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SARS-CoV-2 identified through crystallographic screening and computational docking

Science Advances 2021年第16期7卷

作者： Schuller, Marion Correy, Galen J. Gahbauer, Stefan Fearon, Daren Wu, Taiasean Díaz, Roberto Efraín Young, Iris D. Martins, Luan Carvalho Smith, Dominique H. Schulze-Gahmen, Ursula Owens, Tristan W. Deshpande, Ishan Merz, Gregory E. Thwin, Aye C. Biel, Justin T. Peters, Jessica K. Moritz, Michelle Herrera, Nadia Kratochvil, Huong T. Aimon, Anthony Bennett, James M. Neto, Jose Brandao Cohen, Aina E. Dias, Alexandre Douangamath, Alice Dunnett, Louise Fedorov, Oleg Ferla, Matteo P. Fuchs, Martin R. Gorrie-Stone, Tyler J. Holton, James M. Johnson, Michael G. Krojer, Tobias Meigs, George Powell, Ailsa J. Rack, Johannes Gregor Matthias Rangel, Victor L. Russi, Silvia Skyner, Rachael E. Smith, Clyde A. Soares, Alexei S. Wierman, Jennifer L. Zhu, Kang O Brien, Peter Jura, Natalia Ashworth, Alan Irwin, John J. Thompson, Michael C. Gestwicki, Jason E. Von Delft, Frank Shoichet, Brian K. Fraser, James S. Ahel, Ivan Sir William Dunn School of Pathology University of Oxford South Parks Road OxfordOX1 3RE United Kingdom Department of Bioengineering and Therapeutic Sciences University of California San Francisco San FranciscoCA94158 United States Department of Pharmaceutical Chemistry University of California San Francisco San FranciscoCA94158 United States Diamond Light Source Ltd. Harwell Science and Innovation Campus DidcotOX11 0DE United Kingdom Institute for Neurodegenerative Disease University of California San Francisco San FranciscoCA94158 United States Chemistry and Chemical Biology Graduate Program University of California San Francisco San FranciscoCA94158 United States Tetrad Graduate Program University of California San Francisco San FranciscoCA94158 United States Coronavirus Research Group Structural Biology Consortium University of California San Francisco San FranciscoCA94158 United States Biochemistry Department Institute for Biological Sciences Federal University of Minas Gerais Belo Horizonte Brazil Helen Diller Family Comprehensive Cancer University of California San Francisco San FranciscoCA94158 United States Centre for Medicines Discovery University of Oxford South Parks Road HeadingtonOX3 7DQ United Kingdom Stanford Synchrotron Radiation Lightsource Slac National Accelerator Center Menlo ParkCA94025 United States Wellcome Centre for Human Genetics University of Oxford Old Road Campus OxfordOX3 7BN United Kingdom National Synchrotron Light Source Ii Brookhaven National Laboratory UptonNY11973 United States Department of Biochemistry and Biophysics University of California San Francisco San FranciscoCA94158 United States Department of Molecular Biophysics and Integrated Bioimaging Lawrence Berkeley National Laboratory BerkeleyCA94720 United States ChemPartner Corporation South San FranciscoCA94080 United States Structural Genomics Consortium University of Oxford Old Road Campus HeadingtonOX3 7DQ United Kingdom School of

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here, we report a massive crystallographic screening and computational docking effort, identifying new chemical matter primarily targeting the active site of the macrodomain. Crystallographic screening of 2533 diverse fragments resulted in 214 unique macrodomain-binders. An additional 60 molecules were selected from docking more than 20 million fragments, of which 20 were crystallographically confirmed. X-ray data collection to ultra-high resolution and at physiological temperature enabled assessment of the conformational heterogeneity around the active site. Several fragment hits were confirmed by solution binding using three biophysical techniques (differential scanning fluorimetry, homogeneous time-resolved fluorescence, and isothermal titration calorimetry). The 234 fragment structures explore a wide range of chemotypes and provide starting points for development of potent SARS-CoV-2 macrodomain inhibitors. © 2021 American Association for the Advancement of Science. All rights reserved.

