Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface. (Q42845814)

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scientific article published on March 1997

Language	Label	Description	Also known as
English	Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface.	scientific article published on March 1997

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface. (English)

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

author name string

Herberg FW

1

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Zimmermann B

2

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

McGlone M

3

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Taylor SS

4

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

publication date

1 March 1997

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

6

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

3

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

569-579

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition

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Functional malleability of the carboxyl-terminal tail in protein kinase A.

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Active and inactive protein kinases: structural basis for regulation

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Regulation-defective mutants of type I cAMP-dependent protein kinase. Consequences of replacing arginine 94 and arginine 95.

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Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations

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Three protein kinase structures define a common motif

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Transformation of mammalian cells by constitutively active MAP kinase kinase

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Crystal structure of casein kinase-1, a phosphate-directed protein kinase

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Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase

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Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification

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Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif

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A conserved helix motif complements the protein kinase core

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Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase

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Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase

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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

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cAMP-dependent protein kinase: a framework for a diverse family of enzymes

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A point mutation abolishes binding of cAMP to site A in the regulatory subunit of cAMP-dependent protein kinase.

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Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli.

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

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N-myristylation of the catalytic subunit of cAMP-dependent protein kinase conveys structural stability.

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

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Identifiers

10.1002/PRO.5560060306

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

ResearchGate publication ID

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