About: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

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About: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	vědecký článek publikovaný v roce 1995 (cs) artículu científicu espublizáu en 1995 (ast) наукова стаття, опублікована в грудні 1995 (uk) 1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) 1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت في ديسمبر 1995) (ar) vedecký článok (publikovaný 1995/12/01) (sk) wetenschappelijk artikel (gepubliceerd op 1995/12/01) (nl) article scientifique publié en 1995 (fr) im Dezember 1995 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28616082-8BF0B8AE-9AD3-4520-BE55-334E2E12A826
publication date	1995-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28616082-87787B10-31F0-463C-B038-CFF27F5D323B
language of work or name	English
cites work	wds:Q28616082-1F30098A-A6CE-47F5-8561-6AE72F242849 wds:Q28616082-25D70B88-D238-4A8D-8724-4BA41BFEDCB2 wds:Q28616082-4FC25487-5460-4E50-A5E3-2D4EA18A008E wds:Q28616082-63B81CD2-C7E2-4D3B-A20C-8D9395877D7D wds:Q28616082-6B79A540-C514-4C83-A3D4-4768548D02BC wds:Q28616082-6FA73753-7AA1-4A09-B2B7-DB0E09BF4A8F wds:Q28616082-746D7643-AB76-4D47-8C6B-4D7A5C32BCD9 wds:Q28616082-763B5E46-DE9B-4FD2-AEF9-FCDF646715E0 wds:Q28616082-7D7E9EF3-EDB2-4E6F-BE2F-AA59CCD79624 wds:Q28616082-800F5FBD-84F8-4842-A3FE-35FA1D1B6433 wds:Q28616082-8A16D427-99FA-43F3-BADE-B4A270590D5E wds:Q28616082-8B3E9A2D-104B-4F45-B7E1-74EE0D64FDBF wds:Q28616082-A0334AF1-DD3E-47E8-B017-DC79EE8089E9 wds:Q28616082-AE9DF72D-3D05-4801-9C89-9300279BB6E8 wds:Q28616082-B6EC6FE1-457F-4B52-A49B-CD232E5E7572 wds:Q28616082-DCD23FB0-3E71-4B5E-A139-9CC8D5F92776 wds:Q28616082-DFD4016F-71AB-469C-A836-F42730552831 wds:Q28616082-E985F01A-0744-419C-A4B0-FC995ED684CF
cites work	Examination of automated polypeptide sequencing using standard phenyl isothiocyanate reagent and subpicomole high-performance liquid chromatographic analysis The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain. Internal protein sequence analysis: enzymatic digestion for less than 10 micrograms of protein bound to polyvinylidene difluoride or nitrocellulose membranes Protein kinase C: structure, function, and regulation Atomic structure of the MAP kinase ERK2 at 2.3 A resolution Crystal structure of the tyrosine kinase domain of the human insulin receptor Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase Threonine-497 is a critical site for permissive activation of protein kinase C alpha Determination of in vivo phosphorylation sites in protein kinase C Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart Isolation and characterization of two new drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells. Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing. Three protein kinase structures define a common motif Rhodopsin kinase autophosphorylation. Characterization of site-specific mutations Autophosphorylation of protein kinase C at three separated regions of its primary sequence Crystal structure of cyclin-dependent kinase 2 Protein kinase C association with the retinal cytoskeleton and phosphorylation of vimentin
author name string	wds:Q28616082-9132A7B6-D57C-40D9-98EA-2CAA85DCDBFA wds:Q28616082-B59766D1-2A99-49AB-B177-9F369DCDF3AB wds:Q28616082-C55B2AF0-E267-4764-9623-967D80C58F15
OpenCitations bibliographic resource ID	wds:Q28616082-86756A58-B8B3-40FC-B1F3-88AABCCF3884
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4792953
author name string	A. C. Newton E. M. Dutil L. M. Keranen
OpenCitations bibliographic resource ID	4792953
rdfs:label	Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (en) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (nl) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (ast)
skos:prefLabel	Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (en) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (nl) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (ast)
name	Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (en) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (nl) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (ast)
title	wds:Q28616082-39B7DEF2-0FC9-4DD7-9FF5-AA6AD483A6F3
title	Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (en)
page(s)	wds:Q28616082-56FCE558-E25A-47A8-A944-D704E22CCFA9
page(s)	1394–1403
instance of	wds:Q28616082-51918C97-EFB3-4A08-9C64-8B3AE9D5794D
instance of	scholarly article
main subject	wds:Q28616082-B7E65205-DDAA-42A7-9818-288A7E94F8D3
main subject	phosphorylation
PubMed ID	wds:Q28616082-9EADDB1A-416A-4EE4-BF3F-F5A617985487
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8749392
PubMed ID	8749392
published in	wds:Q28616082-5D858D95-ADA8-4B39-8B0E-42647B1B64FA
published in	Current Biology
issue	wds:Q28616082-821A7F53-810D-4C27-8099-6BAF24F8750A
volume	wds:Q28616082-91170619-CAF9-45BD-B81B-54B9B8B380EC
issue	12
volume	5
DOI	wds:Q28616082-8261D252-D2C0-47B5-B668-EDBCFC1D3052
DOI	http://dx.doi.org/10.1016/S0960-9822(95)00277-6
DOI	10.1016/S0960-9822(95)00277-6
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28616082
is cites work of	PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and β-catenin Mammalian TOR controls one of two kinase pathways acting upon nPKCdelta and nPKCepsilon Protein kinase C activation and its pharmacological inhibition in vascular disease The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation Peptidyl-prolyl isomerase Pin1 controls down-regulation of conventional protein kinase C isozymes The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1. Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha. The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase Up-regulation of anti-apoptotic genes confers resistance to the novel anti-leukaemic compound PEP005 in primary AML cells

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