About: Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum

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

About: Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum Goto Sponge NotDistinct Permalink

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

scientific article published on 01 December 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 2000 (uk) مقالة علمية تنشرت ف 1 دجنبر 2000 (ary) article scientifique publié en 2000 (fr) im Dezember 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 2000 (ast) scientific article published on 01 December 2000 (en)
publication date	wds:Q73035003-5A12AAE6-B82D-49DB-A1D7-50CDE92BEE73
publication date	2000-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73035003-A6EEC205-9162-4685-BF81-FC4D46796D1D
language of work or name	English
cites work	wds:Q73035003-0447EE70-5C35-44E6-A1EB-7395994A24A4 wds:Q73035003-07DD616A-D11B-4FF1-9FE0-8E869CC8EA8E wds:Q73035003-12F7C2A3-BDE1-4B79-AEBF-4055F374C771 wds:Q73035003-1E5249C3-8D82-44F2-90ED-AAC31B6A469E wds:Q73035003-319DFA52-5206-4860-8378-0551B1C1CD71 wds:Q73035003-4C7B759F-ABA9-4F79-B740-205F10527A0E wds:Q73035003-73E8C8A3-7842-456B-8AC7-3D0CAD697088 wds:Q73035003-75E4CE3D-A246-423B-8DA5-91835F8F4C5E wds:Q73035003-8273C038-4B3F-4E89-B430-85D5444E612F wds:Q73035003-9093FB64-0D69-4585-AEFE-9B58C76C28E5 wds:Q73035003-90A3AC8A-46D3-4404-9C07-FF471CC65726 wds:Q73035003-960EA2FB-A92E-4F28-B980-92070C1DB202 wds:Q73035003-9E6E3CFA-1350-4A08-8C78-E8B573C74634 wds:Q73035003-A0B1D3BD-FECF-4F9A-B5D5-4172146B5A11 wds:Q73035003-B9C6DA0C-3F43-4917-9079-FA51F5431BDB wds:Q73035003-ED18FCFF-7E80-4826-A4F6-BB4F10C4C135 wds:Q73035003-FF4E39D4-5E4F-4A70-A677-0243A9BD6718
cites work	Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation Depolymerization of phospholamban in the presence of calcium pump: a fluorescence energy transfer study Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure Pentameric assembly of phospholamban facilitates inhibition of cardiac function in vivo Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum Phospholamban inhibitory function is activated by depolymerization Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban Use of a new label, (13)==(18)O, in the determination of a structural model of phospholamban in a lipid bilayer. Spatial restraints resolve the ambiguity arising from interpretations of mutagenesis data. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers High-level coexpression of the canine cardiac calcium pump and phospholamban in Sf21 insect cells Comparison of the kinetic effects of phospholamban phosphorylation and anti-phospholamban monoclonal antibody on the calcium pump in purified cardiac sarcoplasmic reticulum membranes Mg2+ and ATP effects on K+ activation of the Ca2+-transport ATpase of cardiac sarcoplasmic reticulum Phospholamban reduces cardiac Ca-ATPase sensitivity to thapsigargin and cyclopiazonic acid
author name string	wds:Q73035003-66D050E0-85F2-4005-9B53-110C4CC525D4 wds:Q73035003-BF99514A-2398-4B30-89B6-D26BE7FE0629 wds:Q73035003-DCB5E5B1-A6B8-4A94-827D-01CFA6BB9D95
author name string	Chen Z Jones LR Autry JM
rdfs:label	Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (en) Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (nl)
skos:prefLabel	Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (en) Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (nl)
name	Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (en) Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (nl)
author	wds:Q73035003-67DDC2FB-0708-4556-9EEC-329EB66B3582
author	Razvan L Cornea
title	wds:Q73035003-9F1F6420-5830-452E-9D39-BC85F526E3F9
title	Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum (en)
page(s)	wds:Q73035003-2491665A-6294-4BBD-B024-FBC82FB2D334
page(s)	41487-41494
instance of	wds:Q73035003-EF36AFCA-DF1F-49E0-9BBF-DE3EB7C1FE3A
instance of	scholarly article
PubMed ID	wds:Q73035003-09E4E867-1985-4C97-88D8-7B004CCE9CAF
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11016944
PubMed ID	11016944
published in	wds:Q73035003-DB708997-AFC2-4F46-A876-4D2E4EEA0D27
published in	Journal of Biological Chemistry
issue	wds:Q73035003-3A7E7620-D489-4C19-9206-C24E1150F72A
volume	wds:Q73035003-0FB7BF03-78AE-4E2B-B5F8-2EF949A06DBF
issue	52
volume	275
number of pages	wds:Q73035003-C9FCCD94-238B-48D3-93A9-B757EFAE264E
number of pages	8 (xsd:decimal)
DOI	wds:Q73035003-D5D4D3D9-96D3-4D37-BD27-33DC92EF4764
DOI	http://dx.doi.org/10.1074/JBC.M008195200
DOI	10.1074/JBC.M008195200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73035003
is cites work of	Oligomeric interactions of sarcolipin and the Ca-ATPase Förster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase. Structure, dynamics, and ion conductance of the phospholamban pentamer Computational design of a water-soluble analog of phospholamban Molecular physiology of the SERCA and SPCA pumps Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain. Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic Reticulum Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation. Superinhibitory phospholamban mutants compete with Ca2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure. Solid-state NMR reveals structural changes in phospholamban accompanying the functional regulation of Ca2+-ATPase Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents

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