Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
暂无分享,去创建一个
Daniel Wrapp | Jesper Pallesen | Jason S McLellan | J. Pallesen | B. Graham | H. Turner | A. Ward | J. McLellan | D. Wrapp | Nianshuang Wang | K. Corbett | C. Cottrell | R. Kirchdoerfer | Nianshuang Wang | Kizzmekia S. Corbett | Andrew B Ward | Barney S Graham | Robert N Kirchdoerfer | Hannah L Turner | Christopher A Cottrell | Kizzmekia S Corbett | R. N. Kirchdoerfer
[1] Fang Li,et al. Cryo-Electron Microscopy Structure of Porcine Deltacoronavirus Spike Protein in the Prefusion State , 2017, Journal of Virology.
[2] J. Skehel,et al. Structure of influenza haemagglutinin at the pH of membrane fusion , 1994, Nature.
[3] S. Harrison,et al. Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor , 2005, Science.
[4] F. Dimaio,et al. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer , 2016, Nature.
[5] Ralph S. Baric,et al. Recombination, Reservoirs, and the Modular Spike: Mechanisms of Coronavirus Cross-Species Transmission , 2009, Journal of Virology.
[6] A. Grindeanu. [Immunity and vaccination]. , 1971, Munca sanitara.
[7] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[8] Barney S. Graham,et al. Pre-fusion structure of a human coronavirus spike protein , 2016, Nature.
[9] F. Taguchi,et al. Two-Step Conformational Changes in a Coronavirus Envelope Glycoprotein Mediated by Receptor Binding and Proteolysis , 2009, Journal of Virology.
[10] Frank DiMaio,et al. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy , 2016, Nature Structural &Molecular Biology.
[11] Anchi Cheng,et al. Automated molecular microscopy: the new Leginon system. , 2005, Journal of structural biology.
[12] K. Nakagaki,et al. N-Terminal Domain of the Murine Coronavirus Receptor CEACAM1 Is Responsible for Fusogenic Activation and Conformational Changes of the Spike Protein , 2004, Journal of Virology.
[13] Lisa E. Gralinski,et al. SARS-like WIV1-CoV poised for human emergence , 2016, Proceedings of the National Academy of Sciences.
[14] John P. Moore,et al. Structural Characterization of Cleaved, Soluble HIV-1 Envelope Glycoprotein Trimers , 2013, Journal of Virology.
[15] J. Morais-Cabral,et al. 310 helices in channels and other membrane proteins , 2010, The Journal of general physiology.
[16] G. Whittaker,et al. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites , 2009, Proceedings of the National Academy of Sciences.
[17] Andrew B. Ward,et al. EMHP: an accurate automated hole masking algorithm for single-particle cryo-EM image processing , 2017, bioRxiv.
[18] John P. Moore,et al. Stabilization of the Soluble, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1 , 2002, Journal of Virology.
[19] Sriram Subramaniam,et al. Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures , 2011, Proceedings of the National Academy of Sciences.
[20] D. Falzarano,et al. SARS and MERS: recent insights into emerging coronaviruses , 2016, Nature Reviews Microbiology.
[21] A. Walls,et al. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion , 2017, Proceedings of the National Academy of Sciences.
[22] B. Bosch,et al. The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex , 2003, Journal of Virology.
[23] Gary R. Whittaker,et al. Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis , 2014, Virus Research.
[24] M Radermacher,et al. DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. , 2009, Journal of structural biology.
[25] S. Diamond,et al. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[26] Min-sheng Zhu,et al. SARS Immunity and Vaccination. , 2004, Cellular & molecular immunology.
[27] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[28] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[29] John P. Moore,et al. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies , 2013, PLoS pathogens.
[30] Yi Shi,et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains , 2017, Nature Communications.
[31] G. Gao,et al. Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection , 2016, Cell.
[32] Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections , 2017, Journal of Virology.
[33] John P. Moore,et al. Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike , 2017, Nature.
[34] Matthias J. Brunner,et al. Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local refinement , 2015, Nature Methods.
[35] S. Perlman,et al. Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism , 2016, Proceedings of the National Academy of Sciences.
[36] Jung-Eun Park,et al. Receptor-bound porcine epidemic diarrhea virus spike protein cleaved by trypsin induces membrane fusion , 2011, Archives of Virology.
[37] Kai Zhang,et al. Gctf: Real-time CTF determination and correction , 2015, bioRxiv.
[38] Barney S. Graham,et al. Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen , 2017, Proceedings of the National Academy of Sciences.
[39] John L. Sullivan,et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus , 2003, Nature.
[40] T. Mizutani,et al. Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein. , 2005, The Journal of general virology.
[41] Christopher Irving,et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. , 2009, Journal of structural biology.
[42] G. Whittaker,et al. Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein , 2012, Viruses.
[43] Fabian Sievers,et al. Clustal Omega , 2014, Current protocols in bioinformatics.
[44] G. Millhauser. Views of helical peptides: a proposal for the position of 3(10)-helix along the thermodynamic folding pathway. , 1995, Biochemistry.
[45] Makoto Takeda,et al. Efficient Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by the Transmembrane Protease TMPRSS2 , 2010, Journal of Virology.
[46] Haixia Zhou,et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding , 2016, Cell Research.
[47] J. Freed,et al. The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner , 2017, Journal of Molecular Biology.
[48] S. Morikawa,et al. Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[49] G. Sapiro,et al. Molecular architecture of native HIV-1 gp120 trimers , 2008, Nature.
[50] E. Lindahl,et al. Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2 , 2016, bioRxiv.
[51] G. Gao,et al. Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1 , 2016, Cell.
[52] G. Whittaker,et al. Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells , 2017, Virology.
[53] Wenhui Li,et al. A 193-Amino Acid Fragment of the SARS Coronavirus S Protein Efficiently Binds Angiotensin-converting Enzyme 2* , 2004, Journal of Biological Chemistry.