Z
Zhiping Jiang
Researcher at National Institutes of Health
Publications - 19
Citations - 731
Zhiping Jiang is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Protein–lipid interaction & Membrane. The author has an hindex of 13, co-authored 19 publications receiving 621 citations. Previous affiliations of Zhiping Jiang include Kent State University.
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Journal ArticleDOI
Biophysics of α-Synuclein Membrane Interactions
TL;DR: In this paper, the authors summarize useful biophysical techniques for the study of peripheral membrane proteins and their application in the characterization of the membrane interactions of the natively unfolded and Parkinson's disease related protein, α-synuclein (α-syn) related protein.
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Membrane Remodeling by α-Synuclein and Effects on Amyloid Formation
TL;DR: It is discovered that α-syn deforms vesicles with no net surface charge (phosphatidylcholine, PC) into tubules (average diameter ∼20 nm) and influences bilayer structure with surprisingly weak interaction and no site specificity.
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Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein
TL;DR: In vitro results suggest that N-acetyl α-syn localizes to highly curved, ordered membranes inside a cell, and it is proposed that age-related changes in membrane fluidity can promote the formation of amyloid fibrils, insoluble materials associated with PD.
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Cholesterol stabilizes fluid phosphoinositide domains.
TL;DR: It is believed that cholesterol acts as a spacer between the phosphoinositide lipids, thereby reducing the electrostatic repulsion, while participating in the hydrogen bond network, leading to its further stabilization.
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Structural Features of Membrane-bound Glucocerebrosidase and α-Synuclein Probed by Neutron Reflectometry and Fluorescence Spectroscopy
Thai Leong Yap,Zhiping Jiang,Frank Heinrich,James M. Gruschus,Candace M. Pfefferkorn,Marília A. S. Barros,Joseph E. Curtis,Ellen Sidransky,Jennifer C. Lee +8 more
TL;DR: A model ofα-syn·GCase on the membrane is proposed, providing structural insights into inhibition of GCase by α-syn, and suggests a rearrangement of loops surrounding the catalytic site, where they extend into the hydrocarbon chain region of the outer leaflet.