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Pathological Mutations D169G and P112H Electrostatically Aggravate the Amyloidogenicity of the Functional Domain of TDP-43.

ACS chemical neuroscience - 4 Dec 2024

Pillai Meenakshi, Patil Anjali D, Das Atanu, Jha Santosh Kumar

Abstract excerpt

Aggregation of TDP-43 is linked to the pathogenesis of many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). Notably, electrostatic point mutations such as D169G and P112H, located within the highly conserved functional tandem RNA recognition motif (RRM) domains of the TDP-43 protein (TDP-43tRRM), have been identified in diseased patients as well. In this study, we address how the...

Topics

Humans
DNA-Binding Proteins
Static Electricity
Amyloid
Mutation
Protein Domains
Hydrogen-Ion Concentration
Protein Aggregation, Pathological

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 39558635
DOI: 10.1021/acschemneuro.4c00372

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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