Evidence map›Paper›PMID 39419747›Full record

ArticleTrends in biochemical sciences2024

Anything you can do, glycans do better: deglycosylation and noncanonical ubiquitination vie to rule the proteasome.

Nicolas Lehrbach

Abstract read
In one paragraph

Article in Trends in biochemical sciences, 2024. 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

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

1 author.

Nicolas LehrbachBasic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA, USA. Electronic address: nlehrbach@fredhutch.org.

Funding

Regulation of Proteasome CapacityR35GM142728 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI LEHRBACH, NICOLAS JOHN · 2021 to 2025
$2.3M
NIGMS NIH HHS R35 GM142728
6 · The paper itself

Abstract

The Nrf1/Nfe2L1 transcription factor is a master regulator of proteasome biogenesis. New work by Yoshida and colleagues reveals a surprising mechanism by which ubiquitination of N-glycosylated Nrf1 controls its function.

Indexed as

PolysaccharidesProteasome Endopeptidase ComplexUbiquitinationAnimalsGlycosylationHumansNuclear Respiratory Factor 1Nuclear Respiratory Factor 1PolysaccharidesProteasome Endopeptidase ComplexFBS2/FBXO6NGLY1N-glycosylationNrf1proteasomeubiquitin

Identifiers

PMID39419747
PMCPMC11624994

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.