|1.||Sobue, Gen: 43 articles (12/2015 - 08/2002)|
|2.||Li, Xiao-Jiang: 43 articles (03/2015 - 03/2002)|
|3.||Nukina, Nobuyuki: 41 articles (02/2015 - 04/2003)|
|4.||Hayden, Michael R: 37 articles (06/2015 - 02/2002)|
|5.||Katsuno, Masahisa: 36 articles (12/2015 - 08/2002)|
|6.||La Spada, Albert R: 34 articles (07/2015 - 06/2002)|
|7.||Rubinsztein, David C: 33 articles (05/2015 - 05/2002)|
|8.||Adachi, Hiroaki: 32 articles (12/2015 - 08/2002)|
|9.||Nagai, Yoshitaka: 29 articles (01/2015 - 06/2003)|
|10.||Paulson, Henry L: 28 articles (10/2015 - 07/2002)|
|1.||Huntington Disease (Huntington's Disease)
05/01/2008 - "Using cellular and Drosophila models for Huntington's disease it was also shown that reduced ESCRT levels inhibit clearance of expanded polyglutamine aggregates and aggravate their neurotoxic effect. "
07/01/2015 - "Biology laboratory students then tested the novel potential pharmaceuticals in Huntington's disease model assays, using in vitro polyglutamine peptide aggregation and in vivo lethality studies in Drosophila. "
02/15/2015 - "Although Huntington's disease is caused by the expansion of a CAG triplet repeat within the context of the 3144-amino acid huntingtin protein (HTT), studies reveal that N-terminal fragments of HTT containing the expanded PolyQ region can be produced by proteolytic processing and/or aberrant splicing. "
01/01/2012 - "Modeling the polyglutamine aggregation pathway in Huntington's disease: from basic studies to clinical applications."
10/01/2006 - "During the past 5 years, gene expression studies in cell culture, animal models and in the brains of patients have shown that the perturbation of transcription frequently results in neuronal dysfunction in polyglutamine repeat diseases such as Huntington's disease. "
|2.||Neurodegenerative Diseases (Neurodegenerative Disease)
09/01/2009 - "In the present study we demonstrate that RNA interference mediated downregulation of hsromega-n transcripts is sufficient to suppress pathogenesis in several Drosophila models of human polyQ neurodegenerative diseases. "
11/13/2003 - "This establishes a novel high-throughput approach to study protein misfolding and aggregation associated with neurodegenerative diseases and implicates a signaling pathway of previously unrecognized importance in polyglutamine protein processing."
04/17/2000 - "Recent studies have shown that amplified polyglutamine repeat stretches form cellular aggregates that may be markers for these neurodegenerative diseases. "
12/02/2015 - "Polyglutamine-repeat disorders are part of a larger family of neurodegenerative diseases characterized by protein misfolding and aggregation. "
12/01/2015 - "Over the past two decades, Drosophila has proven to be successful in modeling this family of neurodegenerative disorders, including the faithful recapitulation of pathological features such as polyQ length-dependent formation of protein aggregates and progressive neuronal degeneration. "
04/01/2008 - "Lentivector-mediated expression of CRAG in Purkinje cells of model mice extensively cleared polyQ aggregates and re-activated dendritic differentiation, resulting in a striking rescue from ataxia. "
09/30/2011 - "Taking advantage of this feature, we also showed that lentivirus-mediated CRAG expression in the Purkinje cells of mice expressing polyQ resulted in clearance of the polyQ aggregates and rescue from ataxia. "
09/01/2012 - "Despite its pivotal role for the clinical pictures of these polyglutamine ataxias, no pathoanatomical studies of serial tissue sections through the cerebellum have been performed in SCA2 and SCA3 so far. "
08/01/2015 - "Expansion of the CAG/polyQ region of CACNA1A occurs within α1ACT and leads to ataxia. "
07/01/2014 - "However, at least half of dominant ataxias (SCAs) are caused by (CAG)n repeat expansions resulting in expanded polyglutamine tracts (SCAs 1, 2, 3, 6, 7, 17, and DRPLA), although of the remainder only SCAs 8, 10, 12, 14, 15/16, and 31 are frequent enough that the described phenotype is probably representative. "
|4.||Machado-Joseph Disease (Spinocerebellar Ataxia Type 3)
11/30/2001 - "Here, in studies of the spinocerebellar ataxia type 3 disease protein ataxin-3, we demonstrate that the protein sequence surrounding polyQ specifies the constituents of nuclear inclusions (NI) formed by the disease protein. "
01/01/2015 - "We have made the unexpected observation that PNKP stably associates with Ataxin-3 (ATXN3), a polyglutamine repeat-containing protein mutated in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph Disease (MJD). "
11/01/2014 - "Machado-Joseph disease (MJD) is caused by a (CAG)n trinucleotide repeat expansion that is translated into an abnormally long polyglutamine tract. "
06/01/2014 - "Aqueous extract of Gardenia jasminoides targeting oxidative stress to reduce polyQ aggregation in cell models of spinocerebellar ataxia 3."
01/01/2014 - "We are interested in elucidating the underlying mechanisms of toxicity of the protein ataxin-3, in which a polyglutamine expansion is the genetic determinant for Machado-Joseph Disease (MJD), also referred to as spinocerebellar ataxia 3 (SCA3). "
01/01/2007 - "Our finding that the stability of the ordered aggregates increases as the peptide chain length increases may help to explain the experimentally observed relation between polyglutamine tract length and aggregation in vitro and disease progression in vivo. "
05/12/2011 - "In this issue of Neuron, Wilburn et al. show that in a HDL2 mouse model, the polyglutamine peptide drives disease progression."
02/01/2008 - "Although a polyglutamine expansion encoded in a single allele of each of the responsible genes is sufficient for the onset of each disease, clinical observations suggest that interactions between these genes may affect disease progression. "
01/01/2008 - "Taken together, our data implicate activated p38MAPK in disease progression and suggest that its inhibition may represent a rational strategy for therapeutic intervention in the polyglutamine disorders."
01/01/2007 - "Htt-associated protein 1 (HAP1), a component of neuronal cytoplasmic stigmoid bodies (STBs), can sequester polyQ-expanded Htt and AR in STBs, thereby antagonizing formation of the nuclear aggregates associated with apoptotic neuron loss and disease progression. "
|2.||Proteins (Proteins, Gene)
|4.||Androgen Receptors (Androgen Receptor)
|5.||Proteasome Endopeptidase Complex (Proteasome)
|8.||Staphylococcal Protein A (A, Protein)
|10.||protein TDP-43 (TDP-43)
|4.||Drug Therapy (Chemotherapy)
|5.||Investigational Therapies (Experimental Therapy)