Ataxins

A family of predominantly nuclear proteins that regulate gene transcription and protein degradation. The expansion of CAG trinucleotide repeats in genes that encode Ataxins is associated with SPINOCEREBELLAR ATAXIAS (SCA). In SCA patients, the number of CAG repeats correlates with the severity of disease and inversely correlates with the age of disease onset.

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Networked: 30 relevant articles (1 outcomes, 1 trials/studies)

Relationship Network

Bio-Agent Context: Research Results

Experts

1.	Zoghbi, Huda Y: 3 articles (07/2010 - 10/2004)
2.	Chen, Chiung-Mei: 2 articles (01/2013 - 02/2009)
3.	Chen, I-Cheng: 2 articles (01/2013 - 02/2009)
4.	Hsieh-Li, Hsiu-Mei: 2 articles (01/2013 - 02/2009)
5.	Lee-Chen, Guey-Jen: 2 articles (01/2013 - 02/2009)
6.	Lin, Hsuan-Yuan: 2 articles (01/2013 - 02/2009)
7.	Su, Ming-Tsan: 2 articles (01/2013 - 02/2009)
8.	Wu, Yih-Ru: 2 articles (01/2013 - 02/2009)
9.	Orr, Harry T: 2 articles (07/2010 - 10/2004)
10.	Carrell, Ellie M: 1 article (06/2022)