关键词： Coronavirus

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TET proteins safeguard bivalent promoters from de novo methylation in human embryonic stem cells (vol 50, pg 83, 2017)

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NATURE GENETICS 2018年第5期50卷 764-764页

作者： Verma, Nipun Pan, Heng Dore, Louis C. Shukla, Abhijit Li, Qing V. Pelham-Webb, Bobbie Teijeiro, Virginia Gonzalez, Federico Krivtsov, Andrei Chang, Chan-Jung Papapetrou, Eirini P. He, Chuan Elemento, Olivier Huangfu, Danwei Developmental Biology Program Sloan Kettering Institute New York NY USA Weill Graduate School of Medical Sciences at Cornell University/The Rockefeller University/Sloan Kettering Institute Tri-Institutional MD-PhD Program New York NY USA Department of Physiology and Biophysics Englander Institute for Precision Medicine Institute for Computational Biomedicine Weill Cornell Medical College New York NY USA Weill Cornell Graduate School of Medical Sciences Weill Cornell Medical College New York NY USA Department of Chemistry Department of Biochemistry and Molecular Biology Institute for Biophysical Dynamics Howard Hughes Medical Institute University of Chicago Chicago IL USA Louis V. Gerstner Jr. Graduate School of Biomedical Sciences Memorial Sloan Kettering Cancer Center New York NY USA Cancer Biology and Genetics Program Sloan Kettering Institute New York NY USA Department of Oncological Sciences and Black Family Stem Cell Institute Icahn School of Medicine at Mount Sinai New York NY USA

TET enzymes oxidize 5-methylcytosine (5mC) to 5-hydroxymethylcytosine (5hmC), which can lead to DNA demethylation. However, direct connections between TET-mediated DNA demethylation and transcriptional output are difficult to establish owing to challenges in distinguishing global versus locus-specific effects. Here we show that TET1, TET2 and TET3 triple-knockout (TKO) human embryonic stem cells (hESCs) exhibit prominent bivalent promoter hypermethylation without an overall corresponding decrease in gene expression in the undifferentiated state. Focusing on the bivalent PAX6 locus, we find that increased DNMT3B binding is associated with promoter hypermethylation, which precipitates a neural differentiation defect and failure of PAX6 induction during differentiation. dCas9-mediated locus-specific demethylation and global inactivation of DNMT3B in TKO hESCs partially reverses the hypermethylation at the PAX6 promoter and improves differentiation to neuroectoderm. Taking these findings together with further genome-wide methylation and TET1 and DNMT3B ChIP-seq analyses, we conclude that TET proteins safeguard bivalent promoters from de novo methylation to ensure robust lineage-specific transcription upon differentiation.

关键词： Epigenetics Stem cells

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Genomic basis for RNA alterations in cancer (vol 578, pg 129, 2020)

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NATURE 2023年第7948期614卷 E37-E37页

