The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity

The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity

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http://www.wikidata.org/entity/Q27652230
Design principles underpinning the regulatory diversity of protein kinasesComputational insights for the discovery of non-ATP competitive inhibitors of MAP kinasesMeasuring the constitutive activation of c-Jun N-terminal kinase isoformsUnderstanding the specificity of a docking interaction between JNK1 and the scaffolding protein JIP1.Anthrapyrazolone analogues intercept inflammatory JNK signals to moderate endotoxin induced septic shock.The tobacco smoke component, acrolein, suppresses innate macrophage responses by direct alkylation of c-Jun N-terminal kinase.The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteinsAnalysis of conditions affecting auto-phosphorylation of human kinases during expression in bacteria.Constitutive activity of JNK2 alpha2 is dependent on a unique mechanism of MAPK activation.Flexibility in the inducer binding region is crucial for allostery in the Escherichia coli lactose repressor.JNK: a stress-activated protein kinase therapeutic strategies and involvement in Alzheimer's and various neurodegenerative abnormalities.c-Jun N-terminal kinases in memory and synaptic plasticity.JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1.Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts.GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.cis-Tetrachlorido-bis(indazole)osmium(iv) and its osmium(iii) analogues: paving the way towards the cis-isomer of the ruthenium anticancer drugs KP1019 and/or NKP1339.
P2860

The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity

Item
http://www.wikidata.org/entity/Q27652230
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2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The crystal structure of JNK2 ...... gulation of catalytic activity
@ast
The crystal structure of JNK2 ...... gulation of catalytic activity
@en
The crystal structure of JNK2 ...... gulation of catalytic activity
@nl
type
label
The crystal structure of JNK2 ...... gulation of catalytic activity
@ast
The crystal structure of JNK2 ...... gulation of catalytic activity
@en
The crystal structure of JNK2 ...... gulation of catalytic activity
@nl
prefLabel
The crystal structure of JNK2 ...... gulation of catalytic activity
@ast
The crystal structure of JNK2 ...... gulation of catalytic activity
@en
The crystal structure of JNK2 ...... gulation of catalytic activity
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P356
P1433
P1476
The crystal structure of JNK2 ...... gulation of catalytic activity
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921