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Yang Li

Researcher at Huazhong University of Science and Technology

Publications -  12
Citations -  282

Yang Li is an academic researcher from Huazhong University of Science and Technology. The author has contributed to research in topics: Insulin & Amyloid. The author has an hindex of 9, co-authored 11 publications receiving 185 citations.

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Journal ArticleDOI

Disulfide bonds in amyloidogenesis diseases related proteins.

TL;DR: The role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidsogenic proteins is focused on.
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Dissecting the role of disulfide bonds on the amyloid formation of insulin.

TL;DR: The results indicated that breakage of A7-B7 induced more unfolding of the insulin structure and a higher amyloidogenicity than breakages of A6-A11, but breakages caused a significant cytotoxicity increase and aHigher potency to form high order toxic oligomers.
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C-terminal truncation exacerbates the aggregation and cytotoxicity of α-Synuclein: A vicious cycle in Parkinson's disease.

TL;DR: A hidden vicious cycle in PD is suggested that α-Syn121 rapidly forms amorphous aggregates, which activate caspase-1 to cleave α- Syn FL and generate more α-syn121, and this cycle may contribute to the onset and/or pathogenesis of PD.
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Copper and iron ions accelerate the prion-like propagation of α-synuclein: A vicious cycle in Parkinson's disease

TL;DR: It is reported that copper/iron ions accelerate prion-like propagation of α-synuclein fibrils by promoting cellular internalization of α -synucle in fibril, intracellular α- synuclein aggregation and the subsequent release of mature fibrs to the extracellular space to induce further propagation.
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Interaction between amyloidogenic proteins and biomembranes in protein misfolding diseases: Mechanisms, contributors, and therapy.

TL;DR: A comprehensive review of the mechanisms and contributing factors of the interaction between biomembranes and amyloidogenic proteins, and a summary of the therapeutic approaches to PMDs that target this interaction are provided.