Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains.

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Bibliographic Details
Title: Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains.
Authors: Chau AK; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA., Bracken K; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA., Bai L; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA., Pham D; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA., Good LL; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA., Maillard RA; Department of Chemistry, Georgetown University, Washington, District of Columbia, USA. Electronic address: Rodrigo.Maillard@georgetown.edu.
Source: The Journal of biological chemistry [J Biol Chem] 2023 Jun; Vol. 299 (6), pp. 104790. Date of Electronic Publication: 2023 May 06.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Database: MEDLINE Ultimate
Description
ISSN:1083-351X
DOI:10.1016/j.jbc.2023.104790