Evidence map›Paper›PMID 32395093›Full record

ArticleNatural product communications2019

Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4.

Andrew J Staup, Ivon U De Silva, Justin T Catt, Xuan Tan, Robert G Hammond, Margaret A Johnson

Abstract read
In one paragraph

Article in Natural product communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Biomolecular NMR assignments · 2021
    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

6 authors.

Andrew J StaupDepartment of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Ivon U De SilvaDepartment of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Justin T CattDepartment of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Xuan TanDepartment of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Robert G HammondDepartment of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Margaret A JohnsonDepartment of Chemistry, 1720 2nd Avenue S. CHEM 274, University of Alabama at Birmingham, AL, USA.

Funding

Novel Nucleic Acid-Binding Proteins in Emerging VirusesR35GM119456 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI JOHNSON, MARGARET ALICE · 2016 to 2018
$951k
NIGMS NIH HHS R35 GM119456
6 · The paper itself

Abstract

Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated in viral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from the SARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against 2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the function of HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3. The HKU4 C residues involved in protein-protein interactions are conserved in group 2c CoVs, indicating a conserved function.

Indexed as

chemical shift perturbationcoronavirusfunctional annotationMERSNMRnon-structural proteinSARS-unique domain

Identifiers

PMID32395093
PMCPMC7206560

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.