Evidence map›Paper›PMID 33397718›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4.

Robert G Hammond, Norbert Schormann, Robert Lyle McPherson, Anthony K L Leung, Champion C S Deivanayagam, Margaret A Johnson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Mutation of a highly conserved isoleucine residue in loop 2 of severalbioRxiv : the preprint server for biology · 2024
    Article
  7. Review
  8. Article
  9. Reversible modification of mitochondrial ADP/ATP translocases by pairedProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. 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.

Robert G HammondDepartment of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294.ORCID 0000-0001-6934-9655
Norbert SchormannDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294.ORCID 0000-0003-4215-7017
Robert Lyle McPhersonDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.ORCID 0000-0002-5922-889X
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.ORCID 0000-0001-5569-4036
Champion C S DeivanayagamDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294.ORCID 0000-0003-2972-1824
Margaret A JohnsonDepartment of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294; margaret.a.johnson2@gmail.com.ORCID 0000-0002-4422-399X

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
The Structural and Functional Determination of Streptococcus mutans AdherenceR01DE029007 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DEIVANAYAGAM, CHAMPION CHRISTDOSS SELVAKUMAR, WU, HUI · 2020 to 2024
$2.1M
Novel Nucleic Acid-Binding Proteins in Emerging VirusesR35GM119456 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI JOHNSON, MARGARET ALICE · 2016 to 2018
$951k
NCI NIH HHS T32 CA009110NIDCR NIH HHS R01 DE029007NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM104135NIGMS NIH HHS R35 GM119456
6 · The paper itself

Abstract

Macrodomains are proteins that recognize and hydrolyze ADP ribose (ADPR) modifications of intracellular proteins. Macrodomains are implicated in viral genome replication and interference with host cell immune responses. They are important to the infectious cycle of

Indexed as

Adenosine Diphosphate RiboseAnimalsBinding SitesChiropteraCoronavirusCrystallography, X-RayHydrolysisPyrophosphatasesViral Nonstructural ProteinsAdenosine Diphosphate RiboseADPribose pyrophosphatasePyrophosphatasesViral Nonstructural ProteinsADP-ribosecoronaviruscrystal structuremacrodomainviral protein

Identifiers

PMID33397718
PMCPMC7812796

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.