Protein kinase resource: an integrated environment for phosphorylation research.
about
On the origins of enzyme inhibitor selectivity and promiscuity: a case study of protein kinase binding to staurosporineKinomer v. 1.0: a database of systematically classified eukaryotic protein kinasesEvolutionary paths of the cAMP-dependent protein kinase (PKA) catalytic subunitsInsights into protein kinase regulation and inhibition by large scale structural comparisonThe energy landscape analysis of cancer mutations in protein kinasesAn analysis of expression patterns of genes encoding proteins with catalytic activitiesSequence and structure signatures of cancer mutation hotspots in protein kinasesClassification of protein kinases on the basis of both kinase and non-kinase regionsNovel molecular imaging platform for monitoring oncological kinases.ProKinO: an ontology for integrative analysis of protein kinases in cancer.A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life.Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation.Soybean kinome: functional classification and gene expression patternsAntimalarial drug discovery: targeting protein kinases.Congenital disease SNPs target lineage specific structural elements in protein kinasesReconstitution of modular PDK1 functions on trans-splicing of the regulatory PH and catalytic kinase domainsAn Atlas of the Human Kinome Reveals the Mutational Landscape Underlying Dysregulated Phosphorylation Cascades in Cancer.The PP2C Alphabet is a negative regulator of stress-activated protein kinase signaling in Drosophila.EKPD: a hierarchical database of eukaryotic protein kinases and protein phosphatases.Cyclin-dependent kinase inhibitors: a survey of recent patent literature.PhosphoPOINT: a comprehensive human kinase interactome and phospho-protein database.The proteome and phosphoproteome of maize pollen uncovers fertility candidate proteins.Signaling the signal, cyclic AMP-dependent protein kinase inhibition by insulin-formed H2O2 and reactivation by thioredoxin.
P2860
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P2860
Protein kinase resource: an integrated environment for phosphorylation research.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Protein kinase resource: an integrated environment for phosphorylation research.
@en
Protein kinase resource: an integrated environment for phosphorylation research.
@nl
type
label
Protein kinase resource: an integrated environment for phosphorylation research.
@en
Protein kinase resource: an integrated environment for phosphorylation research.
@nl
prefLabel
Protein kinase resource: an integrated environment for phosphorylation research.
@en
Protein kinase resource: an integrated environment for phosphorylation research.
@nl
P2093
P356
P1433
P1476
Protein kinase resource: an integrated environment for phosphorylation research.
@en
P2093
Ashton Taylor
Michael Gribskov
Nina M Haste
Oleksandr V Buzko
Roland H Niedner
Susan S Taylor
P356
10.1002/PROT.20825
P407
P577
2006-04-01T00:00:00Z