Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase. - Wikidata - awgldk - TriplyDB

Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase.

Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase.

http://www.wikidata.org/entity/Q48034326

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Novel crosstalk to BMP signalling: cGMP-dependent kinase I modulates BMP receptor and Smad activity Scutellarin's Cardiovascular Endothelium Protective Mechanism: Important Role of PKG-Iα Mosquito protein kinase G phosphorylates flavivirus NS5 and alters flight behavior in Aedes aegypti and Anopheles gambiae.Mechanisms associated with cGMP binding and activation of cGMP-dependent protein kinase.Structures of cGMP-Dependent Protein Kinase (PKG) Iα Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.Molecular mechanisms that could contribute to prolonged effectiveness of PDE5 inhibitors to improve erectile function.New nitric oxide donors based on ruthenium complexes.Nitration of tyrosine 247 inhibits protein kinase G-1α activity by attenuating cyclic guanosine monophosphate binding.Phosphorylation events during viral infections provide potential therapeutic targets.West Nile virus methyltransferase domain interacts with protein kinase G.The hinge region operates as a stability switch in cGMP-dependent protein kinase I alpha.Autoinhibition and isoform-specific dominant negative inhibition of the type II cGMP-dependent protein kinase.Functional analysis of type 1alpha cGMP-dependent protein kinase using green fluorescent fusion proteins.NO induces a cGMP-independent release of cytochrome c from mitochondria which precedes caspase 3 activation in insulin producing RINm5F cells.Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their regulation of cyclic AMP response element-dependent gene transcription.A conserved serine juxtaposed to the pseudosubstrate site of type I cGMP-dependent protein kinase contributes strongly to autoinhibition and lower cGMP affinity.cAMP inhibits IP(3)-dependent Ca(2+) release by preferential activation of cGMP-primed PKG.Activation of cGMP-dependent protein kinase by protein kinase C.Probing noncovalent protein-ligand interactions of the cGMP-dependent protein kinase using electrospray ionization time of flight mass spectrometry.A cGMP-dependent protein kinase is implicated in wild-type motility in C. elegans.

P2860

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P2860

Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase.

http://www.wikidata.org/entity/Q48034326

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年学术文章

@wuu

1998年学术文章

@zh

1998年学术文章

@zh-cn

1998年学术文章

@zh-hans

1998年学术文章

@zh-my

1998年学术文章

@zh-sg

1998年學術文章

@yue

1998年學術文章

@zh-hant

name

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@en

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@nl

type

label

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@en

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@nl

prefLabel

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@en

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@nl

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JBC.273.23.14649

P1433

Journal of Biological Chemistry

P1476

Activation by autophosphorylat ...... cGMP-dependent protein kinase.

@en

P2093

Chu DM

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

Corbin JD

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Fosler M

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Francis SH

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Maksymovitch EA

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Thomas JW

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P2860

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

A protein phosphorylation switch at the conserved allosteric site in GP

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases

Autophosphorylation: a salient feature of protein kinases.

Primary structure of the regulatory subunit of type II cAMP-dependent protein kinase from bovine cardiac muscle.

Predicted structures of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites.

cGMP-dependent protein kinase. Autophosphorylation changes the characteristics of binding site 1.

Purification and assay of cAMP, cGMP, and cyclic nucleotide analogs in cells treated with cyclic nucleotide analogs.

Ligand-induced conformational changes in cyclic nucleotide phosphodiesterases and cyclic nucleotide-dependent protein kinases.

P304

14649-14656

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scholarly article

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10.1074/JBC.273.23.14649

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23

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13680200

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9603983

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