Site‐Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation-Reference-Cited by-同舟云学术

Site‐Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation

Published:2022-02-21 Issue:16 Volume:61 Page:
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew Chem Int Ed

Author:

Gao Nan¹²,Liu Zhenqi¹²,Zhang Haochen¹²,Liu Chun¹²,Yu Dongqin¹²,Ren Jinsong¹²^ORCID,Qu Xiaogang¹²^ORCID

Affiliation:

1. Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization Changchun Institute of Applied Chemistry Chinese Academy of Science Changchun, Jilin 130022 P. R. China

2. School of Applied Chemistry and Engineering University of Science and Technology of China Hefei Anhui 230026 P. R. China

Funder

National Natural Science Foundation of China

Chinese Academy of Sciences

National Key Research and Development Program of China

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202115336

Reference41 articles.

1. Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications

2. Posttranslationale Proteinmodifikation: die Chemie der Proteomdiversifizierung

3. Introduction: Posttranslational Protein Modification

4. Polyoxometalate-based nanozyme: Design of a multifunctional enzyme for multi-faceted treatment of Alzheimer’s disease

5. Amyloid aggregates of the HET-s prion protein are infectious

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