Evidence map›Paper›PMID 42681370›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Assays of Thiol Isomerase Activity.

Roelof H Bekendam, Osamede C Owegie, Moua Yang, Robert Flaumenhaft

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. 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

4 authors.

Roelof H BekendamDivision of Hemostasis and Thrombosis, Department of Medicine, BIDMC, Harvard Medical School, Boston, MA, USA.
Osamede C OwegieBloodworks Northwest Research Institute, Seattle, WA, 98102, USA.
Moua YangBloodworks Northwest Research Institute, Seattle, WA, 98102, USA.
Robert FlaumenhaftDivision of Hemostasis and Thrombosis, Department of Medicine, BIDMC, Harvard Medical School, Boston, MA, USA. rflaumen@bidmc.harvard.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thiol isomerases are oxidoreductases that mediate disulfide bond formation in nascent proteins of the endoplasmic reticulum to ensure their structural integrity. In addition to its role in protein folding, thiol isomerases can modify allosteric disulfide bonds in both intracellular and extracellular proteins, thereby controlling protein function. The process of disulfide bond formation and cleavage is strictly regulated and responsive to redox conditions. Understanding disulfide bond regulation under different redox environments is critical to understanding physiological and pathological processes related to disulfide bond chemistry. Here, we describe protocols for the measurement of disulfide bond modulation by thiol isomerases. These assays include reductase, oxidase, denitrosylase, and sulfenylation assays. These methods can be applied to study recombinant thiol isomerases and thiol isomerases in cellular settings.

Indexed as

Enzyme AssaysProtein Disulfide-IsomerasesDisulfidesHumansOxidation-ReductionProtein FoldingDisulfidesProtein Disulfide-IsomerasesDenitrosylation assayDi-eosin-GSSG assayDisulfide bond formationInsulin turbidimetric assayOxidative refolding assayProtein disulfide isomerase (PDI)Sulfenylation assayThiol isomerase

Identifiers

PMID42681370

What OpenQuestion holds

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Registered trials

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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.