Nonstructural Protein 1 of SARS-CoV-2 Is a Potent Pathogenicity Factor Redirecting Host Protein Synthesis Machinery toward Viral RNA
Published 2020 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Nonstructural Protein 1 of SARS-CoV-2 Is a Potent Pathogenicity Factor Redirecting Host Protein Synthesis Machinery toward Viral RNA
Authors
Keywords
SARS-CoV-2, Nsp1, cell viability, transcriptome alteration, cryo-EM, ribosome, translation inhibition mechanism
Journal
MOLECULAR CELL
Volume 80, Issue 6, Pages 1055-1066.e6
Publisher
Elsevier BV
Online
2020-10-30
DOI
10.1016/j.molcel.2020.10.034
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Structure of the RNA specialized translation initiation element that recruits eIF3 to the 5’-UTR of c-Jun
- (2020) Matthew J. Walker et al. JOURNAL OF MOLECULAR BIOLOGY
- A pneumonia outbreak associated with a new coronavirus of probable bat origin
- (2020) Peng Zhou et al. NATURE
- The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2
- (2020) Nature Microbiology
- The Architecture of SARS-CoV-2 Transcriptome
- (2020) Dongwan Kim et al. CELL
- Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19
- (2020) Daniel Blanco-Melo et al. CELL
- SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
- (2020) Markus Hoffmann et al. CELL
- Hepatitis C Virus Translation Regulation
- (2020) Michael Niepmann et al. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
- (2020) David E. Gordon et al. NATURE
- Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2
- (2020) Matthias Thoms et al. SCIENCE
- SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation
- (2020) Katharina Schubert et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Tetrapeptide 60–63 of human ribosomal protein uS3 is crucial for translation initiation
- (2019) Elena Babaylova et al. Biochimica et Biophysica Acta-Gene Regulatory Mechanisms
- Mechanism of ribosome stalling during translation of a poly(A) tail
- (2019) Viswanathan Chandrasekaran et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Insights into Structural and Mechanistic Features of Viral IRES Elements
- (2018) Encarnacion Martinez-Salas et al. Frontiers in Microbiology
- Efficient and Accurate Translation Initiation Directed by TISU Involves RPS3 and RPS10e Binding and Differential Eukaryotic Initiation Factor 1A Regulation
- (2017) Ora Haimov et al. MOLECULAR AND CELLULAR BIOLOGY
- Differential analysis of RNA-seq incorporating quantification uncertainty
- (2017) Harold Pimentel et al. NATURE METHODS
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- Human eIF3: from ‘blobology’ to biological insight
- (2017) Jamie H. D. Cate PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
- Rps3/uS3 promotes mRNA binding at the 40S ribosome entry channel and stabilizes preinitiation complexes at start codons
- (2017) Jinsheng Dong et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation
- (2017) Alan G. Hinnebusch TRENDS IN BIOCHEMICAL SCIENCES
- Exploring accessibility of structural elements of the mammalian 40S ribosomal mRNA entry channel at various steps of translation initiation
- (2016) Dmitri E. Sharifulin et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation
- (2016) Amy S. Y. Lee et al. NATURE
- Near-optimal probabilistic RNA-seq quantification
- (2016) Nicolas L Bray et al. NATURE BIOTECHNOLOGY
- Translational control by 5'-untranslated regions of eukaryotic mRNAs
- (2016) A. G. Hinnebusch et al. SCIENCE
- Structural characterization of ribosome recruitment and translocation by type IV IRES
- (2016) Jason Murray et al. eLife
- A Cap-to-Tail Guide to mRNA Translation Strategies in Virus-Infected Cells
- (2016) Eric Jan et al. Annual Review of Virology
- Molecular contacts of ribose-phosphate backbone of mRNA with human ribosome
- (2015) Dmitri E. Sharifulin et al. Biochimica et Biophysica Acta-Gene Regulatory Mechanisms
- The role of eIF3 and its individual subunits in cancer
- (2015) John W.B. Hershey Biochimica et Biophysica Acta-Gene Regulatory Mechanisms
- Genome-Wide Screen Reveals Valosin-Containing Protein Requirement for Coronavirus Exit from Endosomes
- (2015) Hui Hui Wong et al. JOURNAL OF VIROLOGY
- Structure of a Yeast 40S–eIF1–eIF1A–eIF3–eIF3j initiation complex
- (2015) Christopher H S Aylett et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structure of a Yeast 40S–eIF1–eIF1A–eIF3–eIF3j initiation complex
- (2015) Christopher H S Aylett et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural insights into viral IRES-dependent translation mechanisms
- (2015) Gloria Lozano et al. Current Opinion in Virology
- The Scanning Mechanism of Eukaryotic Translation Initiation
- (2014) Alan G. Hinnebusch Annual Review of Biochemistry
- Human Eukaryotic Initiation Factor 2 (eIF2)-GTP-Met-tRNAiTernary Complex and eIF3 Stabilize the 43 S Preinitiation Complex
- (2014) Masaaki Sokabe et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Eukaryotic ribosomal protein S3: A constituent of translational machinery and an extraribosomal player in various cellular processes
- (2013) Dmitri Graifer et al. BIOCHIMIE
- The initiation of mammalian protein synthesis and mRNA scanning mechanism
- (2013) Ivan B. Lomakin et al. NATURE
- Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit
- (2013) Yaser Hashem et al. NATURE
- Severe Acute Respiratory Syndrome Coronavirus Protein nsp1 Is a Novel Eukaryotic Translation Inhibitor That Represses Multiple Steps of Translation Initiation
- (2012) K. G. Lokugamage et al. JOURNAL OF VIROLOGY
- Severe Acute Respiratory Syndrome Coronavirus nsp1 Facilitates Efficient Propagation in Cells through a Specific Translational Shutoff of Host mRNA
- (2012) T. Tanaka et al. JOURNAL OF VIROLOGY
- Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
- (2011) F. Sievers et al. Molecular Systems Biology
- Viral subversion of the host protein synthesis machinery
- (2011) Derek Walsh et al. NATURE REVIEWS MICROBIOLOGY
- Mechanism of translation initiation by Dicistroviridae IGR IRESs
- (2011) Marla I. Hertz et al. VIROLOGY
- SARS Coronavirus nsp1 Protein Induces Template-Dependent Endonucleolytic Cleavage of mRNAs: Viral mRNAs Are Resistant to nsp1-Induced RNA Cleavage
- (2011) Cheng Huang et al. PLoS Pathogens
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Suppression of Host Gene Expression by nsp1 Proteins of Group 2 Bat Coronaviruses
- (2009) Y. Tohya et al. JOURNAL OF VIROLOGY
- Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
- (2009) Da Wei Huang et al. Nature Protocols
- A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
- (2009) Wataru Kamitani et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
- (2008) Andrey V Pisarev et al. EMBO JOURNAL
- Severe Acute Respiratory Syndrome Coronavirus nsp1 Suppresses Host Gene Expression, Including That of Type I Interferon, in Infected Cells
- (2008) K. Narayanan et al. JOURNAL OF VIROLOGY
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started