Author

Evans S. Adunyah

Observed name: E.S. Adunyah

Institutions: Oklahoma State University, University of Washington, ETH Zurich, Institute of Biochemistry

Observed institutions: Oklahoma State University, Mayo Clinic, University of Washington, Kwame Nkrumah University of Science and Technology, ETH Zurich, Institute of Biochemistry

OpenAlex ID: A5031992218

Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids.

1981 · V. Niggli, E.S. Adunyah, et al. · Journal of Biological Chemistry · 465

Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase.

1981 · V. Niggli, E.S. Adunyah, et al. · Journal of Biological Chemistry · 388

The anticalmodulin drugs trifluoperazine and R24571 remove the activation of the purified erythrocyte Ca2+‐ATPase by acidic phospholipids and by controlled proteolysis

1982 · Evans S. Adunyah, Verena Niggli, et al. · FEBS Letters · 47

Purified red blood cell Ca2+-pump ATPase: Evidence for direct inhibition by presumed anti-calmodulin drugs in the absence of calmodulin

1982 · Frank F. Vincenzi, Evans S. Adunyah, et al. · Cell Calcium · 41

The Ca2+-pump of sickle cell plasma membranes. Purification and reconstitution of the ATPase enzyme

1982 · V. Niggli, E.S. Adunyah, et al. · Cell Calcium · 28

Works count: 5

Citation count: 969

H-index: 5

I10-index: 5