Vibrio cholerae H‐NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H‐NS family members (Q79293752)

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scientific article published on 01 October 2003

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English	Vibrio cholerae H‐NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H‐NS family members	scientific article published on 01 October 2003

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21 December 2019

Vibrio cholerae H-NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H-NS family members (English)

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21 December 2019

Vibrio cholerae H‐NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H‐NS family members (English)

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10.1046/J.1365-2958.2003.03701.X

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Vibrio cholerae

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bacterial gene expression regulation

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Melinda B. Nye

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Ronald K. Taylor

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1 October 2003

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21 December 2019

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Molecular Microbiology

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21 December 2019

The histone-like protein H-NS acts as a transcriptional repressor for expression of the anaerobic and growth phase activator AppY of Escherichia coli

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The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA.

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Organization of tcp, acf, and toxT genes within a ToxT-dependent operon

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Multimeric Self-assembly Equilibria Involving the Histone-like Protein H-NS: A THERMODYNAMIC STUDY

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A branch in the ToxR regulatory cascade of Vibrio cholerae revealed by characterization of toxT mutant strains

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Single amino acid substitutions in the N-terminus of Vibrio cholerae TcpA affect colonization, autoagglutination, and serum resistance.

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H-NS is a repressor of the Proteus mirabilis urease transcriptional activator gene ureR

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H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein

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Mechanism of ToxT-dependent transcriptional activation at the Vibrio cholerae tcpA promoter

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The positive regulator CfaD overcomes the repression mediated by histone-like protein H-NS (H1) in the CFA/I fimbrial operon of Escherichia coli

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10.1046/J.1365-2958.2003.03701.X

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14617169%20AND%20SRC:MED&resulttype=core&format=json

21 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14617169%20AND%20SRC:MED&resulttype=core&format=json

21 December 2019

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