Role of glutamine deamidation in neurodegenerative diseases associated with triplet repeat expansions

A hypothesis

Qurratulain Hasan, Ravindra Varma Alluri, Pragna Rao, Yog Raj Ahuja

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The pathological expansion of unstable trinucleotide repeats is known to cause neurodegenerative diseases. Trinucleotide repeat expansions might prove to be pathological through a variety of mechanisms, including alteration of DNA structure, transcription, RNA-protein interaction, and altered protein conformations/interactions. Deamidation of human proteins have been shown to regulate some time-dependent biological processes such as development and aging. In this paper we hypothesize the possible role of glutamine deamidation as a signaling event in the pathogenesis of neurodegenerative diseases associated with triplet repeat expansion.

Original languageEnglish
Pages (from-to)29-33
Number of pages5
JournalJournal of Molecular Neuroscience
Volume29
Issue number1
DOIs
Publication statusPublished - 05-2006

Fingerprint

Trinucleotide Repeat Expansion
Neurodegenerative diseases
Trinucleotide Repeats
Glutamine
Neurodegenerative Diseases
Biological Phenomena
Protein Conformation
Proteins
RNA
Transcription
Conformations
DNA
Aging of materials

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Biochemistry
  • Genetics

Cite this

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Role of glutamine deamidation in neurodegenerative diseases associated with triplet repeat expansions : A hypothesis. / Hasan, Qurratulain; Alluri, Ravindra Varma; Rao, Pragna; Ahuja, Yog Raj.

In: Journal of Molecular Neuroscience, Vol. 29, No. 1, 05.2006, p. 29-33.

Research output: Contribution to journalArticle

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