The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein
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J. Diedrich | J. Yates | E. Villa | K. Corbett | D. Cleveland | Yong Cao | Q. Ye | Sha Lu | Digvijay Singh
[1] Nicolas L. Fawzi,et al. SARS‐CoV‐2 nucleocapsid protein phase‐separates with RNA and with human hnRNPs , 2020, The EMBO journal.
[2] B. Blencowe,et al. SARS-CoV-2 Nucleocapsid protein attenuates stress granule formation and alters gene expression via direct interaction with host mRNAs , 2020, bioRxiv.
[3] D. Morgan,et al. Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions , 2020, Molecular Cell.
[4] M. Trnka,et al. SARS-CoV-2 nucleocapsid protein forms condensates with viral genomic RNA , 2020, bioRxiv.
[5] K. Corbett,et al. Architecture and self‐assembly of the SARS‐CoV‐2 nucleocapsid protein , 2020, Protein science : a publication of the Protein Society.
[6] Ralf Bartenschlager,et al. SARS-CoV-2 structure and replication characterized by in situ cryo-electron tomography , 2020, Nature Communications.
[7] S. Cascarina,et al. A proposed role for the SARS‐CoV‐2 nucleocapsid protein in the formation and regulation of biomolecular condensates , 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[8] M. Zweckstetter,et al. Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates , 2020, Nature Communications.
[9] Maxwell I. Zimmerman,et al. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA , 2020, bioRxiv.
[10] Chandra L. Theesfeld,et al. Specific viral RNA drives the SARS CoV-2 nucleocapsid to phase separate , 2020, bioRxiv.
[11] K. Corbett,et al. Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein , 2020, bioRxiv.
[12] Benjamin J. Polacco,et al. A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug-Repurposing , 2020, Nature.
[13] Zhigang Wu,et al. Molecular Architecture of the SARS-CoV-2 Virus , 2020, Cell.
[14] Xiaoxu Tian,et al. Virus-Host Interactome and Proteomic Survey Reveal Potential Virulence Factors Influencing SARS-CoV-2 Pathogenesis , 2020, bioRxiv.
[15] V. Uversky,et al. Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis , 2020, Progress in Molecular Biology and Translational Science.
[16] M. Blackledge,et al. Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly , 2020, Science Advances.
[17] Meijuan Niu,et al. Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking , 2020, Cell reports.
[18] E. Dong,et al. An interactive web-based dashboard to track COVID-19 in real time , 2020, The Lancet Infectious Diseases.
[19] Kai Zhao,et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin , 2020, Nature.
[20] R. Parker,et al. Norovirus infection results in eIF2α independent host translation shut-off and remodels the G3BP1 interactome evading stress granule formation , 2020, PLoS pathogens.
[21] Jingjing Ren,et al. G3BP1 inhibits RNA virus replication by positively regulating RIG-I-mediated cellular antiviral response , 2019, Cell Death & Disease.
[22] M. Ulaşlı,et al. Nucleocapsid Protein Recruitment to Replication-Transcription Complexes Plays a Crucial Role in Coronaviral Life Cycle , 2019, Journal of Virology.
[23] Jiwon Woo,et al. An in vivo cell-based assay for investigating the specific interaction between the SARS-CoV N-protein and its viral RNA packaging sequence , 2019, Biochemical and Biophysical Research Communications.
[24] Qiuhong Wang,et al. GTPase-activating protein-binding protein 1 (G3BP1) plays an antiviral role against porcine epidemic diarrhea virus , 2019, Veterinary Microbiology.
[25] Hao Chi,et al. A high-speed search engine pLink 2 with systematic evaluation for proteome-scale identification of cross-linked peptides , 2019, Nature Communications.
[26] Lin Guo,et al. Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death , 2019, Neuron.
[27] M. Panas,et al. Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation , 2019, bioRxiv.
[28] K. Lam,et al. The stress granule protein G3BP1 binds viral dsRNA and RIG-I to enhance interferon-β response , 2019, The Journal of Biological Chemistry.
