High level expression of full-length estrogen receptor in Escherichia coli is facilitated by the uncoupler of oxidative phosphorylation, CCCP

Journal of Steroid Biochemistry and Molecular Biology

Volumn 74, Issue 4, 2000, Pages 169-178

  Zhang, Cheng Cheng ^a   Glenn, Kevin A ^a   Kuntz, Martin A ^a   Shapiro, David J ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Carbonyl cyanide m chlorophenyl hydrazone (CCCP); Escherichia coli; Human estrogen receptor (hER )

Indexed keywords

ARABINOSE; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; DNA; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; MONOCLONAL ANTIBODY; TIMENTIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ESCHERICHIA COLI; ESTROGEN RESPONSIVE ELEMENT; HORMONE RECEPTOR INTERACTION; IMMUNOAFFINITY CHROMATOGRAPHY; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION;

BASE SEQUENCE; BINDING SITES; CARBONYL CYANIDE M-CHLOROPHENYL HYDRAZONE; DNA; ESCHERICHIA COLI; ESTRADIOL; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PHOSPHORYLATION; PROTEIN ENGINEERING; RECEPTORS, ESTROGEN; RECOMBINANT PROTEINS; RESPONSE ELEMENTS; UNCOUPLING AGENTS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034668718     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(00)00120-5     Document Type: Article

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