作者： Calabrese, Claudia Davidson, Natalie R. Demircioglu, Deniz Fonseca, Nuno A. He, Yao Lehmann, Kjong-Van Liu, Fenglin Shiraishi, Yuichi Soulette, Cameron M. Urban, Lara Greger, Liliana Li, Siliang Liu, Dongbing Perry, Marc D. Xiang, Qian Zhang, Fan Zhang, Junjun Bailey, Peter Erkek, Serap Hoadley, Katherine A. Hou, Yong Huska, Matthew R. Kilpinen, Helena Korbel, Jan O. Marin, Maximillian G. Markowski, Julia Nandi, Tannistha Pan-Hammarstrom, Qiang Pedamallu, Chandra Sekhar Siebert, Reiner Stark, Stefan G. Su, Hong Tan, Patrick Waszak, Sebastian M. Yung, Christina Zhu, Shida Awadalla, Philip Creighton, Chad J. Meyerson, Matthew Ouellette, B. F. Francis Wu, Kui Yang, Huanming Brazma, Alvis Brooks, Angela N. Goke, Jonathan Ratsch, Gunnar Schwarz, Roland F. Stegle, Oliver Zhang, Zemin European Molecular Biology Laboratory European Bioinformatics Institute Hinxton UK European Molecular Biology Laboratory European Bioinformatics Institute (EMBL-EBI) Cambridge UK Genome Biology Unit European Molecular Biology Laboratory (EMBL) Heidelberg Germany CIBIO/InBIO - Research Center in Biodiversity and Genetic Resources Universidade do Porto Vairão Portugal Berlin Institute for Medical Systems Biology Max Delbruck Center for Molecular Medicine Berlin Germany German Cancer Consortium (DKTK) partner site Berlin Germany German Cancer Research Center (DKFZ) Heidelberg Germany Berlin Institute for Medical Systems Biology Max Delbrück Center for Molecular Medicine Berlin Germany German Cancer Consortium (DKTK) Partner site Berlin Berlin Germany European Molecular Biology Laboratory Genome Biology Unit Heidelberg Germany Division of Computational Genomics and Systems Genetics German Cancer Research Center (DKFZ) Heidelberg Germany ETH Zurich Zurich Switzerland Memorial Sloan Kettering Cancer Center New York NY USA Weill Cornell Medical College New York NY USA SIB Swiss Institute of Bioinformatics Lausanne Switzerland University Hospital Zurich Zurich Switzerland Computational Biology Center Memorial Sloan Kettering Cancer Center New York NY USA Department of Biology ETH Zurich Zürich Switzerland Department of Computer Science ETH Zurich Zurich Switzerland Korea University Seoul South Korea Computational and Systems Biology Program Memorial Sloan Kettering Cancer Center New York NY USA Department of Physiology and Biophysics Weill Cornell Medicine New York NY USA Institute for Computational Biomedicine Weill Cornell Medicine New York NY USA Controlled Department and Institution New York NY USA Englander Institute for Precision Medicine Weill Cornell Medicine New York NY USA National University of Singapore Singapore Singapore Genome Institute of Singapore Singapore Singapore Computational and Systems Biology Genome Institute of Singap

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Guidelines and definitions for research on epithelial-mesenchymal transition (vol 21, pg 341, 2020)

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NATURE REVIEWS molecular CELL biology 2021年第12期22卷 834-834页

作者： Yang, Jing Antin, Parker Berx, Geert Blanpain, Cedric Brabletz, Thomas Bronner, Marianne Campbell, Kyra Cano, Amparo Casanova, Jordi Christofori, Gerhard Dedhar, Shoukat Derynck, Rik Ford, Heide L. Fuxe, Jonas Garcia de Herreros, Antonio Goodall, Gregory J. Hadjantonakis, Anna-Katerina Huang, Ruby Y. J. Kalcheim, Chaya Kalluri, Raghu Kang, Yibin Khew-Goodall, Yeesim Levine, Herbert Liu, Jinsong Longmore, Gregory D. Mani, Sendurai A. Massague, Joan Mayor, Roberto McClay, David Mostov, Keith E. Newgreen, Donald F. Nieto, M. Angela Puisieux, Alain Runyan, Raymond Savagner, Pierre Stanger, Ben Stemmler, Marc P. Takahashi, Yoshiko Takeichi, Masatoshi Theveneau, Eric Thiery, Jean Paul Thompson, Erik W. Weinberg, Robert A. Williams, Elizabeth D. Xing, Jianhua Zhou, Binhua P. Sheng, Guojun Departments of Pharmacology and Pediatrics Moores Cancer Center University of California San Diego La Jolla CA USA Department of Cellular and Molecular Medicine University of Arizona Tucson AZ USA Molecular and Cellular Oncology Lab Department of Biomedical Molecular Biology Ghent University Cancer Research Institute Ghent (CRIG) VIB Center for Inflammation Research Ghent Belgium Laboratory of Stem Cells and Cancer Université Libre de Bruxelles Bruxelles Belgium Department of Experimental Medicine 1 Nikolaus-Fiebiger-Center for Molecular Medicine Friedrich-Alexander-University Erlangen-Nürnberg Erlangen Germany Division of Biology and Biological Engineering California Institute of Technology Pasadena CA USA Department of Biomedical Science and Bateson Centre University of Sheffield Sheffield UK Departamento de Bioquímica Universidad Autónoma de Madrid (UAM) Instituto de Investigaciones Biomédicas ‘Alberto Sols’ (CSIC-UAM) IdiPAZ & Centro de Investigación Biomédica en Red de Cáncer (CIBERONC) Madrid Spain Institute for Research in Biomedicine (IRB Barcelona) Barcelona Institute of Science and Technology/Institut de Biologia Molecular de Barcelona (IBMB-CSIC) Barcelona Spain Department of Biomedicine University of Basel Basel Switzerland Department of Biochemistry and Molecular Biology University of British Columbia and British Columbia Cancer Research Centre Vancouver BC Canada Departments of Cell and Tissue Biology and Anatomy University of California at San Francisco San Francisco CA USA Department of Pharmacology University of Colorado Anschutz Medical Campus Aurora CO USA Department of Laboratory Medicine (LABMED) Division of Pathology Karolinska University Hospital and Department of Microbiology Tumor and Cell Biology (MTC) Karolinska Institutet Stockholm Sweden Programa de Recerca en Càncer Institut Hospital del Mar d’Investigacions Mèdiques (IMIM) and Departament de Ciències Experimentals i de la Salut Universitat Pompeu Fabra Barcelona Spain C

