Evidence map›Paper›PMID 37812322›Full record

ArticleBiomolecular NMR assignments2023

Xiang Chen, Kylie J Walters

Abstract read
In one paragraph

Article in Biomolecular NMR assignments, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

  • Update of
    2023
5 · Who and what money

Authors and funding

2 authors.

Xiang ChenProtein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA.ORCID 0000-0002-0036-0212
Kylie J WaltersProtein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA. kylie.walters@nih.gov.ORCID 0000-0001-7590-2891

Funding

Ubiquitin signaling for protein degradationZIABC011490 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WALTERS, KYLIE · 2013 to 2025
$21.1M
Intramural NIH HHS ZIA BC011490Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research to K.J.W. 1 ZIA BC011490
6 · The paper itself

Abstract

hHR23a (human homolog of Rad23 a) functions in nucleotide excision repair and proteasome-mediated protein degradation. It contains an N-terminal ubiquitin-like (UBL) domain, an xeroderma pigmentosum C (XPC)-binding domain, and a ubiquitin-associated (UBA) domain preceding and following the XPC-binding domain. Each of the four structural domains are connected by flexible linker regions. We report in this NMR study, the

Indexed as

DNA Repair EnzymesProteasome Endopeptidase ComplexDNA-Binding ProteinsHumansNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryUbiquitinDNA-Binding ProteinsDNA Repair EnzymesProteasome Endopeptidase ComplexUbiquitinDNA repair proteinNMRRad23Shuttle factorUbiquitin-proteasome pathway

Identifiers

PMID37812322
PMCPMC11284958

What OpenQuestion holds

Textmetadata
LicenceTDM
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.