Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif.
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A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoringCrystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific InteractionsTarget highlights in CASP9: Experimental target structures for the critical assessment of techniques for protein structure predictioncGMP-dependent protein kinase I interacts with TRIM39R, a novel Rpp21 domain-containing TRIM protein.cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action.cGMP-dependent protein kinase Iβ interacts with p44/WDR77 to regulate androgen receptor-driven gene expression.The amino terminus of cGMP-dependent protein kinase Iβ increases the dynamics of the protein's cGMP-binding pocketsFunctional osteoclast attachment requires inositol-1,4,5-trisphosphate receptor-associated cGMP-dependent kinase substrate.Huntingtin-associated protein 1 (HAP1) is a cGMP-dependent kinase anchoring protein (GKAP) specific for the cGMP-dependent protein kinase Iβ isoform.The Golgi apparatus regulates cGMP-dependent protein kinase I compartmentation and proteolysis.cGMP-dependent protein kinase anchoring by IRAG regulates its nuclear translocation and transcriptional activityStructures of cGMP-Dependent Protein Kinase (PKG) Iα Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.cGMP-dependent protein kinase Iβ regulates breast cancer cell migration and invasion via interaction with the actin/myosin-associated protein caldesmon.Pathophysiology of TFII-I: Old Guard Wearing New Hats.Inositol 1,4,5-triphosphate-associated cGMP kinase substrate: Basis Sequence: Mouse.IRAG determines nitric oxide- and atrial natriuretic peptide-mediated smooth muscle relaxation.An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation.
P2860
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P2860
Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
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name
Identification of the interfac ...... ls a common interaction motif.
@ast
Identification of the interfac ...... ls a common interaction motif.
@en
Identification of the interfac ...... ls a common interaction motif.
@nl
type
label
Identification of the interfac ...... ls a common interaction motif.
@ast
Identification of the interfac ...... ls a common interaction motif.
@en
Identification of the interfac ...... ls a common interaction motif.
@nl
prefLabel
Identification of the interfac ...... ls a common interaction motif.
@ast
Identification of the interfac ...... ls a common interaction motif.
@en
Identification of the interfac ...... ls a common interaction motif.
@nl
P2093
P2860
P356
P1476
Identification of the interfac ...... ls a common interaction motif.
@en
P2093
Darren E Casteel
Gerry R Boss
Renate B Pilz
P2860
P304
38211-38218
P356
10.1074/JBC.M507021200
P407
P577
2005-09-15T00:00:00Z