Hai-Yan Wang
Chinese Academy of Sciences
8 Papers
18 Citations
Hai-Yan Wang is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Fibril & Denaturation (biochemistry). The author has an hindex of 3, co-authored 3 publications.
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Papers
Chirality of Glutathione Surface Coating Affects the Cytotoxicity of Quantum Dots
TL;DR: The effects of QDs capped with different chiral forms of the tripeptide glutathione (GSH) on cytotoxicity and induction of autophagy were examined and two different sizes of cadmium telluride QDs coated with either l-GSH (lGSH-QDs) or d-G SH (d-Gsh-Zn) were found to show dose-dependent cytotoxic and to significantly increase the levels of autophile vacu
225
A Photoelectrochemical Nanoreactor for Single-Cell Sampling and Near Zero-Background Faradic Detection of Intracellular MicroRNA.
Hai-Yan Wang,Yi-Tong Xu,Bing Wang,Si-Yuan Yu,Xiao-Mei Shi,Wei-Wei Zhao,Dechen Jiang,Hong-Yuan Chen,Jing-Juan Xu +8 more
TL;DR: Low miR concentration in the near nucleus region than that in the main cytosol was revealed by this nanotool, underpinning a zero-biased and near zero-background PEC methodology toward Faradic detection of non-electrogenic miR at single-cell level.
58
An Ultrasensitive and Efficient microRNA Nanosensor Empowered by the CRISPR/Cas Confined in a Nanopore.
Bing Wang,Yi-Tong Xu,Tianyang Zhang,Hai-Yan Wang,Xian Zhang,Zengqiang Wu,Wei-Wei Zhao,Hong-Yuan Chen,Jing-Juan Xu +8 more
- 21 Dec 2023
TL;DR: A new CRISPR/Cas-empowered nanotechnology for ultrasensitive nano-electrochemistry and bioanalysis capable of ultrasensitive microRNA detection is introduced.
11
Flexibility of the Ure2 prion domain is important for amyloid fibril formation
TL;DR: The results suggest that the position of the prion domain affects the ability of Ure2 to form fibrils primarily due to effects on its flexibility.
9
Deletion of a Ure2 C-terminal prion-inhibiting region promotes the rate of fibril seed formation and alters interaction with Hsp40.
TL;DR: The results suggest that the enhanced in vivo prion-inducing ability of the 151-158 deletion mutant is due to its enhanced ability to generate prion seeds.
9