Meyer-Roxlau, Stefanie

[["dc.bibliographiccitation.artnumber","17711"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.lastpage","14"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Singh, Simranjit"],["dc.contributor.author","Lämmle, Simon"],["dc.contributor.author","Giese, Heiko"],["dc.contributor.author","Kämmerer, Susanne"],["dc.contributor.author","Meyer-Roxlau, Stefanie"],["dc.contributor.author","Alfar, Ezzaldin Ahmed"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Guan, Kaomei"],["dc.contributor.author","El-Armouche, Ali"],["dc.contributor.author","Richter, Florian"],["dc.date.accessioned","2019-02-27T15:13:04Z"],["dc.date.available","2019-02-27T15:13:04Z"],["dc.date.issued","2018"],["dc.description.abstract","Heart failure is the most common cause of morbidity and hospitalization in the western civilization. Protein phosphatases play a key role in the basal cardiac contractility and in the responses to β-adrenergic stimulation with type-1 phosphatase (PP-1) being major contributor. We propose here that formation of transient disulfide bridges in PP-1α might play a leading role in oxidative stress response. First, we established an optimized workflow, the so-called “cross-over-read” search method, for the identification of disulfide-linked species using permutated databases. By applying this method, we demonstrate the formation of unexpected transient disulfides in PP-1α to shelter against over-oxidation. This protection mechanism strongly depends on the fast response in the presence of reduced glutathione. Our work points out that the dimerization of PP-1α involving Cys39 and Cys127 is presumably important for the protection of PP-1α active surface in the absence of a substrate. We finally give insight into the electron transport from the PP-1α catalytic core to the surface. Our data suggest that the formation of transient disulfides might be a general mechanism of proteins to escape from irreversible cysteine oxidation and to prevent their complete inactivation."],["dc.identifier.doi","10.1038/s41598-018-36267-6"],["dc.identifier.pmid","30531830"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/57651"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/247"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A02: Bedeutung des Phosphatase-Inhibitors-1 für die SR-spezifische Modulation der Beta- adrenozeptor-Signalkaskade"],["dc.relation","SFB 1002 | A05: Molekulares Imaging von kardialen Calcium-Freisetzungsdomänen"],["dc.relation.issn","2045-2322"],["dc.relation.workinggroup","RG El-Armouche"],["dc.relation.workinggroup","RG Guan (Application of patient-specific induced pluripotent stem cells in disease modelling)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The reduced activity of PP-1α under redox stress condition is a consequence of GSH-mediated transient disulfide formation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]