About: Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific journal article

Attributes	Values
rdf:type	Item
description	artículu científicu espublizáu en 1999 (ast) vědecký článek publikovaný v roce 1999 (cs) 1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в липні 1999 (uk) 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 1999/07/09) (nl) vedecký článok (publikovaný 1999/07/09) (sk) مقالة علمية (نشرت في 9-7-1999) (ar)
publication date	wds:Q28581520-31D986E7-DB3F-4B3C-8463-EB44B8B56263
publication date	1999-07-09 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28581520-EC9A80F0-8EED-42AE-B31C-7B3A72ECA131
language of work or name	English
cites work	wds:Q28581520-01979E68-5730-4EFA-943C-B229E947F01A wds:Q28581520-0CE39662-F802-4329-AFBA-C6F339CE999C wds:Q28581520-10951A55-C2B2-440B-B2D7-86B82ADC64B2 wds:Q28581520-161D44F4-4D47-4D29-916B-C0F9BA01810B wds:Q28581520-1D333EED-E76D-4E42-8A17-9A768CB569E7 wds:Q28581520-224C0BA6-AC99-46BC-8FBD-2447DFD85AA7 wds:Q28581520-27BE353B-99BD-4658-AF24-CF6F74ACF35E wds:Q28581520-2D89B965-70DD-4573-9918-4A25BC81A12D wds:Q28581520-31EE4824-E229-48C7-86A2-D94377B4D41B wds:Q28581520-351710FE-5B1D-4E7D-A277-C345439A1489 wds:Q28581520-4222F953-4269-4378-8CD9-2B31BF2851FD wds:Q28581520-43E57F31-5F40-4A25-A578-940B1DB7972D wds:Q28581520-47BBCBDA-862F-4018-9199-3F7F26E4D332 wds:Q28581520-57282E6B-1FE8-4329-9754-956DB0D31728 wds:Q28581520-5C1B7507-CD84-488F-9184-4884B7397BA8 wds:Q28581520-5E64F96C-ED57-483E-8477-B5B1E34305C3 wds:Q28581520-6452D7D5-862F-4D43-9603-E524A313E2F0 wds:Q28581520-684F4D4C-8E73-453C-8621-056FA2626C89 wds:Q28581520-6CC3E535-7CAB-4AAE-BC2E-2415FCA81391 wds:Q28581520-72C8071A-C3FE-42D6-B909-D97F32157329 wds:Q28581520-73C70EAE-1F27-4843-A128-DC48AEA7A0FA wds:Q28581520-7E0D51E1-F399-4F33-A08F-3E74B626EE25 wds:Q28581520-8EFBE74C-0ACD-4389-9174-E88DEAC60F4B wds:Q28581520-901DB7F3-3FB4-4119-B3A3-416C32257B0C wds:Q28581520-AA28EC19-A4E2-445F-B1AC-9F752A0050C5 wds:Q28581520-B1283B8A-5EFF-4C4B-B300-F9D4328FB229 wds:Q28581520-B57B2436-9599-40BB-829C-392EB38FF218 wds:Q28581520-B7A12F51-7D60-474E-836B-5855FBD995B5 wds:Q28581520-D0580643-8DCC-44D3-B52D-B84479C7F0AD wds:Q28581520-D51C4F83-3CD6-40C7-89A1-95E56646029E wds:Q28581520-D6A64DE1-F640-4947-92CD-F357E638EE4D wds:Q28581520-DA425DDA-427D-4CF2-A983-90887D057B6B wds:Q28581520-DE119F3D-24DC-4542-B63C-53C6AC0A2B5C wds:Q28581520-DF19E554-C0B0-402C-A1EB-5690106C9E48 wds:Q28581520-F8A507C7-1083-48DC-BDEB-88DFEC6A4F70 wds:Q28581520-FCE35BA5-E59F-45AE-98F4-750F3CDBD462
cites work	Protein kinase C--a question of specificity Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations The molecular heterogeneity of protein kinase C and its implications for cellular regulation Stimulus-dependent myristoylation of a major substrate for protein kinase C Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions An improved permeabilization protocol for the introduction of peptides into cardiac myocytes. Application to protein kinase C research The extended protein kinase C superfamily A time-efficient, linear-space local similarity algorithm Localization of protein kinases by anchoring proteins: a theme in signal transduction Characterization of cardiac calsequestrin Multiple sequence alignment with hierarchical clustering Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice. Positive and negative inotropic effects of phorbol 12-myristate 13-acetate: relationship to PKC-dependence and changes in [Ca2+]i Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts. Decreased expression in transformed cells Calsequestrin: more than 'only' a luminal Ca2+ buffer inside the sarcoplasmic reticulum Regulation of current flow through ryanodine receptors by luminal Ca2+. Novel functions for calreticulin: interaction with integrins and modulation of gene expression? Targeting of protein kinase Calpha to caveolae Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane Determination of the specific substrate sequence motifs of protein kinase C isozymes A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function Inhibition of the spontaneous rate of contraction of neonatal cardiac myocytes by protein kinase C isozymes. A putative role for the epsilon isozyme Experimental diabetes is associated with functional activation of protein kinase C epsilon and phosphorylation of troponin I in the heart, which are prevented by angiotensin II receptor blockade The Coatomer Protein '-COP, a Selective Binding Protein (RACK) for Protein Kinase C A major, transformation-sensitive PKC-binding protein is also a PKC substrate involved in cytoskeletal remodeling Phosphorylation of cardiac junctional and free sarcoplasmic reticulum by PKC alpha, PKC beta, PKA and the Ca2+/calmodulin-dependent protein kinase Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-delta Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells Phosphorylation of the cardiac isoform of calsequestrin in cultured rat myotubes and rat skeletal muscle The regulatory domain of protein kinase C-epsilon restricts the catalytic-domain-specificity Pseudosubstrates turn off protein kinases Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol Phosphorylation by protein kinases A and C of myofibrillar proteins in rabbit stunned and non-stunned myocardium. Selective loss of substrate recognition induced by the tumour-associated D294G point mutation in protein kinase Calpha Prolonged phorbol ester treatment down-regulates protein kinase C isozymes and increases contraction rate in neonatal cardiac myocytes
author name string	wds:Q28581520-5F64B154-D8E5-4B69-BE9E-2AF5BEC34A5D wds:Q28581520-DD2081AA-8318-48F0-8F06-9CF1DE126036 wds:Q28581520-E1860EC8-497C-44DB-858D-2BFE7A991323 wds:Q28581520-ED688C72-6FC7-479B-BDC7-3DB476E795F1
OpenCitations bibliographic resource ID	wds:Q28581520-BED389DA-BBA7-4319-812E-A388964FF2B2
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3549470
author name string	C. H. Chen B. L. Smith D. Mochly-Rosen M. M. Rodriguez
OpenCitations bibliographic resource ID	3549470
rdfs:label	Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C (en)

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 180 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software