Evidence map›Paper›PMID 19828617›Full record

ArticleJournal of virology2009

Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3.

Pedro Serrano, Margaret A Johnson, Amarnath Chatterjee, Benjamin W Neuman, Jeremiah S Joseph, Michael J Buchmeier, Peter Kuhn, Kurt Wüthrich

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
0.6field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Why do SARS-CoV-2 NSPs rush to the ER?Journal of neurology · 2021
    Review
  10. Biomolecular NMR assignments · 2021
    Article
  11. Genome composition and genetic characterization of SARS-CoV-2.Saudi journal of biological sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Biomolecular NMR assignments · 2020
    Article
  19. The molecular virology of coronaviruses.The Journal of biological chemistry · 2020
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Pedro SerranoDepartment of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., MB-44, La Jolla, CA 92037, USA.
Margaret A Johnson
Amarnath Chatterjee
Benjamin W Neuman
Jeremiah S Joseph
Michael J Buchmeier
Peter Kuhn
Kurt Wüthrich
Laboratoire d’immunologie intégrative du cancer · FRScripps Research Institute · USUniversity of California, Irvine · US

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2005 to 2009
$50.6M
Human T-cell Epitopes in SARSR01AI059799 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BUCHMEIER, MICHAEL JOSEPH · 2005 to 2008
$2.1M
CIHRNIAID NIH HHS AI059799NIAID NIH HHS R01 AI059799NIGMS NIH HHS U54 GM074898NIGMS NIH HHS U54-GM074898
6 · The paper itself

Abstract

The nuclear magnetic resonance (NMR) structure of a globular domain of residues 1071 to 1178 within the previously annotated nucleic acid-binding region (NAB) of severe acute respiratory syndrome coronavirus nonstructural protein 3 (nsp3) has been determined, and N- and C-terminally adjoining polypeptide segments of 37 and 25 residues, respectively, have been shown to form flexibly extended linkers to the preceding globular domain and to the following, as yet uncharacterized domain. This extension of the structural coverage of nsp3 was obtained from NMR studies with an nsp3 construct comprising residues 1066 to 1181 [nsp3(1066-1181)] and the constructs nsp3(1066-1203) and nsp3(1035-1181). A search of the protein structure database indicates that the globular domain of the NAB represents a new fold, with a parallel four-strand beta-sheet holding two alpha-helices of three and four turns that are oriented antiparallel to the beta-strands. Two antiparallel two-strand beta-sheets and two 3(10)-helices are anchored against the surface of this barrel-like molecular core. Chemical shift changes upon the addition of single-stranded RNAs (ssRNAs) identified a group of residues that form a positively charged patch on the protein surface as the binding site responsible for the previously reported affinity for nucleic acids. This binding site is similar to the ssRNA-binding site of the sterile alpha motif domain of the Saccharomyces cerevisiae Vts1p protein, although the two proteins do not share a common globular fold.

Indexed as

Amino Acid SequenceBinding SitesMagnetic Resonance SpectroscopyMolecular ConformationMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryRNARNA-Dependent RNA PolymeraseViral Nonstructural ProteinsNsp3 protein, SARS-CoVRNARNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID19828617
PMCPMC2786856
OpenAlexW2136245306

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.