Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43-Reference-Cited by-同舟云学术

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Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43

Published:2010-08 Issue:34 Volume:285 Page:26304-26314
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fuentealba Rodrigo A.,Udan Maria,Bell Shaughn,Wegorzewska Iga,Shao Jieya,Diamond Marc I.,Weihl Conrad C.,Baloh Robert H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference77 articles.

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

2. TDP-43A315T mutation in familial motor neuron disease

3. TDP-43mutation in familial amyotrophic lateral sclerosis

4. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis

5. TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

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1. IntermediateHTTCAG repeats worsen disease severity in amyotrophic lateral sclerosis;Journal of Neurology, Neurosurgery & Psychiatry;2024-09-06

2. TDP43 and huntingtin Exon-1 undergo a conformationally specific interaction that strongly alters the fibril formation of both proteins;Journal of Biological Chemistry;2024-09

3. Structural details of helix-mediated TDP-43 C-terminal domain multimerization;2024-07-06

4. Production and characterization of novel monoclonal antibodies against pathological human TDP-43 proteins;Journal of Neuropathology & Experimental Neurology;2024-05-10

5. Amyloid-induced neurodegeneration: A comprehensive review through aggregomics perception of proteins in health and pathology;Ageing Research Reviews;2024-04

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