The AXH module: an independently folded domain common to ataxin-1 and HBP1-Reference-Cited by-同舟云学术

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The AXH module: an independently folded domain common to ataxin-1 and HBP1

Published:2003-08-23 Issue:1-3 Volume:551 Page:107-112
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

de Chiara C.,Giannini C.,Adinolfi S.,de Boer J.,Guida S.,Ramos A.,Jodice C.,Kioussis D.,Pastore A.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference19 articles.

1. Spinocerebellar ataxia type 1

2. Ataxin-1 Nuclear Localization and Aggregation

3. A structural approach to trinucleotide expansion diseases

4. The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract

5. Identification of a self-association region within the SCA1 gene product, ataxin-1

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2. Governing dynamics and preferential binding of the AXH domain influence the aggregation pathway of Ataxin‐1;Proteins: Structure, Function, and Bioinformatics;2022-10-19

3. Living and Coping with Spinocerebellar Ataxia: Palliative Care Approach;Spinocerebellar Ataxia - Concepts, Particularities and Generalities;2022-06-28

4. Making heads or tails – the emergence of capicua ( CIC ) as an important multifunctional tumour suppressor;The Journal of Pathology;2020-03-04

5. ATXN1 N-terminal region explains the binding differences of wild-type and expanded forms;BMC Medical Genomics;2019-10-26

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