Evidence map›Paper›PMID 35963751›Full record

ArticleTrends in biochemical sciences2022

DUB-le vision: snapshots of the proteasome during substrate processing.

Helena M Schnell, John Hanna

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

Article in Trends in biochemical sciences, 2022. 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
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Helena M SchnellDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA.
John HannaDepartment of Pathology, Harvard Medical School and Brigham and Women's Hospital, Boston, MA, USA. Electronic address: jwhanna@bwh.harvard.edu.
Brigham and Women's Hospital · US

Funding

Structural and Functional Analysis of Proteasome Core Particle BiogenesisR01GM144367 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2022 to 2025
$1.6M
Role of very long chain fatty acids in protein quality control and membrane homeostasisR01GM135337 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2020 to 2023
$1.6M
NIGMS NIH HHS R01 GM135337NIGMS NIH HHS R01 GM144367
6 · The paper itself

Abstract

Covalent modification by the small protein ubiquitin can target proteins for destruction by the proteasome, but the ubiquitin signal itself is recycled. Surprisingly, proteasomes contain three different deubiquitinating enzymes (DUBs). Recent work by Zhang and Zou et al. reveals how one of these enzymes, Usp14, regulates, and is regulated by, the proteasome.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinDeubiquitinating EnzymesDeubiquitinating EnzymesProteasome Endopeptidase ComplexUbiquitinproteasomeRpn11ubiquitinUbp6Usp14

Identifiers

PMID35963751
PMCPMC10879984
OpenAlexW4291397339

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.