Evidence map›Paper›PMID 34944465›Full record

ReviewBiomolecules2021

Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.

Carolyn Allain Breckel, Mark Hochstrasser

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

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  16. APC/CmicroPublication biology · 2022
    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.

Carolyn Allain BreckelDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.ORCID 0000-0001-5664-5818
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.ORCID 0000-0002-1131-5484
Yale University · US

Funding

Mechanisms of Cell Regulation and Manipulation by the Ubiquitin SystemR35GM136325 · NIGMS · YALE UNIVERSITY · PI Mark W Hochstrasser · 2020 to 2026
$6.5M
NIGMS NIH HHS R35 GM136325NIH HHS GM136325NIH HHS T32GM7223-43
6 · The paper itself

Abstract

The diverse functions of proteins depend on their proper three-dimensional folding and assembly. Misfolded cellular proteins can potentially harm cells by forming aggregates in their resident compartments that can interfere with vital cellular processes or sequester important factors. Protein quality control (PQC) pathways are responsible for the repair or destruction of these abnormal proteins. Most commonly, the ubiquitin-proteasome system (UPS) is employed to recognize and degrade those proteins that cannot be refolded by molecular chaperones. Misfolded substrates are ubiquitylated by a subset of ubiquitin ligases (also called E3s) that operate in different cellular compartments. Recent research in

Indexed as

Cell NucleusCytoplasmMolecular ChaperonesProtein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitin-Protein LigasesMolecular ChaperonesSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligasesdegronproteasomeprotein degradationprotein quality controlubiquitinubiquitin ligase

Identifiers

PMID34944465
PMCPMC8698790
OpenAlexW4200617527

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.