Proteomics

Dataset Information

0

Nitric oxide synthase-dependent SNOome identification


ABSTRACT: This study aimed to identify proteins whose S-nitrosylation is mediated by each of the three human NOS isoforms.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Divya Seth  

LAB HEAD: Jonathan Stamler

PROVIDER: PXD040633 | Pride | 2023-06-01

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
F003630.dat Other
F003630.mgf Mgf
F003630.mzid.gz Mzid
F003630.raw Raw
F003631.dat Other
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Publications

Comparison of the Nitric Oxide Synthase Interactomes and S-Nitroso-Proteomes: Furthering the Case for Enzymatic S-Nitrosylation.

Seth Divya D   Stomberski Colin T CT   McLaughlin Precious J PJ   Premont Richard T RT   Lundberg Kathleen K   Stamler Jonathan S JS  

Antioxidants & redox signaling 20230601 10-12


<b><i>Aims:</i></b> S-nitrosylation of proteins is the main mechanism through which nitric oxide (NO) regulates cellular function and likely represents the archetype redox-based signaling system across aerobic and anaerobic organisms. How NO generated by different nitric oxide synthase (NOS) isoforms leads to specificity of S-nitrosylation remains incompletely understood. This study aimed to identify proteins interacting with, and whose S-nitrosylation is mediated by, human NOS isoforms in the s  ...[more]

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