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Going Deeper in Cryo Electron Tomography with Neural Networks

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Microscopy and Microanalysis 2017年第S1期23卷 814-815页

作者： Muyuan Chen Wei Dai Stella Y. Sun Michael F. Schmid Wah Chiu Steven J. Ludtke Graduate Program in Structural and Computational Biology and Molecular Biophysics Baylor College of Medicine Houston TX Verna Marrs and McLean Department of Biochemistry and Molecular Biology Baylor College of Medicine Houston TX

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The evolutionary history of 2,658 cancers (vol 578, pg 122, 2020)

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NATURE 2023年第7948期614卷 E42-E42页

作者： Gerstung, Moritz Jolly, Clemency Leshchiner, Ignaty Dentro, Stefan C. Gonzalez, Santiago Rosebrock, Daniel Mitchell, Thomas J. Rubanova, Yulia Anur, Pavana Yu, Kaixian Tarabichi, Maxime Deshwar, Amit Wintersinger, Jeff Kleinheinz, Kortine Vazquez-Garcia, Ignacio Haase, Kerstin Jerman, Lara Sengupta, Subhajit Macintyre, Geoff Malikic, Salem Donmez, Nilgun Livitz, Dimitri G. Cmero, Marek Demeulemeester, Jonas Schumacher, Steven Fan, Yu Yao, Xiaotong Lee, Juhee Schlesner, Matthias Boutros, Paul C. Bowtell, David D. Zhu, Hongtu Getz, Gad Imielinski, Marcin Beroukhim, Rameen Sahinalp, S. Cenk Ji, Yuan Peifer, Martin Markowetz, Florian Mustonen, Ville Yuan, Ke Wang, Wenyi Morris, Quaid D. Spellman, Paul T. Wedge, David C. Van Loo, Peter European Molecular Biology Laboratory European Bioinformatics Institute (EMBL-EBI) Cambridge UK European Molecular Biology Laboratory Genome Biology Unit Heidelberg Germany Wellcome Sanger Institute Cambridge UK Genome Biology Unit European Molecular Biology Laboratory (EMBL) Heidelberg Germany University of Ljubljana Ljubljana Slovenia The Francis Crick Institute London UK Big Data Institute University of Oxford Oxford UK Wellcome Sanger Institute Wellcome Genome Campus Hinxton UK Big Data Institute Li Ka Shing Centre University of Oxford Oxford UK University of Cambridge Cambridge UK Cambridge University Hospitals NHS Foundation Trust Cambridge UK Department of Applied Mathematics and Theoretical Physics Centre for Mathematical Sciences University of Cambridge Cambridge UK Department of Epidemiology and Biostatistics Memorial Sloan Kettering Cancer Center New York NY USA Department of Statistics Columbia University New York NY USA Department of Haematology University of Cambridge Cambridge UK University of Leuven Leuven Belgium Broad Institute of MIT and Harvard Cambridge MA USA Center for Cancer Research Massachusetts General Hospital Charlestown MA USA Department of Pathology Massachusetts General Hospital Boston MA USA Harvard Medical School Boston MA USA Center for Cancer Research Massachusetts General Hospital Boston MA USA Dana-Farber Cancer Institute Boston MA USA Department of Medical Oncology Dana-Farber Cancer Institute Boston MA USA Department of Cancer Biology Dana-Farber Cancer Institute Boston MA USA Oxford NIHR Biomedical Research Centre Oxford UK Oxford NIHR Biomedical Research Centre University of Oxford Oxford UK University of Toronto Toronto Ontario Canada Vector Institute Toronto Ontario Canada Vector Institute Toronto ON Canada Department of Computer Science University of Toronto Toronto ON Canada Ontario Institute for Cancer Research Toronto Ontario Canada University of California Los Angeles

