The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (Q71824244)

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21 October 2019

title

The modulation of Ca2+ binding to sarcoplasmic reticulum ATPase by ATP analogues is pH-dependent (English)

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21 October 2019

author name string

E Mintz

1

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21 October 2019

A M Mata

2

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21 October 2019

V Forge

3

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21 October 2019

M Passafiume

4

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21 October 2019

F Guillain

5

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21 October 2019

language of work or name

English

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publication date

1 November 1995

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Journal of Biological Chemistry

21 October 2019

published in

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21 October 2019

volume

270

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21 October 2019

page(s)

27160-27164

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21 October 2019

issue

45

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The binding of nucleotides and bivalent cations to the calcium-and-magnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum

21 October 2019

cites work

1 reference

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Kinetics of the cooperativity of the Ca2+-transporting adenosine triphosphatase of sarcoplasmic reticulum and the mechanism of the ATP interaction

21 January 2018

1 reference

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Kinetics and Regulation of Sarcoplasmic Reticulum ATPase

21 January 2018

1 reference

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The binding of ATP to the catalytic and the regulatory site of Ca2+,Mg2+-dependent ATPase of the sarcoplasmic reticulum

21 January 2018

1 reference

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Kinetic evidence for two nucleotide binding sites on the calcium ATPase of sarcoplasmic reticulum

21 January 2018

1 reference

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Adenosine 5'-triphosphate at the active site accelerates binding of calcium to calcium adenosinetriphosphatase

21 January 2018

1 reference

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Mechanism for activation of the 4-nitrobenzo-2-oxa-1,3-diazole-labeled sarcoplasmic reticulum ATPase by Ca2+ and its modulation by nucleotides

21 January 2018

1 reference

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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

21 January 2018

1 reference

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Adenosine 5'-triphosphate modulation of catalytic intermediates of calcium-adenosine triphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylation

21 January 2018

1 reference

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Cooperative interaction between Ca2+ and beta,gamma-methylene adenosine triphosphate in their binding to fragmented sarcoplasmic reticulum from bullfrog skeletal muscle

21 January 2018

1 reference

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Accelerating effect of ATP on calcium binding to sarcoplasmic reticulum ATPase

21 January 2018

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Quantification and removal of glycogen phosphorylase and other enzymes associated with sarcoplasmic reticulum membrane preparations

21 January 2018

1 reference

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A rapid-filtration technique for membrane fragments or immobilized enzymes: Measurements of substrate binding or ion fluxes with a few-millisecond time resolution

21 January 2018

1 reference

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Transient kinetics of sarcoplasmic reticulum Ca2++Mg2+ ATPase studied by fluorescence

21 January 2018

1 reference

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Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein

21 January 2018

1 reference

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Modification of the ATP binding site of the Ca2+ -ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate

21 January 2018

1 reference

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Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+ -dependent adenosine triphosphatase of sarcoplasmic reticulum

21 January 2018

1 reference

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Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences

21 January 2018

1 reference

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Participation of H+ in the Ca2(+)-induced conformational transition of 4-nitro-2,1,3-benzoxadiazole-labeled sarcoplasmic reticulum ATPase

21 January 2018

1 reference

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Modulation of calcium binding in sarcoplasmic reticulum adenosinetriphosphatase

21 January 2018

1 reference

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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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.45.27160

21 January 2018

Identifiers

DOI

10.1074/JBC.270.45.27160

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7592971%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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