Evidence map›Paper›PMID 35084835›Full record

ArticleChemical research in toxicology2022

Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis.

Benjamin J Freije, Wilson M Freije, To Uyen Do, Grace E Adkins, Alexander Bruch, Jennifer E Hurtig, Kevin A Morano, Raffael Schaffrath, James D West

Open access · greenAbstract read
In one paragraph

Article in Chemical research in toxicology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. 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

9 authors at 3 institutions in 2 countries.

Benjamin J FreijeBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.
Wilson M FreijeBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.
To Uyen DoBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.
Grace E AdkinsBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.
Alexander BruchFachgebiet Mikrobiologie, Institut für Biologie, Universität Kassel, Kassel 34132, Germany.
Jennifer E HurtigBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.
Kevin A MoranoDepartment of Microbiology & Molecular Genetics, McGovern Medical School, University of Texas at Houston, Houston, Texas 77030, United States.
Raffael SchaffrathFachgebiet Mikrobiologie, Institut für Biologie, Universität Kassel, Kassel 34132, Germany.ORCID 0000-0001-9484-5247
James D WestBiochemistry & Molecular Biology Program, Departments of Biology and Chemistry, The College of Wooster, Wooster, Ohio 44691, United States.ORCID 0000-0003-0892-5254
College of Wooster · USUniversity of Kassel · DEThe University of Texas Health Science Center at Houston · US

Funding

Mechanisms of cytosolic proteostasis in yeastR01GM127287 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MORANO, KEVIN ANTHONY · 2018 to 2021
$1.4M
NIGMS NIH HHS R01 GM127287
6 · The paper itself

Abstract

Protein disulfide isomerases (PDIs) function in forming the correct disulfide bonds in client proteins, thereby aiding the folding of proteins that enter the secretory pathway. Recently, several PDIs have been identified as targets of organic electrophiles, yet the client proteins of specific PDIs remain largely undefined. Here, we report that PDIs expressed in

Indexed as

Cross-Linking ReagentsEndoplasmic ReticulumMolecular StructureProtein Disulfide-IsomerasesProteolysisProteostasisSaccharomyces cerevisiaeSulfhydryl CompoundsSulfonesCross-Linking Reagentsdivinyl sulfoneProtein Disulfide-IsomerasesSulfhydryl CompoundsSulfones

Identifiers

PMID35084835
PMCPMC8860869
OpenAlexW4210803742

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.