ArticleProtein & cell2010
New nsp8 isoform suggests mechanism for tuning viral RNA synthesis.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- Structural biology of SARS-CoV-2 and implications for therapeutic development.Nature reviews. Microbiology · 2021Review
- Hallmarks ofScience advances · 2021Article
- Hallmarks ofbioRxiv : the preprint server for biology · 2020Article
- Article
- Structure of the RNA-dependent RNA polymerase from COVID-19 virus.Science (New York, N.Y.) · 2020Article
- Processing of the SARS-CoV pp1a/ab nsp7-10 region.The Biochemical journal · 2020Article
- Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2.Molecular biomedicine · 2020Article
- Strategies for Targeting SARS CoV-2: Small Molecule Inhibitors-The Current Status.Frontiers in immunology · 2020Review
- The newly emerged SARS-like coronavirus HCoV-EMC also has an "Achilles' heel": current effective inhibitor targeting a 3C-like protease.Protein & cell · 2013Article
- Purification, crystallization and preliminary X-ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Nonstructural proteins 7 and 8 of feline coronavirus form a 2:1 heterotrimer that exhibits primer-independent RNA polymerase activity.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During severe acute respiratory syndrome coronavirus (SARS-CoV) infection, the activity of the replication/transcription complexes (RTC) quickly peaks at 6 hours post infection (h.p.i) and then diminishes significantly in the late post-infection stages. This "down-up-down" regulation of RNA synthesis distinguishes different viral stages: primary translation, genome replication, and finally viron assembly. Regarding the nsp8 as the primase in RNA synthesis, we confirmed that the proteolysis product of the primase (nsp8) contains the globular domain (nsp8C), and indentified the resectioning site that is notably conserved in all the three groups of coronavirus. We subsequently crystallized the complex of SARS-CoV nsp8C and nsp7, and the 3-D structure of this domain revealed its capability to interfuse into the hexadecamer super-complex. This specific proteolysis may indicate one possible mechanism by which coronaviruses to switch from viral infection to genome replication and viral assembly stages.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.