ScholarLens Back to search
2020•Free Radical Biology and MedicineRequires access

Cysteine 343 in the substrate binding domain is the primary S-Nitrosylated site in protein disulfide isomerase

Jiro Ogura, Lloyd W. Ruddock, Nariyasu Mano

Open publisher page 12 citations

Abstract

This record does not include an abstract. Use the full-text link above if available.

About this research paper

What this paper is about

An abstract is not available in the OpenAlex record for this paper.

Why it matters

OpenAlex reports 12 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Key concepts: S-Nitrosylation, Protein disulfide-isomerase, Cysteine, Chemistry, Neurodegeneration, Biochemistry, Glutathione, In vitro

Related papers

Related paper 1Related paper 2
Back to paper searchBrowse research topicsOriginal source
Cysteine 343 in the substrate binding domain is the primary S-Nitrosylated site in protein disulfide isomerase — Research Paper | ScholarLens