Binding-Dependent Disorder−Order Transition in PKIα: A Fluorescence Anisotropy Study-Reference-Cited by-同舟云学术

Binding-Dependent Disorder−Order Transition in PKIα: A Fluorescence Anisotropy Study

Published:1999-05-01 Issue:21 Volume:38 Page:6774-6780
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hauer Jennifer A.¹,Taylor Susan S.¹,Johnson David A.¹

Affiliation:

1. Department of Chemistry and Biochemistry and the Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA, 92093-0654, and Division of Biomedical Sciences, University of California, Riverside, Riverside, CA, 92521-0121

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi983074k

Reference24 articles.

1. DNA-binding characteristics of theEscherichia coliCytR regulator: a relaxed spacing requirement between operator half-sites is provided by a flexible, unstructured interdomain linker

2. Thermostable inhibitor of cAMP-dependent protein kinase enhances the rate of export of the kinase catalytic subunit from the nucleus.

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