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Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

Data up to Jan 2025

Published1994
Citations132
References18

Total Citations Per Year

Abstract

References (18)

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Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.

1994 • 166 citations

Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban.

1993 • 145 citations

Expression and Site-specific Mutagenesis of Phospholamban

1989 • 123 citations

Phospholamban regulation of cardiac sarcoplasmic reticulum (Ca(2+)-Mg2+)-ATPase. Mechanism of regulation and site of monoclonal antibody interaction

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The nucleotide binding/hinge domain plays a crucial role in determining isoform-specific Ca2+ dependence of organellar Ca(2+)-ATPases.

1992 • 71 citations

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Modulation by Polyelectrolytes of Canine Cardiac Microsomal Calcium Uptake and the Possible Relationship to Phospholamban

1989 • 53 citations

Residues 2-25 of phospholamban are insufficient to inhibit Ca2+ transport ATPase of cardiac sarcoplasmic reticulum

1993 • 49 citations

Involvement of electrostatic phenomena in phospholamban‐induced stimulation of Ca uptake into cardiac sarcoplasmic reticulum

1989 • 46 citations

Regulation of the calcium ion pump of sarcoplasmic reticulum: Reversible inhibition by phospholamban and by the calmodulin binding domain of the plasma membrane calcium pump

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Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic… (1994) – Journal of Biological Chemistry | Metascience Observatory Explorer