[29] Shinji Makino,et al. Inhibition of Stress Granule Formation by Middle East Respiratory Syndrome Coronavirus 4a Accessory Protein Facilitates Viral Translation, Leading to Efficient Virus Replication , 2018, Journal of Virology.
[30] Anne-Claude Gingras,et al. High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. , 2018, Molecular cell.
[31] Gene W. Yeo,et al. Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules , 2018, Cell.
[32] E. Martínez-Salas,et al. G3BP1 interacts directly with the FMDV IRES and negatively regulates translation , 2017, The FEBS journal.
[33] A. Deniz,et al. Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets. , 2017, Angewandte Chemie.
[34] Beata Turoňová,et al. Efficient 3D-CTF correction for cryo-electron tomography using NovaCTF improves subtomogram averaging resolution to 3.4 Å , 2017, Journal of structural biology.
[35] Cathy L. Miller,et al. Mammalian Orthoreovirus Factories Modulate Stress Granule Protein Localization by Interaction with G3BP1 , 2017, Journal of Virology.
[36] Jiahui Chen,et al. Improvements to the APBS biomolecular solvation software suite , 2017, Protein science : a publication of the Protein Society.
[37] Sonja Kroschwald,et al. Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments , 2017 .
[38] Y. Liao,et al. Newcastle disease virus induces stable formation of bona fide stress granules to facilitate viral replication through manipulating host protein translation , 2017, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[39] D. Agard,et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.
[40] J. Briggs,et al. Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging , 2017, Journal of structural biology.
[41] Robert H. Brown,et al. Decoding ALS: from genes to mechanism , 2016, Nature.
[42] R. Parker,et al. Principles and Properties of Stress Granules. , 2016, Trends in cell biology.
[43] Ben Lehner,et al. A Concentration-Dependent Liquid Phase Separation Can Cause Toxicity upon Increased Protein Expression , 2016, Cell reports.
[44] C. A. Koetzner,et al. Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein Chimeras , 2016, Journal of Virology.
[45] Roy Parker,et al. Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins. , 2015, Molecular cell.
[46] A. Kanagaraj,et al. Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization , 2015, Cell.
[47] Marco Y. Hein,et al. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation , 2015, Cell.
[48] C. Brangwynne,et al. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics , 2015, Proceedings of the National Academy of Sciences.
[49] M. V. van Hemert,et al. Stress Granule Components G3BP1 and G3BP2 Play a Proviral Role Early in Chikungunya Virus Replication , 2015, Journal of Virology.
[50] Colin W. Combe,et al. xiNET: Cross-link Network Maps With Residue Resolution , 2015, Molecular & Cellular Proteomics.
[51] Lucas C. Reineke,et al. The Stress Granule Protein G3BP1 Recruits Protein Kinase R To Promote Multiple Innate Immune Antiviral Responses , 2014, Journal of Virology.
[52] David T. Jones,et al. DISOPRED3: precise disordered region predictions with annotated protein-binding activity , 2014, Bioinform..
[53] Pei-Jer Chen,et al. Nucleocapsid Phosphorylation and RNA Helicase DDX1 Recruitment Enables Coronavirus Transition from Discontinuous to Continuous Transcription , 2014, Cell Host & Microbe.
[54] A. Hyman,et al. Liquid-liquid phase separation in biology. , 2014, Annual review of cell and developmental biology.
[55] B. Fielding,et al. The Coronavirus Nucleocapsid Is a Multifunctional Protein , 2014, Viruses.
[56] Hao Chi,et al. pQuant improves quantitation by keeping out interfering signals and evaluating the accuracy of calculated ratios. , 2014, Analytical chemistry.
[57] Honglin Luo,et al. Production of a Dominant-Negative Fragment Due to G3BP1 Cleavage Contributes to the Disruption of Mitochondria-Associated Protective Stress Granules during CVB3 Infection , 2013, PloS one.
[58] Tai-Huang Huang,et al. Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging , 2013, PloS one.
[59] Cara T. Pager,et al. Modulation of hepatitis C virus RNA abundance and virus release by dispersion of processing bodies and enrichment of stress granules. , 2013, Virology.
