G. C. (1974) · Journal of Applied Crystallography · doi:10.1107/s0021889874010430 · Cited by 26 · see citing works

An empirical method for correcting rotation-camera data for absorption and decay effects

Stuart, D. I., & Walker, N. (1979) · Acta Crystallographica Section A · doi:10.1107/s0567739479002072 · Cited by 15 · see citing works

Determination of the orientation of a randomly placed crystal from a single oscillation photograph

Vriend, G., & Rossmann, M. G. (1987) · Journal of Applied Crystallography · doi:10.1107/s0021889887086515 · Cited by 12 · see citing works

Relative absorption correction for rotation film data

Schutt, C. E., & Evans, P. R. (1985) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767385001234 · Cited by 5 · see citing works

A simple method of absorption and decay correction in intensities measured by area-detector X-ray diffractometer

Takusagawa, F. (1987) · Journal of Applied Crystallography · doi:10.1107/s0021889887086771 · Cited by 2 · see citing works

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 · see citing works

Towards automated crystallographic structure refinement with <i>phenix.refine</i>

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

Cancer-associated IDH1 mutations produce 2-hydroxyglutarate

Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154 · see citing works

Structural basis of receptor recognition by SARS-CoV-2

Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works

Molecular basis of agonism and antagonism in the oestrogen receptor

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

Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892 · see citing works

Crystal structure of the β2 adrenergic receptor–Gs protein complex

Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009 · see citing works

Pore-forming activity and structural autoinhibition of the gasdermin family

Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works

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 · see citing works

Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247 · see citing works

Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma

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

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 · see citing works

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 · see citing works

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 · see citing works

Recognition of Cognate Transfer RNA by the 30 <i>S</i> 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 · see citing works

Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus

McLellan, J. S., Chen, M., Joyce, M. G., Sastry, M., Stewart-Jones, G. B. E., Yang, Y., Zhang, B., Chen, L., Srivatsan, S., Zheng, A., et al. (2013) · Science · doi:10.1126/science.1243283 · Cited by 1,126 · see citing works

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 · see citing works

Cyclic [G(2′,5′)pA(3′,5′)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase.

Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.046 · Cited by 1,101 · see citing works

mTOR kinase structure, mechanism and regulation

Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., & Pavletich, N. P. (2013) · Nature · doi:10.1038/nature12122 · Cited by 1,075 · see citing works

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 · see citing works

Latent TGF-β structure and activation

Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody

McLellan, J. S., Chen, M., Leung, S., Graepel, K. W., Du, X., Yang, Y., Zhou, T., Baxa, U., Yasuda, E., Beaumont, T., et al. (2013) · Science · doi:10.1126/science.1234914 · Cited by 883 · see citing works

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 · see citing works

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 · see citing works

Targeted inhibition of mutant IDH2 in leukemia cells induces cellular differentiation

Wang, F., Travins, J., DeLaBarre, B., Penard-Lacronique, V., Schalm, S., Hansen, E., Straley, K., Kernytsky, A., Liu, W., Gliser, C., et al. (2013) · Science · doi:10.1126/science.1234769 · Cited by 804 · see citing works

Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis

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

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 · see citing works

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 · see citing works

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 · see citing works

Crystal structure of the human glucose transporter GLUT1

Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., & Yan, N. (2014) · Nature · doi:10.1038/nature13306 · Cited by 777 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

Pejchal, R., Doores, K. J., Walker, L. M., Khayat, R., Huang, P.-S., Wang, S.-K., Stanfield, R. L., Julien, J.-P., Ramos, A., Crispin, M., et al. (2011) · Science · doi:10.1126/science.1213256 · Cited by 694 · see citing works

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 · see citing works

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 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works

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 · see citing works

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 · see citing works

A Potent and Selective Small-Molecule Degrader of STAT3 Achieves Complete Tumor Regression In Vivo

Bai, L., Zhou, H., Xu, R., Zhao, Y., Chinnaswamy, K., McEachern, D., Chen, J., Yang, C.-Y., Liu, Z., Wang, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.10.002 · Cited by 652 · see citing works

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 · see citing works

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 · see citing works

Design of protein-binding proteins from the target structure alone

Cao, L., Coventry, B., Goreshnik, I., Huang, B., Sheffler, W., Park, J. S., Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., et al. (2022) · Nature · doi:10.1038/s41586-022-04654-9 · Cited by 577 · see citing works

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 · see citing works

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 · see citing works

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

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

Non-Homeostatic Body Weight Regulation Through a Brainstem-Restricted Receptor for GDF15

Hsu, J.-Y., Crawley, S., Chen, M., Ayupova, D. A., Lindhout, D. A., Higbee, J., Kutach, A., Joo, W., Gao, Z., Fu, D., et al. (2017) · Nature · doi:10.1038/nature24042 · Cited by 616 · see citing works

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

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

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

Czabotar, P. E., Westphal, D., Dewson, G., Ma, S., Hockings, C., Fairlie, W. D., Lee, E. F., Yao, S., Robin, A. Y., Smith, B. J., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.031 · Cited by 573 · see citing works

IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding

Hymowitz, S. G., Filvaroff, E. H., Yin, J., Lee, J., Cai, L., Risser, P., Maruoka, M., Mao, W., Foster, J., Kelley, R. F., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.19.5332 · Cited by 548 · see citing works

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

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

Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40

Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548 · see citing works

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 · see citing works

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 · see citing works

Complementation of mitochondrial electron transport chain by manipulation of the NAD ⁺ /NADH ratio

Titov, D. V., Cracan, V., Goodman, R. P., Peng, J., Grabarek, Z., & Mootha, V. K. (2016) · Science · doi:10.1126/science.aad4017 · Cited by 518 · see citing works

