Localization of the hinge region of the Ca2+-ATPase of sarcoplasmic reticulum using resonance energy transfer
- 1 June 1994
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1192 (1), 53-60
- https://doi.org/10.1016/0005-2736(94)90142-2
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Labeling the calcium-magnesium-ATPase of sarcoplasmic reticulum at Glu-439 with 5-(bromomethyl)fluoresceinBiochemistry, 1993
- Localization of Cys-344 on the (Ca2+ −Mg2+)-ATPase of sarcoplasmic reticulum using resonance energy transferBiochimica et Biophysica Acta (BBA) - Biomembranes, 1993
- Definition of surface-exposed and trans-membranous regions of the (Ca2+-Mg2+)-ATPase of sarcoplasmic reticulum using anti-peptide antibodiesBiochemical Journal, 1992
- Cystic fibrosis transmembrane conductance regulator and the etiology and pathogenesis of cystic fibrosisThe FASEB Journal, 1992
- Ca2+-Dependent Conformational Change of the ATP-Binding Site of Ca2+-Transporting ATPase of Sarcoplasmic Reticulum as Revealed by an Alteration of the Target-Site Specificity of Adenosine Tr iphosphopyridoxal1The Journal of Biochemistry, 1989
- Positions of the sites labeled by N-cyclohexyl-N′-(4-dimethylamino-1-naphthyl)carbodiimide on the (Ca2+ + Mg2+)-ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1989
- Affinity Labeling of the ATP-Binding Site of Ca2+ -Transporting ATPase of Sarcoplasmic Reticulum by Adenosine Triphosphopyridoxal: Identification of the Reactive Lysyl Residue1The Journal of Biochemistry, 1988
- Structure and function of proton translocating ATPase in plasma membranes of plants and fungiBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1988
- The position of the ATP binding site on the (Ca2+ + Mg2+)-ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequenceNature, 1985