[60] D. Giedroc,et al. Solution Structure of Mouse Hepatitis Virus (MHV) nsp3a and Determinants of the Interaction with MHV Nucleocapsid (N) Protein , 2013, Journal of Virology.
[61] T. Parisi,et al. The Virion Host Shutoff RNase Plays a Key Role in Blocking the Activation of Protein Kinase R in Cells Infected with Herpes Simplex Virus 1 , 2013, Journal of Virology.
[62] Lucas C. Reineke,et al. Diversion of stress granules and P-bodies during viral infection , 2013, Virology.
[63] Debasis Panda,et al. Induction of Stress Granule-Like Structures in Vesicular Stomatitis Virus-Infected Cells , 2012, Journal of Virology.
[64] F. Chisari,et al. Hepatitis C Virus (HCV) Induces Formation of Stress Granules Whose Proteins Regulate HCV RNA Replication and Virus Assembly and Egress , 2012, Journal of Virology.
[65] M. Dong,et al. Identification of cross-linked peptides from complex samples , 2012, Nature Methods.
[66] C. Brangwynne,et al. Getting RNA and Protein in Phase , 2012, Cell.
[67] Denys A. Khaperskyy,et al. Influenza A virus inhibits cytoplasmic stress granule formation , 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[68] N. Kato,et al. Hepatitis C Virus Hijacks P-Body and Stress Granule Components around Lipid Droplets , 2011, Journal of Virology.
[69] P. Anderson,et al. Formation of Antiviral Cytoplasmic Granules during Orthopoxvirus Infection , 2010, Journal of Virology.
[70] I. Wilson,et al. A structural analysis of M protein in coronavirus assembly and morphology , 2010, Journal of Structural Biology.
[71] P. Rottier,et al. The Coronavirus Nucleocapsid Protein Is Dynamically Associated with the Replication-Transcription Complexes , 2010, Journal of Virology.
[72] S. Whelan,et al. Protein Expression Redirects Vesicular Stomatitis Virus RNA Synthesis to Cytoplasmic Inclusions , 2010, PLoS pathogens.
[73] B. Chait,et al. Host Factors Associated with the Sindbis Virus RNA-Dependent RNA Polymerase: Role for G3BP1 and G3BP2 in Virus Replication , 2010, Journal of Virology.
[74] R. Parker,et al. Eukaryotic stress granules: the ins and outs of translation. , 2009, Molecular cell.
[75] I. Sola,et al. Coronavirus Nucleocapsid Protein Facilitates Template Switching and Is Required for Efficient Transcription , 2009, Journal of Virology.
[76] D. Giedroc,et al. Coronavirus N Protein N-Terminal Domain (NTD) Specifically Binds the Transcriptional Regulatory Sequence (TRS) and Melts TRS-cTRS RNA Duplexes , 2009, Journal of Molecular Biology.
[77] Ding‐Shinn Chen,et al. Glycogen Synthase Kinase-3 Regulates the Phosphorylation of Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Protein and Viral Replication* , 2009, Journal of Biological Chemistry.
[78] Abraham J. Koster,et al. Cryo-electron tomography of mouse hepatitis virus: Insights into the structure of the coronavirion , 2009, Proceedings of the National Academy of Sciences.
[79] Kuan-rong Lee,et al. Phosphorylation of the arginine/serine dipeptide‐rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization , 2008, The FEBS journal.
[80] P. Anderson,et al. Stress granules: the Tao of RNA triage. , 2008, Trends in biochemical sciences.
[81] R. Lloyd,et al. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. , 2007, Cell host & microbe.
[82] C. M. Romero,et al. Effect of temperature on the surface tension of diluted aqueous solutions of 1,2-hexanediol, 1,5-hexanediol, 1,6-hexanediol and 2,5-hexanediol , 2007 .
[83] B. Hogue,et al. Identification of mouse hepatitis coronavirus A59 nucleocapsid protein phosphorylation sites , 2007, Virus Research.
[84] C. Hsiao,et al. Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA , 2007, Journal of Molecular Biology.
[85] I. Mohr,et al. Maintenance of Endoplasmic Reticulum (ER) Homeostasis in Herpes Simplex Virus Type 1-Infected Cells through the Association of a Viral Glycoprotein with PERK, a Cellular ER Stress Sensor , 2007, Journal of Virology.