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Analyses of protein cores reveal fundamental differences between solution and crystal structures

arXiv

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arXiv 2019年

作者： Mei, Zhe Treado, John D. Grigas, Alex T. Levine, Zachary A. Regan, Lynne O'Hern, Corey S. Integrated Graduate Program in Physical & Engineering Biology Yale University New HavenCT06520 United States Department of Chemistry Yale University New HavenCT06520 United States Department of Mechanical Engineering & Materials Science Yale University New HavenCT06520 United States Graduate Program in Computational Biology & Bioinformatics Yale University New HavenCT06520 United States Department of Pathology Yale University New HavenCT06520 United States Department of Molecular Biophysics and Biochemistry Yale University New HavenCT06520 United States Institute of Quantitative Biology Biochemistry and Biotechnology Center for Synthetic and Systems Biology School of Biological Sciences University of Edinburgh Department of Physics Yale University New HavenCT06520 United States Department of Applied Physics Yale University New HavenCT06520 United States

There have been several studies suggesting that protein structures solved by NMR spectroscopy and x-ray crystallography show significant differences. To understand the origin of these differences, we assembled a database of high-quality protein structures solved by both methods. We also find significant differences between NMR and crystal structures|in the root-mean-square deviations of the Cα atomic positions, identities of core amino acids, backbone and sidechain dihedral angles, and packing fraction of core residues. In contrast to prior studies, we identify the physical basis for these differences by modelling protein cores as jammed packings of amino-acid-shaped particles. We find that we can tune the jammed packing fraction by varying the degree of thermalization used to generate the packings. For an athermal protocol, we find that the average jammed packing fraction is identical to that observed in the cores of protein structures solved by x-ray crystallography. In contrast, highly thermalized packing-generation protocols yield jammed packing fractions that are even higher than those observed in NMR structures. These results indicate that thermalized systems can pack more densely than athermal systems, which suggests a physical basis for the structural differences between protein structures solved by NMR and x-ray crystallography. Copyright © 2019, The Authors. All rights reserved.

关键词： X ray crystallography

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Author Correction: Genomic footprints of activated telomere maintenance mechanisms in cancer (Dec, 10.1038/s41467-019-13824-9, 2022)

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NATURE COMMUNICATIONS 2022年第1期13卷 1-1页

