A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking-Reference-Cited by-同舟云学术

A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking

Published:2015-09-24 Issue:12 Volume:24 Page:1956-1963
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Thompson Jackie A.¹,Nadeau Owen W.¹,Carlson Gerald M.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology; University of Kansas Medical Center; Kansas Kansas 66160

Funder

National Institutes of Health

University of Kansas Medical Center

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference34 articles.

1. Inhibition of the catalytic subunit of phosphorylase kinase by its α/β subunits;Paudel;J Biol Chem,1987

2. The activation of rabbit skeletal muscle phosphorylase kinase requires the binding of 3 Ca2+ per δ subunit;Burger;Biochem Biophys Res Commun,1982

3. The interrelationship between cAMP-dependent α and β subunit phosphorylation in the regulation of phosphorylase kinase activity. Studies using subunit specific phosphatases;Ramachandran;J Biol Chem,1987

4. Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex;Nadeau;J Biol Chem,2012

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The regulation of glycogenolysis in the brain;Journal of Biological Chemistry;2018-05

2. Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex;Protein Science;2017-11-21

3. Activation of Phosphorylase Kinase by Physiological Temperature;Biochemistry;2015-12-14