The Folding and Aggregation Energy Landscapes of Tethered RRM Domains of Human TDP-43 Are Coupled via a Metastable Molten Globule-like Oligomer-Reference-Cited by-同舟云学术

The Folding and Aggregation Energy Landscapes of Tethered RRM Domains of Human TDP-43 Are Coupled via a Metastable Molten Globule-like Oligomer

Published:2018-12-06 Issue:6 Volume:58 Page:608-620
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Pillai Meenakshi¹,Jha Santosh Kumar¹^ORCID

Affiliation:

1. Physical and Materials Chemistry Division, Academy of Scientific and Innovative Research (AcSIR), CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, Maharashtra, India

Funder

University Grants Commission

Science and Engineering Research Board

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b01013

Reference65 articles.

1. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration

2. TDP-43: gumming up neurons through protein–protein and protein–RNA interactions

3. Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

4. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

5. TAR DNA-binding protein 43 in neurodegenerative disease

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