About: The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent

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About: The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent Goto Sponge NotDistinct Permalink

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scientific article published on 01 November 1995

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1995 (uk) article scientifique publié en 1995 (fr) im November 1995 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 November 1995 (en) artículu científicu espublizáu en payares de 1995 (ast)
publication date	wds:Q71824244-0E50B9A5-F220-48FD-BBD6-D91BAC260A4F
publication date	1995-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71824244-25C2ADF3-B8DF-43A7-B2AD-900CA8BABB0D
language of work or name	English
cites work	wds:Q71824244-0A4987C4-F4E5-43DE-96A9-1F01D459E2D3 wds:Q71824244-2B3241B3-1591-42BF-BC72-97C848B5585C wds:Q71824244-31CA3063-58F1-42C2-B1CC-59601D9A62AE wds:Q71824244-4B2BC3DA-8513-4140-B01B-BF52DEFB41BE wds:Q71824244-4FCFFD3B-6373-4BD5-A85B-8F18521EB681 wds:Q71824244-53FD1C5D-D072-4226-B6A7-28D1D8DC1A56 wds:Q71824244-56CC01AE-D608-4E79-9D66-633670F16DD8 wds:Q71824244-65CC40CA-FC45-4F86-BADD-CEB35AF4D89D wds:Q71824244-8D5BEECC-D7EB-45E4-B6F4-F18E04828EE0 wds:Q71824244-97028016-D382-4B0F-99D6-573219254496 wds:Q71824244-B3975D18-C575-4EFC-8DB3-7746FA18120C wds:Q71824244-BB4EF674-301C-4C5E-B6E5-B0F4150BA6C3 wds:Q71824244-C931E261-431D-4039-B7C1-486884200265 wds:Q71824244-D20F4525-6942-4333-8E4A-7DF58E52DE72 wds:Q71824244-E3511685-24E9-446D-BA23-59C36ED59077 wds:Q71824244-E3C2794A-BF73-4DD9-ACAA-BAA5EC11CAEA wds:Q71824244-E8DC239A-1AA8-4AB2-BAD9-90AB3164C419 wds:Q71824244-F7D9C6C7-F7B4-4025-A999-19CD5BD68004 wds:Q71824244-F8E62836-A22E-4F6D-8775-53B0D8F54DC6 wds:Q71824244-FB9A9FA6-8916-4482-83C1-ACF698EABB47 wds:Q71824244-FFECC011-B1A4-4560-92B2-3F8E62175FC6
cites work	Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences The reaction mechanism of Ca(2+)-ATPase of sarcoplasmic reticulum. Direct measurement of the Mg.ATP dissociation constant gives similar values in the presence or absence of calcium Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+ -dependent adenosine triphosphatase of sarcoplasmic reticulum Rapid filtration study of the phosphorylation-dependent dissociation of calcium from transport sites of purified sarcoplasmic reticulum ATPase and ATP modulation of the catalytic cycle The binding of ATP to the catalytic and the regulatory site of Ca2+,Mg2+-dependent ATPase of the sarcoplasmic reticulum Modulation of calcium binding in sarcoplasmic reticulum adenosinetriphosphatase Participation of H+ in the Ca2(+)-induced conformational transition of 4-nitro-2,1,3-benzoxadiazole-labeled sarcoplasmic reticulum ATPase The binding of nucleotides and bivalent cations to the calcium-and-magnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum Kinetics of the cooperativity of the Ca2+-transporting adenosine triphosphatase of sarcoplasmic reticulum and the mechanism of the ATP interaction Adenosine 5'-triphosphate modulation of catalytic intermediates of calcium-adenosine triphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylation Kinetics and Regulation of Sarcoplasmic Reticulum ATPase Transient kinetics of sarcoplasmic reticulum Ca2++Mg2+ ATPase studied by fluorescence Modification of the ATP binding site of the Ca2+ -ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate Adenosine 5'-triphosphate at the active site accelerates binding of calcium to calcium adenosinetriphosphatase A rapid-filtration technique for membrane fragments or immobilized enzymes: Measurements of substrate binding or ion fluxes with a few-millisecond time