Evidence map›Paper›PMID 38836811›Full record

ArticleThe Journal of cell biology2024

The HERCulean task of recognizing, ubiquitinating, and shielding misfolded integral membrane proteins.

Christopher J Guerriero, Jeffrey L Brodsky

Abstract readComment
In one paragraph

Article in The Journal of cell biology, 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

5 · Who and what money

Authors and funding

2 authors.

Christopher J GuerrieroDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.ORCID 0000-0002-1046-2300
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.ORCID 0000-0002-6984-8486

Funding

Modulating Hsp70-dependent proteostasis in Alzheimer's DiseaseR35GM131732 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JEFFREY L. BRODSKY · 2019 to 2026
$3.4M
Developing a new platform to characterize and treat disease-associated polycystin variantsR21DK137149 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GUERRIERO, CHRISTOPHER JAMES · 2023 to 2023
$199k
NIDDK NIH HHS R21 DK137149NIGMS NIH HHS R35 GM131732
6 · The paper itself

Abstract

During ER-associated decay, unfolded membrane-resident proteins are targeted for removal and degradation by ubiquitin ligases whose identities and precise operations remain unclear. In this issue, Guerriero and Brodsky discuss new results from Kamada et al. (https://doi.org/10.1083/jcb.202308003) showing the clearance of misfolded CFTR by the E3 ligase HERC3.

Indexed as

Cystic Fibrosis Transmembrane Conductance RegulatorMembrane ProteinsUbiquitinationEndoplasmic ReticulumHumansProtein FoldingUbiquitin-Protein LigasesCystic Fibrosis Transmembrane Conductance RegulatorMembrane ProteinsUbiquitin-Protein Ligases

Identifiers

PMID38836811
PMCPMC11153772

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.