ATP is a cryptic binder of TDP-43 RRM domains to enhance stability and inhibit ALS/AD-associated fibrillation-Reference-Cited by-同舟云学术

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ATP is a cryptic binder of TDP-43 RRM domains to enhance stability and inhibit ALS/AD-associated fibrillation

Published:2020-01 Issue:1 Volume:522 Page:247-253
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Dang Mei,Kang Jian,Lim Liangzhong,Li Yifan,Wang Lu,Song Jianxing

Funder

Ministry of Education of Singapore

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. ATP as a biological hydrotrope;Patel;Science,2017

2. Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP;Sridharan;Nat. Commun.,2019

3. ATP enhances at low concentrations but dissolves at high concentrations liquid-liquid phase separation (LLPS) of ALS/FTD-causing FUS;Kang;Biochem. Biophys. Res. Commun.,2018

4. A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids,;Kang;PLoS Biol.,2019

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2. Adenosine Triphosphate: The Primordial Molecule That Controls Protein Homeostasis and Shapes the Genome–Proteome Interface;Biomolecules;2024-04-19

3. Liquid–liquid phase separation in Alzheimer’s disease;Journal of Molecular Medicine;2024-01-02

4. Suitability of Adenosine Derivatives in Improving the Activity and Stability of Cytochrome c under Stress: Insights into the Effect of Phosphate Groups;The Journal of Physical Chemistry B;2023-12-21

5. Mitigation of TDP-43-induced toxic phenotype by expression of RGNEF N-terminal fragment in ALS models;2023-10-01

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