resolution Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein Quantification and removal of glycogen phosphorylase and other enzymes associated with sarcoplasmic reticulum membrane preparations Kinetic evidence for two nucleotide binding sites on the calcium ATPase of sarcoplasmic reticulum Mechanism for activation of the 4-nitrobenzo-2-oxa-1,3-diazole-labeled sarcoplasmic reticulum ATPase by Ca2+ and its modulation by nucleotides Cooperative interaction between Ca2+ and beta,gamma-methylene adenosine triphosphate in their binding to fragmented sarcoplasmic reticulum from bullfrog skeletal muscle Accelerating effect of ATP on calcium binding to sarcoplasmic reticulum ATPase
author name string	wds:Q71824244-16AB7060-F23C-4BFC-A7E5-887E7B458C34 wds:Q71824244-2A5168A0-9B5B-4B12-A530-79DA54EAE3EA wds:Q71824244-79B497B5-FE7E-449B-8CAA-4F5208A1DD6E wds:Q71824244-9E9B47E4-82A4-4C2E-88B8-D95A4C1EA593 wds:Q71824244-B512E1CB-9B43-4110-8881-1426E3DDE155
author name string	E Mintz A M Mata F Guillain V Forge M Passafiume
rdfs:label	The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (en) The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (nl)
skos:prefLabel	The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (en) The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (nl)
name	The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (en) The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (nl)
title	wds:Q71824244-34C073A8-0BF0-49BF-A081-BDA4264E8184
title	The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (en)
page(s)	wds:Q71824244-FE7C05FD-0C50-4571-B6ED-9E907316D924
page(s)	27160-27164
instance of	wds:Q71824244-4D290857-D96A-445E-90AB-108499BB14AA
instance of	scholarly article
PubMed ID	wds:Q71824244-9112D799-9BF4-481A-A369-27FD63AF8232
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7592971
PubMed ID	7592971
published in	wds:Q71824244-D11BF570-7048-497A-8961-2A91D3BA9197
published in	Journal of Biological Chemistry
issue	wds:Q71824244-5984443F-B7FE-478B-890A-A6DCA7740420
volume	wds:Q71824244-BE091FA0-028D-44BE-8B05-1E4530626152
issue	45
volume	270
DOI	wds:Q71824244-3FC6BC65-6CA8-4DB0-8564-7A93C239B707
DOI	http://dx.doi.org/10.1074/JBC.270.45.27160
DOI	10.1074/JBC.270.45.27160
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71824244
is cites work of	Modulatory and catalytic modes of ATP binding by the calcium pump Interaction of nucleotides with Asp(351) and the conserved phosphorylation loop of sarcoplasmic reticulum Ca(2+)-ATPase. Fast kinetic analysis of conformational changes in mutants of the Ca(2+)-ATPase of sarcoplasmic reticulum Calcium transport by sarcoplasmic reticulum Ca(2+)-ATPase. Role of the A domain and its C-terminal link with the transmembrane region. Concerted conformational effects of Ca2+ and ATP are required for activation of sequential reactions in the Ca2+ ATPase (SERCA) catalytic cycle Ca2+ transport by the sarcoplasmic reticulum ATPase pH and ligand binding modulate the strength of protein-protein interactions in the Ca(2+)-ATPase from sarcoplasmic reticulum membranes Effect of orthophosphate, nucleotide analogues, ADP, and phosphorylation on the cytoplasmic domains of Ca(2+)-ATPase from scallop sarcoplasmic reticulum Neutralization of the charge on Asp 369 of Na+,K+-ATPase triggers E1 <--> E2 conformational changes Calcium additional to that bound to the transport sites is required for full activation of the sarcoplasmic reticulum Ca-ATPase from skeletal muscle A remarkably stable phosphorylated form of Ca2+-ATPase prepared from Ca2+-loaded and fluorescein isothiocyanate-labeled sarcoplasmic reticulum vesicles Redistribution of SERCA calcium pump conformers during intracellular calcium signaling

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