Effects of Cation Binding on the Conformation of Calsequestrin and the High Affinity Calcium-binding Protein of Sarcoplasmic Reticulum

scientific article published on September 25, 1974

Effects of Cation Binding on the Conformation of Calsequestrin and the High Affinity Calcium-binding Protein of Sarcoplasmic Reticulum is …
instance of (P31):
scholarly articleQ13442814

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P953full work available at URLhttp://intl.jbc.org/cgi/content/abstract/249/18/5867
https://api.elsevier.com/content/article/PII:S0021925820798984?httpAccept=text/plain
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P698PubMed publication ID4472093

P2093author name stringD. H. MacLennan
K. J. Dorrington
T. J. Ostwald
P2860cites workProtein measurement with the Folin phenol reagentQ20900776
Effects of ATP on the interaction of Ca++, Mg++, and K+ with fragmented sarcoplasmic reticulum isolated from rabbit skeletal muscleQ36427555
Isolation of a calcium-sequestering protein from sarcoplasmic reticulumQ37477859
Control of muscle contractionQ40000256
Conformational changes accompanying the dissociation and association of immunoglobulin-G subunitsQ43851179
Effect of molecular aggregation on circular dichroism and optical rotatory dispersion of helical poly-L-glutamic acid in solutionQ72232709
Binding of cations by microsomes from rabbit skeletal muscleQ72847388
P433issue18
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
cell biologyQ7141
P304page(s)5867-5871
P577publication date1974-09-01
1974-09-25
P1433published inJournal of Biological ChemistryQ867727
P1476titleEffects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum
Effects of Cation Binding on the Conformation of Calsequestrin and the High Affinity Calcium-binding Protein of Sarcoplasmic Reticulum
P478volume249

Reverse relations

cites work (P2860)
Q37278605A mutation in calsequestrin, CASQ2D307H, impairs Sarcoplasmic Reticulum Ca2+ handling and causes complex ventricular arrhythmias in mice
Q34599121Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin deduced from cDNA and peptide sequencing
Q35312872C-terminal residues of skeletal muscle calsequestrin are essential for calcium binding and for skeletal ryanodine receptor inhibition
Q35767396Calcium binding proteins in the sarcoplasmic/endoplasmic reticulum of muscle and nonmuscle cells
Q24528015Calreticulin
Q28305104Calreticulin: not just another calcium-binding protein
Q42800803Characterization of a calsequestrin-like protein from sea-urchin eggs
Q41902930Characterization of calsequestrin of avian skeletal muscle
Q70261521Coexpression of two isoforms of calsequestrin in rabbit slow-twitch muscle
Q39651113Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle
Q42130390Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin
Q36211309Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
Q41819575Protons induce calsequestrin conformational changes
Q37691457Purification and crystallization of the calcium binding protein of sarcoplasmic reticulum from skeletal muscle
Q34190203Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.
Q40565740Sarcoplasmic reticulum calsequestrins: structural and functional properties
Q34829628The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors

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