Related Diseases

1.	Spinocerebellar Ataxias (Spinocerebellar Ataxia) 06/09/2022 - "Addressing both disease mechanisms, we have shown that virally expressed RNA interference targeting ATXN1 can both prevent and reverse disease phenotypes in SCA1 mice, and that overexpression of the ATXN1 homolog, ataxin 1-like (ATXN1L), improves disease readouts when delivered pre-symptomatically. " 01/01/2021 - "A family of such diseases are those caused by expansion of CAG repeats in genes of the ataxin family, resulting in spinocerebellar ataxias (SCA). " 01/01/2018 - "The AXH domain of protein Ataxin 1 is thought to play a key role in the misfolding and aggregation pathway responsible for Spinocerebellar ataxia 1. For this reason, a molecular level understanding of AXH oligomerization pathway is crucial to elucidate the aggregation mechanism, which is thought to trigger the disease. " 01/01/2013 - "Spinocerebellar ataxia type 8 (SCA8) involves the expansion of CTG/CAG repeats from the overlapping ataxin 8 opposite strand (ATXN8OS) and ataxin 8 (ATXN8) genes located on chromosome 13q21. " 07/08/2010 - "These results support a model in which Ataxin 1-Like overexpression represses SCA1 pathogenesis by compensating for a partial loss of function of Atxn1. "
2.	Hepatic Encephalopathy 10/01/2001 - "In an immunohistochemical study of Marinesco bodies--a neuronal intranuclear inclusion often seen in neurons of the substantia nigra of patients with hepatic encephalopathy--it was shown that one of the polyglutamine proteins, ataxin-3, is preferentially recruited into this inclusion, whereas other polyglutamine proteins (ataxin-2 and TATA box-binding protein) are not. "
3.	Neurodegenerative Diseases (Neurodegenerative Disease) 04/10/2012 - "However, neurodegenerative disease genes, for example huntingtin (HTT), the ataxins, the presenilins (PSEN1/PSEN2) are not simply localized to neurons but are ubiquitously expressed throughout peripheral tissues; it is therefore paramount to properly understand the earliest precipitating events leading to neuronal pathogenesis to develop effective long-term therapies. " 07/01/2007 - "As LANP interacts with ataxin 1--a protein mutated in the neurodegenerative disease spinocerebellar ataxia type 1 (SCA1)--we tested whether ataxin 1 can alter the E4F-LANP interaction. " 10/15/2004 - "Spinocerebellar ataxia type 1 (SCA1) is a neurodegenerative disease caused by the expansion of a polyglutamine repeat within the disease protein, ataxin 1. To elucidate cellular pathways involved in SCA1, we used DNA microarrays to determine the pattern of gene expression in SCA1 transgenic mice at two specific times in the disease process; 5 weeks, a timepoint prior to onset of pathology, and 12 weeks, at the midpoint of the disease progression. " 01/01/2010 - "A number of neurodegenerative diseases, including Alzheimer's disease, tauopathies, Parkinson's disease, and synucleinopathies, polyglutamine diseases, including Huntington's disease, amyotrophic lateral sclerosis, and transmissible spongiform encephalopathy, are characterized by the existence of a protein or peptide prone to aggregation specific to the disease: amyloid-β, tau protein, α-synuclein, atrophin 1, androgen receptor, prion protein, copper-zinc superoxide dismutase, α 1A subunit of CaV2.1, TATA-box binding protein, huntingtin, and ataxins 1, 2, 3, and 7. Beside this common molecular feature, we have found three additional main properties related to the disease-connected protein or peptide, which are shared by all those neurological disorders: first, proneness to aggregation, which, in many cases, seems to be bound to the lack of a clearly defined secondary structure; second, reported presence of the disease-related protein inside the nucleus; and finally, an apparently unspecific interaction with DNA. "
4.	Huntington Disease (Huntington's Disease) 03/01/2011 - "For example, expansion of the polyQ tract (>40 repeats) in huntingtin (htt) proteins leads to Huntington disease, while polyQ-expanded ataxins cause several types of ataxias. " 06/01/1998 - "The two shorter constructs containing the beta A4 sequence formed similar intranuclear aggregates to those reported for intranuclear inclusions of polyglutamine peptides from huntingtin (in Huntington's disease) and ataxin protein fragments (in spinocerebellar ataxia). " 01/01/2010 - "A number of neurodegenerative diseases, including Alzheimer's disease, tauopathies, Parkinson's disease, and synucleinopathies, polyglutamine diseases, including Huntington's disease, amyotrophic lateral sclerosis, and transmissible spongiform encephalopathy, are characterized by the existence of a protein or peptide prone to aggregation specific to the disease: amyloid-β, tau protein, α-synuclein, atrophin 1, androgen receptor, prion protein, copper-zinc superoxide dismutase, α 1A subunit of CaV2.1, TATA-box binding protein, huntingtin, and ataxins 1, 2, 3, and 7. Beside this common molecular feature, we have found three additional main properties related to the disease-connected protein or peptide, which are shared by all those neurological disorders: first, proneness to aggregation, which, in many cases, seems to be bound to the lack of a clearly defined secondary structure; second, reported presence of the disease-related protein inside the nucleus; and finally, an apparently unspecific interaction with DNA. "
5.	Parkinson Disease (Parkinson's Disease) 07/01/2002 - "Mutations in genes that cause inherited forms of Alzheimer's disease (amyloid precursor protein and presenilins), Parkinson's disease (alpha-synuclein and Parkin), and trinucleotide repeat disorders (huntingtin, androgen receptor, ataxin, and others) overwhelm endogenous neuroprotective mechanisms; other genes, such as those encoding apolipoprotein E(4), have more subtle effects on brain aging. " 01/01/2010 - "A number of neurodegenerative diseases, including Alzheimer's disease, tauopathies, Parkinson's disease, and synucleinopathies, polyglutamine diseases, including Huntington's disease, amyotrophic lateral sclerosis, and transmissible spongiform encephalopathy, are characterized by the existence of a protein or peptide prone to aggregation specific to the disease: amyloid-β, tau protein, α-synuclein, atrophin 1, androgen receptor, prion protein, copper-zinc superoxide dismutase, α 1A subunit of CaV2.1, TATA-box binding protein, huntingtin, and ataxins 1, 2, 3, and 7. Beside this common molecular feature, we have found three additional main properties related to the disease-connected protein or peptide, which are shared by all those neurological disorders: first, proneness to aggregation, which, in many cases, seems to be bound to the lack of a clearly defined secondary structure; second, reported presence of the disease-related protein inside the nucleus; and finally, an apparently unspecific interaction with DNA. "

Related Drugs and Biologics

1.	Interferon-beta
2.	polyglutamine
3.	Proteins (Proteins, Gene)
4.	TATA-Box Binding Protein (TATA-Binding Protein)
5.	Ataxin-3
6.	Androgen Receptors (Androgen Receptor)
7.	Presenilins
8.	Peptides (Polypeptides)
9.	DNA (Deoxyribonucleic Acid)
10.	Amyloid (Amyloid Fibrils)

Related Therapies and Procedures

1.	Therapeutics