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Genetic analysis of the fluorescein isothiocyanate binding site of the yeast plasma membrane H(+)-ATPase.
Maldonado AM, Portillo F. Maldonado AM, et al. Among authors: portillo f. J Biol Chem. 1995 Apr 14;270(15):8655-9. doi: 10.1074/jbc.270.15.8655. J Biol Chem. 1995. PMID: 7721767 Free article.
The highly conserved motif of Saccharomyces cerevisiae H(+)-ATPase 474KGAP has been proposed to participate in the formation of the phosphorylated intermediate during the catalytic cycle (Portillo, F., and Serrano, R. (1988) EMBO J. 7, 1793-1798). In addition, Lys-4 …
The highly conserved motif of Saccharomyces cerevisiae H(+)-ATPase 474KGAP has been proposed to participate in the formation of the phosphor …
Molecular mechanism of regulation of yeast plasma membrane H(+)-ATPase by glucose. Interaction between domains and identification of new regulatory sites.
Eraso P, Portillo F. Eraso P, et al. Among authors: portillo f. J Biol Chem. 1994 Apr 8;269(14):10393-9. J Biol Chem. 1994. PMID: 8144622 Free article.
The carboxyl terminus of yeast plasma membrane H(+)-ATPase is an autoinhibitory domain, and its effect is counteracted by modification of the enzyme triggered by glucose metabolism (Portillo, F., Larrinoa, I. F., and Serrano, R. (1989) FEBS Lett. 247, 381-385 …
The carboxyl terminus of yeast plasma membrane H(+)-ATPase is an autoinhibitory domain, and its effect is counteracted by modification of th …
148 results