Conformational stability and ligand binding properties of BldR, a member of the MarR family, from Sulfolobus solfataricus-Reference-Cited by-同舟云学术

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Conformational stability and ligand binding properties of BldR, a member of the MarR family, from Sulfolobus solfataricus

Published:2014-06 Issue:6 Volume:1844 Page:1167-1172
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Fiorentino Gabriella,Del Giudice Immacolata,Petraccone Luigi,Bartolucci Simonetta,Del Vecchio Pompea

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference32 articles.

1. Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators;Perera;J. Mol. Cell Biol.,2010

2. The X-ray crystal structure of PA1374 from Pseudomonas aeruginosa, a putative oxidative-stress sensing transcriptional regulator;Kim;Biochem. Biophys. Res. Commun.,2013

3. Study of PcaV from Streptomyces coelicolor yields new insights into ligand-responsive MarR family transcription factors;Davis;Nucleic Acids Res.,2013

4. Structural insight on the mechanism of regulation of the MarR family of proteins: high-resolution crystal structure of a transcriptional repressor from Methanobacterium thermoautotrophicum;Saridakis;J. Mol. Biol.,2008

5. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3A resolution;Alekshun;Nat. Struct. Biol.,2001

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3. A physicochemical investigation on the metal binding properties of TtSmtB, a thermophilic member of the ArsR/SmtB transcription factor family;International Journal of Biological Macromolecules;2019-10

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5. Structural analysis of the regulatory mechanism of MarR protein Rv2887 in M. tuberculosis;Scientific Reports;2017-07-25

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