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Beyond the Qs in the polyglutamine diseases: Table 1.

Beyond the Qs in the polyglutamine diseases: Table 1. Downloaded from genesdev.cshlp.org on September 20, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Beyond the Qs in the polyglutamine diseases Harry T. Orr Departments of Laboratory Medicine and Pathology, Genetics, Cell Biology and Development, Biochemistry, Molecular Biology and Biophysics, and Institute of Human Genetics, University of Minnesota, Minneapolis, Minnesota 55455, USA It was 10 years ago that Kurt Fischbeck and his col- polyglutamine tract itself regardless of the protein con- leagues (La Spada et al. 1991) reported the identification text in which it is located. In the first case, the altered of a novel mutational mechanism that altered the se- toxic function of the protein could be a new function quence of a protein: the addition of glutamines to a poly- that is, for the most part, unrelated to the natural func- glutamine tract within the androgen receptor (AR). This tion of the protein. On the other hand, the alteration in mutation occurred in individuals affected with the mo- function could be related to the normal function of the tor neuron disease spinal and bulbar muscular atrophy protein. If this latter scenario were to be the case, it (SBMA) or Kennedy’s disease. With the cloning of http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Genes & Development Unpaywall

Beyond the Qs in the polyglutamine diseases: Table 1.

Orr, Harry T.
Genes & Development – Apr 15, 2001
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Unpaywall
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0890-9369
DOI
10.1101/gad.888401
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Abstract

Downloaded from genesdev.cshlp.org on September 20, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Beyond the Qs in the polyglutamine diseases Harry T. Orr Departments of Laboratory Medicine and Pathology, Genetics, Cell Biology and Development, Biochemistry, Molecular Biology and Biophysics, and Institute of Human Genetics, University of Minnesota, Minneapolis, Minnesota 55455, USA It was 10 years ago that Kurt Fischbeck and his col- polyglutamine tract itself regardless of the protein con- leagues (La Spada et al. 1991) reported the identification text in which it is located. In the first case, the altered of a novel mutational mechanism that altered the se- toxic function of the protein could be a new function quence of a protein: the addition of glutamines to a poly- that is, for the most part, unrelated to the natural func- glutamine tract within the androgen receptor (AR). This tion of the protein. On the other hand, the alteration in mutation occurred in individuals affected with the mo- function could be related to the normal function of the tor neuron disease spinal and bulbar muscular atrophy protein. If this latter scenario were to be the case, it (SBMA) or Kennedy’s disease. With the cloning of

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Genes & Development – Unpaywall

Published: Apr 15, 2001

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