Patent
Regulators of protein misfolding and aggregation and methods of using the same
Guy A. Caldwell,Kim A. Caldwell +1 more
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In this article, the authors describe genes that affect the misfolding of, and subsequent aggregation of, aggregation-prone proteins such as alpha-synuclein and have implications for the diagnosis and treatment of neurological diseases related to protein aggregation such as Parkinson's disease.Abstract:
Polynucleotide molecules and the proteins encoded by the molecules, diagnostic and treatment methods for neurological disorders characterized by protein aggregation are provided. Genes are described herein that affect the misfolding of, and subsequent aggregation of, aggregation-prone proteins such as alpha-synuclein and have implications for the diagnosis and treatment of neurological diseases related to protein aggregation such as Parkinson's disease. Knockdown of expression of the genes described herein using RNAi results in alpha-synuclein protein aggregation in a C. elegans model of protein aggregation. Dopaminergic neuroprotection after exposure to the neurotoxin 6-OHDA or overexpression of alpha-synuclein may also be provided by overexpression of proteins. Knowledge of genes relating to protein misfolding and aggregation provides powerful means to develop diagnostic screening methods, mutation analysis and drug design information for the development of novel therapeutic and neuroprotective compounds to treat neurodegenerative diseases such as Parkinson's disease.read more
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Regulators of protein misfolding and neuroprotection and methods of use
Guy A. Caldwell,Kim A. Caldwell +1 more
TL;DR: In this paper, the authors describe genes that affect the misfolding of, and subsequent aggregation of, aggregation-prone proteins such as alpha-synuclein and have implications for the diagnosis and treatment of neurological diseases related to protein aggregation such as Parkinson's disease.
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References
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Journal ArticleDOI
Ubiquitination of a New Form of α-Synuclein by Parkin from Human Brain: Implications for Parkinson's Disease
Hideki Shimura,Michael G. Schlossmacher,Nobutaka Hattori,Matthew P. Frosch,Alexander Trockenbacher,Rainer Schneider,Yoshikuni Mizuno,Kenneth S. Kosik,Dennis J. Selkoe +8 more
TL;DR: It is concluded that αSp22 is a substrate for parkin's ubiquitin ligase activity in normal human brain and that loss of parkin function causes pathologicalαSp22 accumulation in conventional PD brains.
Journal ArticleDOI
Ibuprofen Suppresses Plaque Pathology and Inflammation in a Mouse Model for Alzheimer's Disease
Giselle P. Lim,Giselle P. Lim,Fusheng Yang,Fusheng Yang,T. Chu,T. Chu,Patrick B. Chen,Patrick B. Chen,Walter Beech,Walter Beech,Bruce Teter,Bruce Teter,Tracy S. Tran,Tracy S. Tran,Oliver J. Ubeda,Oliver J. Ubeda,K. Hsiao Ashe,Sally A. Frautschy,Greg M. Cole +18 more
TL;DR: The anti-inflammatory drug ibuprofen, which has been associated with reduced AD risk in human epidemiological studies, can significantly delay some forms of AD pathology, including amyloid deposition, when administered early in the disease course of a transgenic mouse model of AD.
Journal ArticleDOI
Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an α-synuclein rat model of Parkinson's disease
Christophe Lo Bianco,Bernard L. Schneider,Matthias R. Bauer,Ali Sajadi,Alexis Brice,Takeshi Iwatsubo,Patrick Aebischer +6 more
TL;DR: Results indicate that parkin gene therapy may represent a promising candidate treatment for PD, with significant reductions in alpha-synuclein-induced neuropathology, and a key role for parkin in the genesis of Lewy bodies.
Journal ArticleDOI
Neurodegeneration and Neuroprotection in Parkinson Disease
Stanley Fahn,David Sulzer +1 more
TL;DR: Genetic and environmental findings related to PD epidemiology, suggestions that aberrant protein degradation may play a role in disease pathogenesis, and pathogenetic mechanisms including oxidative stress due to DA oxidation that could underlie the selectivity of neurodegeneration are outlined.
Journal ArticleDOI
Suppression of polyglutamine-induced protein aggregation in Caenorhabditis elegans by torsin proteins
Guy A. Caldwell,Songsong Cao,Elaina G. Sexton,Christopher C. Gelwix,John Paul Bevel,Kim A. Caldwell +5 more
TL;DR: It is determined that ectopic overexpression of both human and C. elegans torsin proteins results in a dramatic reduction of polyglutamine-dependent protein aggregation in a manner similar to that previously reported for molecular chaperones, and this data represent the first functional evidence of a role for torsins in effectively managing protein folding.