28 Papers
549 Citations
G. Inesi is an academic researcher from University of the Pacific (United States). The author has contributed to research in topics: Endoplasmic reticulum & ATPase. The author has an hindex of 23, co-authored 28 publications. Previous affiliations of G. Inesi include University of California, San Francisco & Federal University of Rio de Janeiro.
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Papers
Phase changes in the lipid moieties of sarcoplasmic reticulum membranes induced by temperature and protein conformation changes
TL;DR: Evidence is presented that the second transition reflects hydrophobic lipid-protein interactions and the effect of protein conformational changes on the dynamic state of membrane lipids.
97
ATP synthesis by sarcoplasmic reticulum ATPase following Ca2+, PH, temperature, and water activity jumps.
L de Meis,G. Inesi +1 more
TL;DR: It is postulated that high and low affinity binding sites are expressions of two interconverting states of the phosphoenzyme that allow transformation of the sites from the alkaline pH and low temperature regime.
82
Interdependence of H+, Ca2+, and Pi (or vanadate) sites in sarcoplasmic reticulum ATPase.
G. Inesi,D Lewis,A J Murphy +2 more
TL;DR: The known binding competition between the two cations and their opposite effects on the phosphorylation reaction suggest that interdependence of phosphorylated site, H+ sites, and Ca2+ sites is a basic mechanistic feature of enzyme catalysis and cation transport.
64
Mg2+ and Mn2+ modulation of Ca2+ transport and ATPase activity in sarcoplasmic reticulum vesicles.
Michele Chiesi,G. Inesi +1 more
TL;DR: Kinetic experimentation was used to characterize the Mg 2+ and Mn 2+ modulation of Ca 2+ transport and ATPase activity in sarcoplasmic reticulum vesicles and it was shown that this activation is due to M g 2+ occupancy of an allosteric site easily accessible on the outer surface of the vesicle, rather than to participation in an antiport mechanism.
55
Functional and structural roles of sarcoplasmic reticulum protein components
TL;DR: It is shown that the Ca 2+ ATPase in fact accounts for 70-90% of the total SR protein and that other minor protein components are not involved in the mechanism of active Ca 2÷ transport.
49