Structure and function of the Ah receptor: Sulfhydryl groups required for binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin to cytosolic receptor from rodent livers-Reference-Cited by-同舟云学术

Structure and function of the Ah receptor: Sulfhydryl groups required for binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin to cytosolic receptor from rodent livers

Published:1987-02 Issue:2 Volume:252 Page:388-395
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Denison Michael S.,Vella Lynn M.,Okey Allan B.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference31 articles.

1. Stereospecific, high affinity binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin by hepatic cytosol. Evidence that the binding species is receptor for induction of aryl hydrocarbon hydroxylase.

2. Regulatory gene product of the Ah locus. Characterization of the cytosolic inducer-receptor complex and evidence for its nuclear translocation.

3. Regulatory gene product of the Ah complex. Comparison of 2,3,7,8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene binding to several moieties in mouse liver cytosol.

4. Binding of 3-Methylcholanthrene and 2,3,7,8-Tetrachlorodibenzo-p-dioxin to a Common Ah Receptor Site in Mouse and Rat Hepatic Cytosols

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