(Q33184868)

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Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the R(I)alpha subunit of protein kinase A.

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Europe PubMed Central

23 July 2017

Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the R(I)alpha subunit of protein kinase A. (English)

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Europe PubMed Central

23 July 2017

author name string

Ganesh S Anand

1

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Europe PubMed Central

23 July 2017

Carrie A Hughes

2

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Europe PubMed Central

23 July 2017

John M Jones

3

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Europe PubMed Central

23 July 2017

Susan S Taylor

4

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Europe PubMed Central

23 July 2017

Elizabeth A Komives

5

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Europe PubMed Central

23 July 2017

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publication date

1 October 2002

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23 July 2017

Journal of Molecular Biology

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23 July 2017

323

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23 July 2017

377-386

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23 July 2017

2

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Europe PubMed Central

23 July 2017

Nobel Lecture. Protein phosphorylation and cellular regulation I.

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Dynamics of cAMP-dependent protein kinase

1 reference

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7 January 2021

Interaction of the regulatory and catalytic subunits of cAMP-dependent protein kinase. Electrostatic sites on the type Ialpha regulatory subunit

1 reference

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7 January 2021

Crosstalk between domains in the regulatory subunit of cAMP-dependent protein kinase: influence of amino terminus on cAMP binding and holoenzyme formation

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7 January 2021

The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium

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7 January 2021

Cyclic nucleotides modulate the release of [3H] adenosine cyclic 3',5'-phosphate bound to the regulatory moiety of protein kinase I by the catalytic subunit of the kinase.

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7 January 2021

Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase

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Comparison of the two classes of binding sites (A and B) of type I and type II cyclic-AMP-dependent protein kinases by using cyclic nucleotide analogs

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Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase

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Dissecting cAMP binding domain A in the RIalpha subunit of cAMP-dependent protein kinase. Distinct subsites for recognition of cAMP and the catalytic subunit

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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7 January 2021

Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with a water-soluble carbodiimide: identification of carboxyl groups protected by MgATP and inhibitor peptides

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7 January 2021

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains

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Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit

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7 January 2021

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

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Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange

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Identification of protein-protein interfaces by decreased amide proton solvent accessibility

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Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB.

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Solvent accessibility of the thrombin-thrombomodulin interface

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Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry

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7 January 2021

Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection

1 reference

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7 January 2021

Identification of electrostatic interaction sites between the regulatory and catalytic subunits of cyclic AMP-dependent protein kinase

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7 January 2021

Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli: multiple isozymes reflect different phosphorylation states.

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Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family

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7 January 2021

Identifiers

10.1016/S0022-2836(02)00919-1

1 reference

Europe PubMed Central

23 July 2017

1 reference

Europe PubMed Central

23 July 2017

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