Fadeng Yang
Overview
Explore the profile of Fadeng Yang including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
7
Citations
32
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Liu J, Sun J, Yang F, Tian Z, Wan C, Yin F, et al.
Small
. 2024 Dec;
:e2406214.
PMID: 39632353
Peptide self-assembly is a complex hierarchical process involving the progressive formation of secondary structures, such as α-helices, β-sheets, and turns, during the early stages. It is precisely these multi-component building...
2.
Dai C, Guo X, Pan Z, Wan C, Yang D, Li Y, et al.
Anal Chem
. 2023 Nov;
95(46):17125-17134.
PMID: 37934015
Cell surface proteins (CSPs) are valuable targets for therapeutic agents, but achieving highly selective CSP enrichment in cellular physiology remains a technical challenge. To address this challenge, we propose a...
3.
Tian Y, Liu J, Yang F, Lian C, Zhang H, Viles J, et al.
FEBS J
. 2022 Jun;
289(21):6767-6781.
PMID: 35670622
Inhibition of amyloid-β peptide (Aβ) aggregation is a promising therapeutic strategy for Alzheimer's disease (AD), as Aβ aggregation is generally believed to trigger AD pathology. Pre-fibril Aβ-oligomers induce membrane disruption...
4.
Jiang Y, Zhang W, Yang F, Wan C, Cai X, Liu J, et al.
Sci Adv
. 2021 Feb;
7(4).
PMID: 33523941
Peptide self-assembly inspired by natural superhelical coiled coils has been actively pursued but remains challenging due to limited helicity of short peptides. Side chain stapling can strengthen short helices but...
5.
Yang F, Zhang W, Jiang Y, Yin F, Han W, Li Z
Biochemistry
. 2019 Nov;
59(3):290-296.
PMID: 31702899
Amyloid-β (Aβ) oligomers are well-known toxic molecular species associated with Alzheimer's disease. Recent discoveries of the ability of amyloid fibril surfaces to convert soluble proteins into toxic oligomers suggested that...
6.
Jiang Y, Jiang X, Shi X, Yang F, Cao Y, Qin X, et al.
iScience
. 2019 Jul;
17:87-100.
PMID: 31255986
Amyloid fibril surfaces can convert soluble proteins into toxic oligomers and are attractive targets for intervention of protein aggregation diseases. Thus far, molecules identified with inhibitory activity are either large...
7.
Xiong Q, Jiang Y, Cai X, Yang F, Li Z, Han W
ACS Nano
. 2019 Mar;
13(4):4455-4468.
PMID: 30869864
The molecular design of peptide-assembled nanostructures relies on extensive knowledge pertaining to the relationship between conformational features of peptide constituents and their behavior regarding self-assembly, and characterizing the conformational details...