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The Conformation of Calsequestrin Determines Its Ability to Regulate Skeletal Ryanodine Receptors

Biophysical journal, 2006-08, Vol.91 (4), p.1288-1301

2006

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ARVC-Related Mutations in Divergent Region 3 Alter Functional Properties of the Cardiac Ryanodine Receptor

Biophysical journal, 2008-06, Vol.94 (12), p.4668-4677

2008

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Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin

Cell calcium (Edinburgh), 2008-10, Vol.44 (4), p.363-373

2008

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Composite polymorphisms in the ryanodine receptor 2 gene associated with arrhythmogenic right ventricular cardiomyopathy

Cardiovascular research, 2006-08, Vol.71 (3), p.496-505

2006

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VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

FEBS letters, 1996-05, Vol.386 (2), p.205-210

1996

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Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation

Biophysical journal, 2005-05, Vol.88 (5), p.3444-3454

2005

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Characterization of Human Cardiac Calsequestrin and its Deleterious Mutants

Journal of molecular biology, 2007-11, Vol.373 (4), p.1047-1057

2007

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Identification of a 200 kDa polypeptide as type 3 phosphatidylinositol 4-kinase from bovine brain by partial protein and cDNA sequencing

Biochimica et biophysica acta, 1996-03, Vol.1311 (1), p.53-63

1996

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Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca(2+) release channel/ryanodine receptor with calsequestrin

FEBS letters, 2000-04, Vol.472 (1), p.73-77

2000

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Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca2+ release channel/ryanodine receptor with calsequestrin

FEBS letters, 2000-04, Vol.472 (1), p.73-77

2000

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The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor

Biochimica et biophysica acta, 1996-08, Vol.1283 (1), p.89-100

1996

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Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca 2+ release channel/ryanodine receptor with calsequestrin

FEBS letters, 2000-04, Vol.472 (1), p.73-77

2000

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Compartmentalized ATP synthesis in skeletal muscle triads

Biochemistry (Easton), 1992-01, Vol.31 (2), p.377-384

1992

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Calsequestrin: more than 'only' a luminal Ca2+ buffer inside the sarcoplasmic reticulum

Biochemical journal, 1999-01, Vol.337 ( Pt 1) (1), p.19-22

1999

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Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca^sup 2+^ and Phosphorylation

Biophysical journal, 2005-05, Vol.88 (5), p.3444

2005

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Enhancement of Ca2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor

FEBS letters, 1993-10, Vol.332 (3), p.237-242

1993

Volltextzugriff (PDF)

Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca 2+ and Phosphorylation

Biophysical journal, 2005, Vol.88 (5), p.3444-3454

2005

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Troponin I converts the skeletal muscle ryanodine receptor into a rectifying calcium release channel

FEBS letters, 2002-03, Vol.515 (1), p.155-158

2002

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Phosphorylation of the 100 000 M r Ca2+‐transport ATPase by Ca2+ or cyclic AMP‐dependent and ‐independent protein kinases

FEBS letters, 1981-08, Vol.131 (2), p.223-228

1981

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Phosphorylation of the 100 000 M r Ca 2+ ‐transport ATPase by Ca 2+ or cyclic AMP‐dependent and ‐independent protein kinases

FEBS letters, 1981-08, Vol.131 (2), p.223-228

1981

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Phosphorylation of the 100 000 Mr Ca 2+-transport ATPase by Ca 2+ or cyclic AMP-dependent and -independent protein kinases

FEBS letters, 1981, Vol.131 (2), p.223-228

1981

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Regulation of the Sarcoplasmic Reticular Ca2+ Transport ATPase by Phosphorylation and Dephosphorylation

Zeitschrift für Naturforschung C. A journal of biosciences, 1982-08, Vol.37 (7), p.682-684

1982

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Calsequestrin: more than ‘only’ a luminal Ca2+ buffer inside the sarcoplasmic reticulum

Biochemical journal, 1999-01, Vol.337 (1), p.19-22

1999

Volltextzugriff (PDF)

Enhancement of Ca 2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor

FEBS letters, 1993-10, Vol.332 (3), p.237-242

1993

Volltextzugriff (PDF)

Relation of phosphatidylinositol metabolism to glycolytic pathway in skeletal muscle membranes

Molecular and cellular biochemistry, 1990-12, Vol.99 (2), p.111-116

1990

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The Conformation of Calsequestrin Determines Its Ability to Regulate Skeletal Ryanodine Receptors

ARVC-Related Mutations in Divergent Region 3 Alter Functional Properties of the Cardiac Ryanodine Receptor

Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin

Composite polymorphisms in the ryanodine receptor 2 gene associated with arrhythmogenic right ventricular cardiomyopathy

VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation

Characterization of Human Cardiac Calsequestrin and its Deleterious Mutants

Identification of a 200 kDa polypeptide as type 3 phosphatidylinositol 4-kinase from bovine brain by partial protein and cDNA sequencing

Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca(2+) release channel/ryanodine receptor with calsequestrin

Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca2+ release channel/ryanodine receptor with calsequestrin

The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor

Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca 2+ release channel/ryanodine receptor with calsequestrin

Compartmentalized ATP synthesis in skeletal muscle triads

Calsequestrin: more than 'only' a luminal Ca2+ buffer inside the sarcoplasmic reticulum

Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca^sup 2+^ and Phosphorylation

Enhancement of Ca2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor

Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca 2+ and Phosphorylation

Troponin I converts the skeletal muscle ryanodine receptor into a rectifying calcium release channel

Phosphorylation of the 100 000 M r Ca2+‐transport ATPase by Ca2+ or cyclic AMP‐dependent and ‐independent protein kinases

Phosphorylation of the 100 000 M r Ca 2+ ‐transport ATPase by Ca 2+ or cyclic AMP‐dependent and ‐independent protein kinases

Phosphorylation of the 100 000 Mr Ca 2+-transport ATPase by Ca 2+ or cyclic AMP-dependent and -independent protein kinases

Regulation of the Sarcoplasmic Reticular Ca2+ Transport ATPase by Phosphorylation and Dephosphorylation

Calsequestrin: more than ‘only’ a luminal Ca2+ buffer inside the sarcoplasmic reticulum

Enhancement of Ca 2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor

Relation of phosphatidylinositol metabolism to glycolytic pathway in skeletal muscle membranes

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