About: The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation

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About: The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	artículu científicu espublizáu en 1999 (ast) vědecký článek publikovaný v roce 1999 (cs) 1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 1999/07/15) (sk) наукова стаття, опублікована в липні 1999 (uk) مقالة علمية (نشرت في 15-7-1999) (ar) 1999 թվականի հուլիսին հրատարակված գիտական հոդված (hy) article scientifique publié en 1999 (fr) scientific journal article (en) im Juli 1999 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1999/07/15) (nl)
publication date	wds:Q28646394-359043EC-95DA-4CC5-A4E4-967B420EC2DE
publication date	1999-07-15 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28646394-A99A326B-2546-4700-8C2A-DB5C69DED491
language of work or name	English
cites work	wds:Q28646394-07302281-70B7-400F-86BA-CBB9BA746C4C wds:Q28646394-12FF4D17-4A29-4D1B-ABDD-88AC311ECF76 wds:Q28646394-223DEEDA-8BCF-4E3D-8D80-5AF6354359CA wds:Q28646394-2C587452-0AC2-4DAA-BE27-E4C7ADF65BBF wds:Q28646394-315F7B86-80BE-4876-9BBE-E311229123A9 wds:Q28646394-3712A6F8-2708-4ABC-B8EE-4A86ABF188EB wds:Q28646394-3755B0EB-604E-4AC3-A4DC-325D2483542E wds:Q28646394-469B4658-F142-4AB6-BDFF-2FACACC61B50 wds:Q28646394-5A672293-3696-494E-93E2-BF0A3BB2901A wds:Q28646394-5AB8E2A0-5B7A-4DA1-ABBA-AF4CF8E9AAB2 wds:Q28646394-7094D4DA-96A9-4068-9B8D-742FBE5E3F0C wds:Q28646394-7828FF73-C830-4AAC-97F9-4C19F2FFCE5B wds:Q28646394-8103D5C0-9C98-42EF-8C97-F2B349F63B82 wds:Q28646394-85136BFA-C32B-4D0C-B7CE-1FBDBFB50860 wds:Q28646394-86B4B3C4-1AB8-4397-B955-0C273F050045 wds:Q28646394-9CD72D62-27F6-4D01-99F6-148526303D07 wds:Q28646394-9D55B641-FCD5-4C33-B930-FF0771423E87 wds:Q28646394-9F40BC4F-7D3F-4664-9FD2-393A47036FDD wds:Q28646394-A06C6E6D-1E3E-4D2E-9A7E-884DBCF794F5 wds:Q28646394-B98D6965-EA58-4DEA-B65D-B4269E18BE43 wds:Q28646394-CE60B19F-7BA0-46CF-8BB5-F282920E749B wds:Q28646394-DAE1643B-20B8-4BD2-BC50-1489FC549380 wds:Q28646394-DF6C3C26-CEA7-4106-922D-131B7DB01828 wds:Q28646394-DFEE504F-7568-40C5-AE55-CA6AB206BAA4 wds:Q28646394-E6D8DD62-DD8F-411D-957D-890B257ADF46 wds:Q28646394-E9286550-70CD-4E3D-99E4-D2F76B3F67F4 wds:Q28646394-F67A0EBD-A829-4B73-B840-2B2CE6B26711 wds:Q28646394-FA192063-0844-4BEC-9438-270DA72E96E3 wds:Q28646394-FCA3ADB1-7EF4-4EBB-9BE1-7293B3BDFD00
cites work	Cloning and expression of multiple protein kinase C cDNAs Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C betaII. A conserved helix motif complements the protein kinase core The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain. Autophosphorylation: a salient feature of protein kinases Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C Active and inactive protein kinases: structural basis for regulation Mitogen-activated protein kinase pathways Protein kinase C is regulated in vivo by three functionally distinct phosphorylations Regulation of protein kinase C. Regulation of the p70 S6 kinase by phosphorylation in vivo. Analysis using site-specific anti-phosphopeptide antibodies. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Mechanisms and consequences of activation of protein kinase B/Akt Regulation of protein kinase C zeta by PI 3-kinase and PDK-1 Protein kinase C and lipid signaling for sustained cellular responses Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1 Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1) Threonine-497 is a critical site for permissive activation of protein kinase C alpha Determination of in vivo phosphorylation sites in protein kinase C The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate Autophosphorylation of protein kinase C at three separated regions of its primary sequence Protected-Site Phosphorylation of Protein Kinase C in Hippocampal Long-Term Potentiation Contributions to maxima in protein kinase C activation Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag. Networking with protein kinases. Ca2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation
author name string	wds:Q28646394-0B970000-6BC5-40AF-9E12-11E3D3F95896 wds:Q28646394-67A35668-A647-421A-8F20-0A5E05E0C01F
author name string	A. C. Newton A. Behn-Krappa
rdfs:label	The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (en) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (nl) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (ast)
skos:prefLabel	The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (en) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (nl) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (ast)
name	The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (en) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (nl) The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (ast)
title	wds:Q28646394-90C72B6C-2DE4-4059-AF27-C77795C5058E
title	The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation (en)
page(s)	wds:Q28646394-6531993A-A047-4777-9829-6C922359206D
page(s)	728–737
instance of	wds:Q28646394-5614191C-CF1C-4A9B-911C-67C93FF1D7B4
instance of	scholarly article
main subject	wds:Q28646394-C27E5912-303B-47B4-B3A6-E48B5A95E957 wds:Q28646394-C36F7E42-1E6B-40B9-8674-4CDA75D181B4
main subject	hydrophobicity phosphorylation
PubMed ID	wds:Q28646394-919752F2-9D95-4E45-81C9-C61677472B58
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10421574
PubMed ID	10421574

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