A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
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An Isozyme-specific Redox Switch in Human Brain Glycogen Phosphorylase Modulates Its Allosteric Activation by AMP.A Phosphorylation Switch on Lon Protease Regulates Bacterial Type III Secretion System in Host.Identification of allosteric disulfides from labile bonds in X-ray structures.ROLE OF THIOLS IN OXIDATIVE STRESSMultiple domains of bacterial and human Lon proteases define substrate selectivity
P2860
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
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im November 2014 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 2014
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A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@en
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@nl
type
label
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@en
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@nl
prefLabel
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@en
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@nl
P2093
P2860
P356
P1476
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis
@en
P2093
Hiroshi Kihara
Masaki Kojima
Mikako Shirouzu
Takaho Terada
Tomonari Muramatsu
Wataru Nishii
P2860
P2888
P356
10.1038/NCHEMBIO.1688
P577
2014-11-10T00:00:00Z