Proteomics

Dataset Information

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Protein S-sulfenylation Arabidopsis - AtMAPK4


ABSTRACT: Study the oxidation-sensitivity of recombinant AtMAPK4 by treatment with 0 mM hydrogen peroxide (H2O2) (sample '_01'), 1 mM (sample '_02'), and 10 mM (sample '_03'). Each sample subdivided for trypsin and chymotrypsin digestion.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Patrick Willems  

LAB HEAD: Joris Messens

PROVIDER: PXD013588 | Pride | 2019-09-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
EOS438_chymo_01.mgf Mgf
EOS438_chymo_01.raw Raw
EOS438_chymo_01.xlsx Xlsx
EOS438_chymo_01_PSM.xlsx Xlsx
EOS438_chymo_02.mgf Mgf
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Publications

Mining for protein S-sulfenylation in <i>Arabidopsis</i> uncovers redox-sensitive sites.

Huang Jingjing J   Willems Patrick P   Wei Bo B   Tian Caiping C   Ferreira Renan B RB   Bodra Nandita N   Martínez Gache Santiago Agustín SA   Wahni Khadija K   Liu Keke K   Vertommen Didier D   Gevaert Kris K   Carroll Kate S KS   Van Montagu Marc M   Yang Jing J   Van Breusegem Frank F   Messens Joris J  

Proceedings of the National Academy of Sciences of the United States of America 20191002 42


Hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) is an important messenger molecule for diverse cellular processes. H<sub>2</sub>O<sub>2</sub> oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we  ...[more]

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