The catalytic domain limits the translocation of protein kinase C alpha in response to increases in Ca2+ and diacylglycerol.
about
A spatiotemporally coordinated cascade of protein kinase C activation controls isoform-selective translocation.Ca2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages.Immunogold electron microscopic demonstration of distinct submembranous localization of the activated gammaPKC depending on the stimulation.Conserved modular domains team up to latch-open active protein kinase CαPKCalpha expression is a marker for breast cancer aggressiveness.Insight into intra- and inter-molecular interactions of PKC: design of specific modulators of kinase function.Protein kinase C, focal adhesions and the regulation of cell migration.Human cytomegalovirus pUL37x1-induced calcium flux activates PKCα, inducing altered cell shape and accumulation of cytoplasmic vesicles.Structural optimization of 10-methyl-aplog-1, a simplified analog of debromoaplysiatoxin, as an anticancer lead.Identification of acidic amino acid residues in the protein kinase C alpha V5 domain that contribute to its insensitivity to diacylglycerol.Heterogeneity of cellular proliferation within transitional cell carcinoma: correlation of protein kinase C alpha/betaI expression and activity.The origin of C1A-C2 interdomain interactions in protein kinase Calpha.Identification of conserved amino acids N-terminal of the PKC epsilon C1b domain crucial for protein kinase C epsilon-mediated induction of neurite outgrowth.Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Calpha in response to diacylglycerol.Identification of an amino acid residue in the protein kinase C C1b domain crucial for its localization to the Golgi network.A critical intramolecular interaction for protein kinase Cepsilon translocation.Fluorescence resonance energy transfer imaging of PKC signalling in living cells using genetically encoded fluorescent probes.
P2860
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P2860
The catalytic domain limits the translocation of protein kinase C alpha in response to increases in Ca2+ and diacylglycerol.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@en
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@nl
type
label
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@en
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@nl
prefLabel
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@en
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@nl
P2093
P2860
P356
P1433
P1476
The catalytic domain limits th ...... es in Ca2+ and diacylglycerol.
@en
P2093
Arathi Raghunath
Christer Larsson
P2860
P304
P356
10.1042/BJ20021420
P407
P577
2003-03-01T00:00:00Z