Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Davey B. Parekh"'
Autor:
C P Downes, Davey B. Parekh, N R Leslie, Mike Waterfield, Peter J. Parker, Roy Katso, Katarzyna J. Procyk
Publikováno v:
Biochemical Journal. 352:425-433
Phosphorylation of protein kinase C (PKC) provides an amplitude control that operates in conjunction with allosteric effectors. Under many conditions, PKC isotypes appear to be highly phosphorylated; however, the cellular inputs that maintain these p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36d8d139094039ed1600ad75e213acf5
https://doi.org/10.1042/bj3520425
https://doi.org/10.1042/bj3520425
Publikováno v:
The EMBO Journal. 19:496-503
The protein kinase C (PKC) family of signal transducers are characterized by a dependence upon lipids for activity. Specifically, the classical (cPKCα, β and γ) and novel (nPKCδ, ϵ, η and θ) PKC isotypes display a physiological requirement for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b75ba11558f2a6fc40bf4f2592acea1
https://doi.org/10.1093/emboj/19.4.496
https://doi.org/10.1093/emboj/19.4.496
Publikováno v:
Journal of Biological Chemistry. 274:34758-34764
There are three conserved phosphorylation sites in protein kinase C (PKC) isotypes that have been termed priming sites and play an important role in PKC function. The requirements and pathways involved in novel (nPKC) phosphorylation have been invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01365d7ff144dd23de11bfd2591e7ca9
https://doi.org/10.1074/jbc.274.49.34758
https://doi.org/10.1074/jbc.274.49.34758
Autor:
Davey B. Parekh, J.J. Kelly, M. Frech, Richard D. H. Whelan, J.A. Le Good, Brian A. Hemmings, Wolfgang H. Ziegler, Peter J. Parker
Publikováno v:
Current biology : CB. 9(10)
The protein kinase C (PKC) family has been implicated in the control of many cellular functions. Although PKC isotypes are characterized by their allosteric activation, phosphorylation also plays a key role in controlling activity. In classical PKC i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e0606db286973d9dfe6402cb7468282
https://pubmed.ncbi.nlm.nih.gov/10339425
https://pubmed.ncbi.nlm.nih.gov/10339425
Autor:
Davey B. Parekh, J. Ann Le Good, Wolfgang H. Ziegler, Dario R. Alessi, Philip Cohen, Peter J. Parker
Publikováno v:
Science (New York, N.Y.). 281(5385)
Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f9a86399188055d320dbabe81876aa4
https://pubmed.ncbi.nlm.nih.gov/9748166
https://pubmed.ncbi.nlm.nih.gov/9748166