Evidence map›Paper›PMID 27188292›Full record

ArticleBiomolecular NMR assignments2016

(1)H, (15)N, (13)C resonance assignments for Saccharomyces cerevisiae Rad23 UBL domain.

Xiang Chen, Kylie J Walters

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2016. 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, top 97% of its field
1 · What the graph read from it

What it found

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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.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Xiang ChenProtein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.
Kylie J WaltersProtein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA. kylie.walters@nih.gov.
National Cancer Institute · US

Funding

Ubiquitin signaling for protein degradationZIABC011490 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WALTERS, KYLIE · 2013 to 2025
$21.1M
Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC011490
6 · The paper itself

Abstract

Rad23 functions in nucleotide excision repair and proteasome-mediated protein degradation. It has four distinct structural domains that are connected by flexible linker regions, including an N-terminal ubiquitin-like (UBL) domain that binds proteasomes. We report in this NMR study the (1)H, (15)N and (13)C resonance assignments for the backbone and side chain atoms of the Rad23 UBL domain (Rad23(UBL)) with BioMagResBank accession number 25825. We find that a Rad23 proline amino acid (P20) located in a loop undergoes isomerization. The secondary structural elements predicted from the NMR data fit well to that of the Rad23(UBL) when complexed with E4 ubiquitin ligase Ufd2, as reported in a crystallographic structure. These complete assignments can be used to study the protein dynamics of the Rad23(UBL) and its interaction of with other ubiquitin receptors or proteasome subunits.

Indexed as

Nuclear Magnetic Resonance, BiomolecularDNA-Binding ProteinsProteasome Endopeptidase ComplexProtein DomainsSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsNMRUbiquitin-like domainUbiquitin–proteasome pathwayUV excision repair protein Rad23

Identifiers

PMID27188292
PMCPMC5042828
OpenAlexW2406291173

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Registered trials

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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.