作者： Sieverling, Lina Hong, Chen Koser, Sandra D. Ginsbach, Philip Kleinheinz, Kortine Hutter, Barbara Braun, Delia M. Cortes-Ciriano, Isidro Xi, Ruibin Kabbe, Rolf Park, Peter J. Eils, Roland Schlesner, Matthias Brors, Benedikt Rippe, Karsten Jones, David T. W. Feuerbach, Lars Division of Applied Bioinformatics German Cancer Research Center (DKFZ) 69120 Heidelberg Germany Faculty of Biosciences Heidelberg University 69120 Heidelberg Germany Division of Applied Bioinformatics German Cancer Research Center (DKFZ) Heidelberg Germany Faculty of Biosciences Heidelberg University Heidelberg Germany Division of Theoretical Bioinformatics German Cancer Research Center (DKFZ) 69120 Heidelberg Germany Department for Bioinformatics and Functional Genomics Institute for Pharmacy and Molecular Biotechnology (IPMB) and BioQuant 69120 Heidelberg Germany Division of Theoretical Bioinformatics German Cancer Research Center (DKFZ) Heidelberg Germany Institute of Pharmacy and Molecular Biotechnology and BioQuant Heidelberg University Heidelberg Germany German Cancer Consortium (DKTK) Heidelberg Germany National Center for Tumor Diseases (NCT) Heidelberg Heidelberg Germany Heidelberg Center for Personalized Oncology (DKFZ-HIPO) German Cancer Research Center (DKFZ) Heidelberg Germany German Cancer Consortium (DKTK) German Cancer Research Center (DKFZ) Heidelberg Germany Division of Chromatin Networks German Cancer Research Center (DKFZ) and BioQuant 69120 Heidelberg Germany Department of Biomedical Informatics Harvard Medical School Boston Massachusetts 02115 USA Department of Chemistry Centre for Molecular Science Informatics University of Cambridge Cambridge CB2 1EW UK Ludwig Center at Harvard Medical School Boston Massachusetts 02115 USA Department of Biomedical Informatics Harvard Medical School Boston MA USA Department of Chemistry Centre for Molecular Science Informatics University of Cambridge Cambridge UK Ludwig Center at Harvard Medical School Boston MA USA School of Mathematical Sciences and Center for Statistical Science Peking University Beijing 100871 China Heidelberg University Heidelberg Germany New BIH Digital Health Center Berlin Institute of Health (BIH) and Charité - Universitätsmedizin Berlin Berlin Germany Bioi

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Structuring stress for active materials control

arXiv

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arXiv 2019年

作者： Zhang, Rui Redford, Steven A. Ruijgrok, Paul V. Kumar, Nitin Mozaffari, Ali Zemsky, Sasha Dinner, Aaron R. Vitelli, Vincenzo Bryant, Zev Gardel, Margaret L. de Pablo, Juan J. Pritzker School of Molecular Engineering University of Chicago ChicagoIL60637 United States The graduate program in Biophysical Sciences University of Chicago ChicagoIL60637 United States James Franck Institute University of Chicago ChicagoIL60637 United States Department of Bioengineering Stanford University StanfordCA94305 United States Program in Biophysics Stanford University StanfordCA94305 United States Department of Chemistry University of Chicago ChicagoIL60637 United States Department of Physics University of Chicago ChicagoIL60637 United States Department of Structural Biology Stanford University Medical Center StanfordCA94305 United States Center for Molecular Engineering Argonne National Laboratory LemontIL60439 United States

Active materials are capable of converting free energy into mechanical work to produce autonomous motion, and exhibit striking collective dynamics that biology relies on for essential functions. Controlling those dynamics and transport in synthetic systems has been particularly challenging. Here, we introduce the concept of spatially structured activity as a means to control and manipulate transport in active nematic liquid crystals consisting of actin filaments and light-sensitive myosin motors. Simulations and experiments are used to demonstrate that topological defects can be generated at will, and then constrained to move along specified trajectories, by inducing local stresses in an otherwise passive material. These results provide a foundation for design of autonomous and reconfigurable microfluidic systems where transport is controlled by modulating activity with light. Copyright © 2019, The Authors. All rights reserved.

关键词： Nematic liquid crystals

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New Strategies for Improving CryoEM Single Particle Analysis in EMAN2.2

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Microscopy and Microanalysis 2017年第S1期23卷 810-811页

作者： Steven J. Ludtke Tunay Durmaz Muyuan Chen James M. Bell Verna and Marrs McLean Dept. of Biochemistry Baylor College of Medicine Houston TX USA. Graduate Program in Structural and Computational Biology & Molecular Biophysics Baylor College of Medicine Houston TX USA.

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