J
Jie Li
Researcher at University of California, Santa Cruz
Publications - 18
Citations - 6832
Jie Li is an academic researcher from University of California, Santa Cruz. The author has contributed to research in topics: Alpha-synuclein & Protein folding. The author has an hindex of 18, co-authored 18 publications receiving 6345 citations. Previous affiliations of Jie Li include University of California, Berkeley.
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Evidence for a partially folded intermediate in alpha-synuclein fibril formation.
TL;DR: A model for the fibrillation of α-synuclein is proposed in which the first step is the conformational transformation of the natively unfolded protein into the aggregation-competent partially folded intermediate.
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Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure.
TL;DR: It is indicated that low concentrations of some metals can directly induce alpha-synuclein fibril formation and the potential for ligand bridging by polyvalent metal ions is proposed to be an important factor in the metal-induced conformational changes of alpha- synuclein.
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The Herbicide Paraquat Causes Up-regulation and Aggregation of α-Synuclein in Mice PARAQUAT AND α-SYNUCLEIN
Amy B. Manning-Boğ,Alison L. McCormack,Jie Li,Vladimir N. Uversky,Anthony L. Fink,Donato A. Di Monte +5 more
TL;DR: The results suggest that up-regulation of α-synuclein as a consequence of toxicant insult and direct interactions between the protein and environmental agents are potential mechanisms leading to α- Synuclein pathology in neurodegenerative disorders.
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Effect of Familial Parkinson's Disease Point Mutations A30P and A53T on the Structural Properties, Aggregation, and Fibrillation of Human α-Synuclein†
TL;DR: It is attributed to the increased propensity of these mutants to aggregate, relative to wild-type alpha-synuclein, rather than to any changes in the monomeric natively unfolded species.
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Biophysical Properties of the Synucleins and Their Propensities to Fibrillate INHIBITION OF α-SYNUCLEIN ASSEMBLY BY β- AND γ-SYNUCLEINS
Vladimir N. Uversky,Vladimir N. Uversky,Jie Li,Pierre O. Souillac,Ian S. Millett,Sebastian Doniach,Ross Jakes,Michel Goedert,Anthony L. Fink +8 more
TL;DR: In this paper, the authors showed that β-synuclein fibrillation was inhibited by β-and γ-Synuclein, which exhibited the properties of a random coil, whereas α- and γ -synucleins were slightly more compact and structured.