The interaction of nucleotides with pertussis toxin. Direct evidence for a nucleotide binding site on the toxin regulating the rate of ADP-ribosylation of Ni, the inhibitory regulatory component of adenylyl cyclase.-Reference-Cited by-同舟云学术

The interaction of nucleotides with pertussis toxin. Direct evidence for a nucleotide binding site on the toxin regulating the rate of ADP-ribosylation of Ni, the inhibitory regulatory component of adenylyl cyclase.

Published:1986-08 Issue:24 Volume:261 Page:11173-11179
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mattera R,Codina J,Sekura R D,Birnbaumer L

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Identification of the predominant substrate for ADP-ribosylation by islet activating protein.

2. Pertussis toxin substrate, the putative Ni component of adenylyl cyclases, is an alpha beta heterodimer regulated by guanine nucleotide and magnesium.

3. Identification of a gamma subunit associated with the adenylyl cyclase regulatory proteins Ns and Ni.

4. Stimulation and inhibition of adenylyl cyclases mediated by distinct regulatory proteins

5. Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein.

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