[86] I. Sola,et al. Coronavirus nucleocapsid protein is an RNA chaperone , 2006, Virology.
[87] Stuart G. Siddell,et al. A Contemporary View of Coronavirus Transcription , 2006, Journal of Virology.
[88] I. Yu,et al. Crystal Structure of the Severe Acute Respiratory Syndrome (SARS) Coronavirus Nucleocapsid Protein Dimerization Domain Reveals Evolutionary Linkage between Corona- and Arteriviridae* , 2006, Journal of Biological Chemistry.
[89] J. Onderwater,et al. Ultrastructure and Origin of Membrane Vesicles Associated with the Severe Acute Respiratory Syndrome Coronavirus Replication Complex , 2006, Journal of Virology.
[90] Tai-Huang Huang,et al. Assembly of Severe Acute Respiratory Syndrome Coronavirus RNA Packaging Signal into Virus-Like Particles Is Nucleocapsid Dependent , 2005, Journal of Virology.
[91] C. A. Koetzner,et al. A Major Determinant for Membrane Protein Interaction Localizes to the Carboxy-Terminal Domain of the Mouse Coronavirus Nucleocapsid Protein , 2005, Journal of Virology.
[92] Adam Zlotnick,et al. Theoretical aspects of virus capsid assembly , 2005, Journal of molecular recognition : JMR.
[93] Wei-Lun Chang,et al. Modular organization of SARS coronavirus nucleocapsid protein , 2005, Journal of biomedical science.
[94] David N Mastronarde,et al. Automated electron microscope tomography using robust prediction of specimen movements. , 2005, Journal of structural biology.
[95] Tai-Huang Huang,et al. The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus‐like structure , 2005, FEBS Letters.
[96] Hongying Chen,et al. Mass Spectroscopic Characterization of the Coronavirus Infectious Bronchitis Virus Nucleoprotein and Elucidation of the Role of Phosphorylation in RNA Binding by Using Surface Plasmon Resonance , 2005, Journal of Virology.
[97] A. Gunasekera,et al. Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein. , 2004, Biochemistry.
[98] V. Chow,et al. The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain , 2004, Biochemical and Biophysical Research Communications.
[99] Alexander E Gorbalenya,et al. Mechanisms and enzymes involved in SARS coronavirus genome expression. , 2003, The Journal of general virology.
[100] Y. Guan,et al. Unique and Conserved Features of Genome and Proteome of SARS-coronavirus, an Early Split-off From the Coronavirus Group 2 Lineage , 2003, Journal of Molecular Biology.
[101] D. Görlich,et al. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion , 2002, The EMBO journal.
[102] M. Gross,et al. The Herpes Simplex Virus Type 1 US11 Protein Interacts with Protein Kinase R in Infected Cells and Requires a 30-Amino-Acid Sequence Adjacent to a Kinase Substrate Domain , 2002, Journal of Virology.
[103] L. Enjuanes,et al. The Membrane M Protein Carboxy Terminus Binds to Transmissible Gastroenteritis Coronavirus Core and Contributes to Core Stability , 2001, Journal of Virology.
[104] B. Roizman,et al. The γ134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase , 1997 .
[105] P. Masters. Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus , 1992, Archives of Virology.
[106] P. Masters,et al. Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein , 1990, Virology.
[107] R. Baric,et al. Specific interaction between coronavirus leader RNA and nucleocapsid protein , 1988, Journal of virology.
[108] H. Davies,et al. Ribonucleoprotein of avian infectious bronchitis virus. , 1981, The Journal of general virology.
[109] E. Caul,et al. Coronavirus-like particles present in simian faeces , 1979, Veterinary Record.
[110] H. Davies,et al. Ribonucleoprotein-like structures from coronavirus particles. , 1978, The Journal of general virology.
[111] S. Tahara,et al. High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA. , 2000, The Journal of general virology.
[112] J R Kremer,et al. Computer visualization of three-dimensional image data using IMOD. , 1996, Journal of structural biology.