Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities
about
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.A Phosphorylation Switch on Lon Protease Regulates Bacterial Type III Secretion System in Host.Mitochondrial Lon sequesters and stabilizes p53 in the matrix to restrain apoptosis under oxidative stress via its chaperone activity.
P2860
Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Mutations to a glycine loop in ...... eptidase and ATPase activities
@ast
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en-gb
Mutations to a glycine loop in ...... eptidase and ATPase activities
@nl
type
label
Mutations to a glycine loop in ...... eptidase and ATPase activities
@ast
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en-gb
Mutations to a glycine loop in ...... eptidase and ATPase activities
@nl
prefLabel
Mutations to a glycine loop in ...... eptidase and ATPase activities
@ast
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en-gb
Mutations to a glycine loop in ...... eptidase and ATPase activities
@nl
P2093
P2860
P3181
P356
P1433
P1476
Mutations to a glycine loop in ...... eptidase and ATPase activities
@en
P2093
Eva Kutejová
Gabriela Ondrovičová
Jacob Bauer
Jana Bellová
Nina Kunová
Ľuboš Ambro
P2860
P304
P3181
P356
10.1111/FEBS.12740
P407
P577
2014-03-01T00:00:00Z