The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity-Reference-Cited by-同舟云学术

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The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity

Published:2012-08 Issue:2 Volume:425 Page:219-224
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Chang Chung-ke,Wu Tzong-Huah,Wu Chu-Ya,Chiang Ming-hui,Toh Elsie Khai-Woon,Hsu Yin-Chih,Lin Ku-Feng,Liao Yu-heng,Huang Tai-huang,Huang Joseph Jen-Tse

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference33 articles.

1. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease;Buratti;Front. Biosci.,2008

2. Structural insights into TDP-43 in nucleic-acid binding and domain interactions;Kuo;Nucleic Acids Res.,2009

3. Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance;Buratti;Am. J. Hum. Genet.,2004

4. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis;Neumann;Science,2006

5. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs;Ou;J. Virol.,1995

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1. Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin α1/β Signaling;Journal of Molecular Biology;2024-10

2. TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategies;Ageing Research Reviews;2024-09

3. Pathogenic TDP‐43 accelerates the generation of toxic exon1 HTT in Huntington's disease knock‐in mice;Aging Cell;2024-08-26

4. Biophysical characterization of the phase separation of TDP-43 devoid of the C-terminal domain;Cellular & Molecular Biology Letters;2024-07-13

5. TDP43 autoregulation gives rise to shortened isoforms that are tightly controlled by both transcriptional and post-translational mechanisms;2024-07-04

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