The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding.
about
An intrinsically disordered entropic switch determines allostery in Phd-Doc regulationCrystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate AntitoxinStructural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry.
P2860
The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding.
description
2014 nî lūn-bûn
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name
The intrinsically disordered d ...... e inactivation and misfolding.
@en
The intrinsically disordered d ...... e inactivation and misfolding.
@nl
type
label
The intrinsically disordered d ...... e inactivation and misfolding.
@en
The intrinsically disordered d ...... e inactivation and misfolding.
@nl
prefLabel
The intrinsically disordered d ...... e inactivation and misfolding.
@en
The intrinsically disordered d ...... e inactivation and misfolding.
@nl
P2093
P2860
P356
P1476
The intrinsically disordered d ...... le inactivation and misfolding
@en
P2093
Albert Konijnenberg
Annika Butterer
Ariel Talavera
Henri De Greve
Remy Loris
Sarah Haesaerts
Steven De Gieter
P2860
P304
34013-34023
P356
10.1074/JBC.M114.572396
P407
P577
2014-10-16T00:00:00Z