An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicity
Abstract The self-assembly of biomolecules through noncovalent interactions is critical in both physiological and pathological processes, as exemplified by the assembly of amyloid β peptide (Aβ) into oligomers or fibrils in Alzheimer’s disease (AD). Developing molecules that can modulate this assemb...
Saved in:
| Main Authors: | Qijia Wei, Dangliang Liu, Wencheng Xia, Fengzhang Wang, Lu Huang, Jun Zhang, Xiaoya Wang, Zhongxin Xu, Changdong He, Wenzhe Li, Xiaomeng Shi, Chu Wang, Yuan Liu, Cong Liu, Suwei Dong |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-07-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-60978-w |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Rationally Designed Pentapeptide Analogs of Aβ19–23 Fragment as Potent Inhibitors of Aβ42 Aggregation
by: Sachin B. Baravkar, et al.
Published: (2025-05-01) -
Plasma phosphorylated tau 217 and amyloid‑β 42/40 for amyloid risk in subgroups
by: Heekyoung Kang, et al.
Published: (2025-08-01) -
New insights into the 17β-hydroxysteroid dehydrogenase type 10 and amyloid-β 42 derived cytotoxicity relevant to Alzheimer’s disease
by: Aneta Houfková, et al.
Published: (2025-07-01) -
Rigid DNA Frameworks Anchored Transistor Enabled Ultrasensitive Detection of Aβ-42 in Serum
by: Yungen Wu, et al.
Published: (2025-05-01) -
Nasal Aβ42 mirrors brain amyloid dynamics and cognitive decline across the Alzheimer’s disease continuum
by: Da Hae Jung, et al.
Published: (2025-08-01)