Studies of the interactions of 2‘,3‘-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site (Q72573097)

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scientific article published on March 10, 1984

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English	Studies of the interactions of 2‘,3‘-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site	scientific article published on March 10, 1984

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6142049%20AND%20SRC:MED&resulttype=core&format=json

27 October 2019

Studies of the interactions of 2',3'-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6142049%20AND%20SRC:MED&resulttype=core&format=json

27 October 2019

Studies of the interactions of 2‘,3‘-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site (English)

1 reference

10.1016/S0021-9258(17)43243-1

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10.1016/S0021-9258(17)43243-1

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10.1016/S0021-9258(17)43243-1

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author name string

R. K. Nakamoto

1

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13 August 2023

G. Inesi

2

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13 August 2023

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publication date

1 March 1984

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27 October 2019

10 March 1984

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=6142049

13 August 2023

full work available at URL

http://intl.jbc.org/cgi/content/abstract/259/5/2961

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13 August 2023

https://api.elsevier.com/content/article/PII:S0021925817432431?httpAccept=text/xml

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10.1016/S0021-9258(17)43243-1

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https://api.elsevier.com/content/article/PII:S0021925817432431?httpAccept=text/plain

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10.1016/S0021-9258(17)43243-1

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Journal of Biological Chemistry

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27 October 2019

259

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27 October 2019

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27 October 2019

2961-2970

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27 October 2019

The reversibility of the sarcoplasmic calcium pump

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10.1016/S0021-9258(17)43243-1

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Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

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Sulfhydryl group modification of sarcoplasmic reticulum membranes

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Sarcoplasmic reticulum adenosine triphosphatase: Labeling of an essential lysyl residue with pyridoxal-5′-phosphate

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Chemical modification of the Ca2+-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. III. Changes in the distribution of exposed lysine residues among subfragments with change in enzymatic state

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The reactivity of the thiol groups of the adenosine triphosphatase of sarcoplasmic reticulum and their location on tryptic fragments of the molecule

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

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

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Dynamic interconversions of phosphorylated and non-phosphorylated intermediates of the Ca-ATPase from sarcoplasmic reticulum followed in a fluorescein-labeled enzyme

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ATP dependent conformational change in "spin labelled" sarcoplasmic reticulum

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Reactivity of sarcoplasmic reticulum ATPase with iodoacetamide spin-label: evidence for two conformational states of the substrate binding site

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Structural effects of substrate utilization on the ATPase chains of sarcoplasmic reticulum

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Structure and function of the calcium pump protein of sarcoplasmic reticulum

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Titration of the nucleotide binding sites of Sarcoplasmic Reticulum Ca2+-ATPase with 2′, 3′-0-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate and 5′-diphosphate

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Preparation and properties of 2'(or 3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate, an analog of adenosine triphosphate.

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Fluorescence properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate and its use in the study of binding to heavy meromyosin ATPase

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Phospholipid orientation in sarcoplasmic membranes: spin-label ESR and proton MNR studies

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Protein measurement with the Folin phenol reagent

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Correction of timing errors in photomultiplier tubes used in phase-modulation fluorometry

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Partial reactions in the catalytic and transport cycle of sarcoplasmic reticulum ATPase

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Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies.

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Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions

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Calcium Gradient-Dependent and Calcium Gradient-Independent Phosphorylation of Sarcoplasmic Reticulum by Orthophosphate. The Role of Magnesium

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Biological activities and spectroscopic properties of chromophoric and fluorescent analogs of adenine nucleoside and nucleotides, 2′,3′-O-(2,4,6-trinitrocyclohexadienylidene) adenosine derivatives

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Vanadate inhibition of the Ca2+-dependent conformational change of the sarcoplasmic reticulum Ca2+-ATPase

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Enzyme-Catalyzed Phosphoryl Transfer Reactions

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The primary structure of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum. Peptides derived from digestion with cyanogen bromide, and the sequences of three long extramembranous segments

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

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An Algorithm for Least-Squares Estimation of Nonlinear Parameters

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Evaluation of H2O activity in the free or phosphorylated catalytic site of Ca2+-ATPase

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Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient

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Measurement of protein-binding phenomena by gel filtration

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

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6142049%20AND%20SRC:MED&resulttype=core&format=json

27 October 2019

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