Lidia M. Mannuzzu
University of California, Berkeley
9 Papers
50 Citations
Lidia M. Mannuzzu is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Gating & Voltage-gated potassium channel. The author has an hindex of 9, co-authored 9 publications. Previous affiliations of Lidia M. Mannuzzu include University of California & University of Sassari.
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Papers
Direct Physical Measure of Conformational Rearrangement Underlying Potassium Channel Gating
TL;DR: During channel activation, a stretch of at least seven amino acids of the putative transmembrane segment S4 moved from a buried position into the extracellular environment, providing physical evidence in support of the hypothesis that S4 is the voltage sensor of voltage-gated ion channels.
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Independence and Cooperativity in Rearrangements of a Potassium Channel Voltage Sensor Revealed by Single Subunit Fluorescence
TL;DR: The results show that the first S4 movement occurs independently in each subunit, while the second occurs cooperatively, and at least part of the cooperativity appears to be intrinsic to the second S4 charge-carrying rearrangement.
98
Patent
Biomolecular optical sensors
Ehud Y. Isacoff,Lidia M. Mannuzzu,Mario Manuel Moronne +2 more
- 13 Jan 1997
TL;DR: In this paper, the authors proposed a method to report changes at a cell surface membrane using a post-translationally generated luminescer at a predetermined residue of the sensor protein, where a wide variety of luminescers and chemistries for generating the selected luminecer at the target residue of a sensor protein may be used.
50
Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial.
TL;DR: It is concluded that a significant hydrophobic barrier limits access to the urea inhibition site, suggesting that the Urea site is buried in the bilayer or in ahydrophobic region of the transporter.
Increased red cell calcium, decreased calcium adenosine triphosphatase, and altered membrane proteins during fava bean hemolysis in glucose-6-phosphate dehydrogenase-deficient (Mediterranean variant) individuals.
TL;DR: Oxidant-mediated damage to active calcium extrusion, hypothetically associated with increased calcium permeability, may explain the large increase in calcium levels, which could activate calcium-dependent protease activity, giving rise to the profound changes in the ghost protein pattern.