Evidence map›Paper›PMID 35120648›Full record

ArticleMolecular cell2022

Co-adaptor driven assembly of a CUL3 E3 ligase complex.

David Akopian, Colleen A McGourty, Michael Rapé

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

David AkopianDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA.
Colleen A McGourtyDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA.
Michael RapéDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley CA 94720, USA; Quantitative Biosciences Institute, QB3, University of California at Berkeley, Berkeley CA 94720, USA. Electronic address: mrape@berkeley.edu.
University of California, Berkeley · USQB3 · US

Funding

Targeting the Regulatory Network of Large COPII Vesicle Formation to Treat Extracellular Matrix-Linked DisordersF32GM123716 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI AKOPIAN, DAVID · 2017 to 2018
$118k
NIGMS NIH HHS F32 GM123716
6 · The paper itself

Abstract

Cullin-RING E3 ligases (CRLs) are essential ubiquitylation enzymes that combine a catalytic core built around cullin scaffolds with ∼300 exchangeable substrate adaptors. To ensure robust signal transduction, cells must constantly form new CRLs by pairing substrate-bound adaptors with their cullins, but how this occurs at the right time and place is still poorly understood. Here, we show that formation of individual CRL complexes is a tightly regulated process. Using CUL3

Indexed as

Adaptor Proteins, Signal TransducingCalcium-Binding ProteinsCullin ProteinsHEK293 CellsHumansMannosyltransferasesMembrane ProteinsProtein BindingProtein Interaction Domains and MotifsProtein StabilityUbiquitinationUbiquitin ThiolesteraseAdaptor Proteins, Signal TransducingCalcium-Binding ProteinsCUL3 protein, humanCullin ProteinsKLHL12 protein, humanLNPK protein, humanMannosyltransferasesMembrane ProteinsPEF1 protein, humanUbiquitin ThiolesteraseUSP9X protein, humanadaptor exchangeALG2CAND1CUL3KLHL12monoubiquitylationPEF1SEC31ubiquitin

Identifiers

PMID35120648
PMCPMC8884472
OpenAlexW4210307049

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.