A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1. - Wikidata - awgldk - TriplyDB

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

http://www.wikidata.org/entity/Q39970659

about

PKA: lessons learned after twenty years Assembly of allosteric macromolecular switches: lessons from PKA Design principles underpinning the regulatory diversity of protein kinases Adenosine-binding motif mimicry and cellular effects of a thieno[2,3-d]pyrimidine-based chemical inhibitor of atypical protein kinase C isoenzymes Deciphering the structural basis of eukaryotic protein kinase regulation Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases Protein kinases: evolution of dynamic regulatory proteins Co-conserved features associated with cis regulation of ErbB tyrosine kinases.Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target Dynamic architecture of a protein kinase.Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.Hydrophobic motif phosphorylation is not required for activation loop phosphorylation of p70 ribosomal protein S6 kinase 1 (S6K1).Direct modulation of the protein kinase A catalytic subunit α by growth factor receptor tyrosine kinases.Cotranslational cis-phosphorylation of the COOH-terminal tail is a key priming step in the maturation of cAMP-dependent protein kinase Syk inhibits the activity of protein kinase A by phosphorylating tyrosine 330 of the catalytic subunit Influence of N-myristylation and ligand binding on the flexibility of the catalytic subunit of protein kinase A.Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target On the segregation of protein ionic residues by charge type.Regulation of the interaction between protein kinase C-related protein kinase 2 (PRK2) and its upstream kinase, 3-phosphoinositide-dependent protein kinase 1 (PDK1).Discovery of Allostery in PKA Signaling.

P2860

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P2860

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

http://www.wikidata.org/entity/Q39970659

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@en

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@nl

type

label

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@en

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@nl

prefLabel

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@en

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.

@nl

P1433

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P1433

Protein Science

P1476

A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1

@en

P2093

Craig J Allison

http://www.w3.org/2001/XMLSchema#string

Natarajan Kannan

http://www.w3.org/2001/XMLSchema#string

Robert A Romano

http://www.w3.org/2001/XMLSchema#string

Susan S Taylor

http://www.w3.org/2001/XMLSchema#string

P2860

Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways

Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2

The protein kinase complement of the human genome

Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA

High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.

PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation

PKA Type II Holoenzyme Reveals a Combinatorial Strategy for Isoform Diversity

Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

Contribution of Non-catalytic Core Residues to Activity and Regulation in Protein Kinase A

A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility

P304

1486-1497

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scholarly article

P356

10.1002/PRO.146

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P433

7

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P478

18

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Alexandr P Kornev

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2009-07-01T00:00:00Z

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26295554

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19530248

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phosphorylation

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2775216

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