Allosteric Communication between cAMP Binding Sites in the RI Subunit of Protein Kinase A Revealed by NMR-Reference-Cited by-同舟云学术

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Allosteric Communication between cAMP Binding Sites in the RI Subunit of Protein Kinase A Revealed by NMR

Published:2010-04 Issue:18 Volume:285 Page:14062-14070
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Byeon In-Ja L.,Dao Khanh K.,Jung Jinwon,Keen Jeffrey,Leiros Ingar,Døskeland Stein O.,Martinez Aurora,Gronenborn Angela M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Cyclic nucleotide research — still expanding after half a century

2. Dynamics of signaling by PKA

3. The rate of recombination of the subunits (RI and C) of cAMP-dependent protein kinase depends on whether one or two cAMP molecules are bound per RI monomer.

4. PKA-I Holoenzyme Structure Reveals a Mechanism for cAMP-Dependent Activation

5. Reversible autophosphorylation of a cyclic 3':5'-AMP-dependent protein kinase from bovine cardiac muscle.

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1. Simulations of a PKA RIα homodimer reveal cAMP-coupled conformational dynamics of each protomer and the dimer interface with functional implications;Physical Chemistry Chemical Physics;2024

2. Adenylate control in cAMP signaling: implications for adaptation in signalosomes;Biochemical Journal;2020-08-21

3. Tuning the “violin” of protein kinases: The role of dynamics‐based allostery;IUBMB Life;2019-05-07

4. Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation;Journal of Molecular Biology;2018-08

5. An N-terminally truncated form of cyclic GMP–dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation;Journal of Biological Chemistry;2018-05

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