Characterization of the Phd repressor-antitoxin boundary.
about
Hypothetical functions of toxin-antitoxin systemsThe solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin bindingDoc of Prophage P1 Is Inhibited by Its Antitoxin Partner Phd through Fold ComplementationAn intrinsically disordered entropic switch determines allostery in Phd-Doc regulationNoncognate Mycobacterium tuberculosis toxin-antitoxins can physically and functionally interactPercolation of the phd repressor-operator interface.Genome anatomy of the gastrointestinal pathogen, Vibrio parahaemolyticus of crustacean origin.Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding moduleBacterial addiction module toxin Doc inhibits translation elongation through its association with the 30S ribosomal subunit.Characterization of the phd-doc and ccd toxin-antitoxin cassettes from Vibrio superintegrons.Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Doc toxin is a kinase that inactivates elongation factor TuThe Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-TuCrystallization of Doc and the Phd-Doc toxin-antitoxin complex.
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P2860
Characterization of the Phd repressor-antitoxin boundary.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-my
2005年学术文章
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2005年學術文章
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2005年學術文章
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2005年學術文章
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name
Characterization of the Phd repressor-antitoxin boundary.
@en
type
label
Characterization of the Phd repressor-antitoxin boundary.
@en
prefLabel
Characterization of the Phd repressor-antitoxin boundary.
@en
P2860
P1476
Characterization of the Phd repressor-antitoxin boundary.
@en
P2093
James Estle McKinley
Roy David Magnuson
P2860
P304
P356
10.1128/JB.187.2.765-770.2005
P577
2005-01-01T00:00:00Z