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 · see citing works

Structure of the human Cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs

Chamberlain, P. P., Lopez-Girona, A., Miller, K., Carmel, G., Pagarigan, B., Chie-Leon, B., Rychak, E., Corral, L. G., Ren, Y. J., Wang, M., et al. (2014) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.2874 · Cited by 531 · see citing works

Histone deacetylase 6 structure and molecular basis of catalysis and inhibition

Hai, Y., & Christianson, D. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2134 · Cited by 521 · see citing works

Structure of a cytochrome P450-redox partner electron-transfer complex

Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501 · see citing works

Massively parallel de novo protein design for targeted therapeutics

Chevalier, A., Silva, D.-A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K.-H., Yao, G., et al. (2017) · Nature · doi:10.1038/nature23912 · Cited by 453 · see citing works

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 · see citing works

AG-221, a First-in-Class Therapy Targeting Acute Myeloid Leukemia Harboring Oncogenic <i>IDH2</i> 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 · see citing works

Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459 · see citing works

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway

Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457 · see citing works

Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450 · see citing works

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 · see citing works

Structure of a complex of the ATPase SecA and the protein-translocation channel.

Zimmer, J., Nam, Y., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07335 · Cited by 459 · see citing works

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

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

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Groves, M. R., Hanlon, N., Turowski, P., Hemmings, B. A., & Barford, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80963-0 · Cited by 442 · see citing works

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 · see citing works

An Extremely Potent Inhibitor of Xanthine Oxidoreductase

Okamoto, K., Eger, B. T., Nishino, T., Kondo, S., Pai, E. F., & Nishino, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208307200 · Cited by 434 · see citing works

Structural Basis of DNA Recognition by p53 Tetramers

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

Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin

Drum, C. L., Yan, S.-Z., Bard, J., Shen, Y.-Q., Lu, D., Soelaiman, S., Grabarek, Z., Bohm, A., & Tang, W.-J. (2002) · Nature · doi:10.1038/415396a · Cited by 413 · see citing works

The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer

Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418 · see citing works

Structural basis of androgen receptor binding to selective androgen response elements

Shaffer, P. L., Jivan, A., Dollins, D. E., Claessens, F., & Gewirth, D. T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401123101 · Cited by 400 · see citing works

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

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

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding

Chen, J. C.-H., Krucinski, J., Miercke, L. J. W., Finer-Moore, J. S., Tang, A. H., Leavitt, A. D., & Stroud, R. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150220297 · Cited by 404 · see citing works

Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α11Edited by K. Nagai

Fontes, M. R. M., Teh, T., & Kobe, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3642 · Cited by 398 · see citing works

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

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

De novo design of a fluorescence-activating β-barrel

Dou, J., Vorobieva, A. A., Sheffler, W., Doyle, L. A., Park, H., Bick, M. J., Mao, B., Foight, G. W., Lee, M. Y., Gagnon, L. A., et al. (2018) · Nature · doi:10.1038/s41586-018-0509-0 · Cited by 351 · see citing works

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

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

Crystal Structure of the CSL-Notch-Mastermind Ternary Complex Bound to DNA

Wilson, J. J., & Kovall, R. A. (2006) · Cell · doi:10.1016/j.cell.2006.01.035 · Cited by 371 · see citing works

Structural basis of gating by the outer membrane transporter FecA

Ferguson, A. D., Chakraborty, R., Smith, B. S., Esser, L., van der Helm, D., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1067313 · Cited by 373 · see citing works

XPD Helicase Structures and Activities: Insights into the Cancer and Aging Phenotypes from XPD Mutations

Fan, L., Fuss, J. O., Cheng, Q. J., Arvai, A. S., Hammel, M., Roberts, V. A., Cooper, P. K., & Tainer, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.04.030 · Cited by 369 · see citing works

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 · see citing works

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 · see citing works

A Therapeutic Non-self-reactive SARS-CoV-2 Antibody Protects from Lung Pathology in a COVID-19 Hamster Model

Kreye, J., Reincke, S. M., Kornau, H.-C., Sánchez-Sendin, E., Corman, V. M., Liu, H., Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.049 · Cited by 347 · see citing works

CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator

Liu, T., Ramesh, A., Ma, Z., Ward, S. K., Zhang, L., George, G. N., Talaat, A. M., Sacchettini, J. C., & Giedroc, D. P. (2007) · Nature Chemical Biology · doi:10.1038/nchembio844 · Cited by 338 · see citing works

Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.09.025 · Cited by 334 · see citing works

Discussion on the Application of Visualization Technology in Modeling and Simulation

Na, Y., Shu, Y., Chang, L., et al. (2011) · International Conference on Information Management, Innovation Management and Industrial Engineering (ICIII) · doi:10.1109/iciii.2011.336 · Cited by 5 · see citing works

Visualization and New Product Evaluation: The Role of Memory- and Imagination-Focused VisualizationPreprint

Zhao, M., Hoeffler, S., & Dahl, D. W. (2006) · SSRN Electronic Journal · doi:10.2139/ssrn.935048 · Cited by 1 · see citing works

Views on Visualization

van Wijk, J. J. (2006) · IEEE Transactions on Visualization and Computer Graphics · doi:10.1109/tvcg.2006.80 · Cited by 125 · see citing works

Selecting Visualization Web Services Based on Visualization Characteristics

Gao, S., Xin, F., & Yu, J. (2013) · doi:10.1109/iccis.2013.33

HENSON: a visualization framework for genetic algorithm users

Collins, T. (2003) · doi:10.1109/cec.1999.781983 · Cited by 5 · see citing works