Prion, 2011-10, Vol.5 (4), p.250-257
2011
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Details
- Autor(en) / Beteiligte
- Titel
- Modeling ALS and FTLD proteinopathies in yeast: An efficient approach for studying protein aggregation and toxicity
- Ist Teil von
- Prion, 2011-10, Vol.5 (4), p.250-257
- Ort / Verlag
- United States: Taylor & Francis
- Erscheinungsjahr
- 2011
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- In recent years there have been several reports of human neurodegenerative diseases that involve protein misfolding being modeled in the yeast Saccharomyces cerevisiae. This review summarizes recent advances in understanding the specific mechanisms underlying intracellular neuronal pathology during Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Lobar Degeneration (FTLD), including SOD1, TDP-43 and FUS protein inclusions and the potential of these proteins to be involved in pathogenic prion-like mechanisms. More specifically, we focus on findings from yeast systems that offer tremendous possibilities for screening for genetic and chemical modifiers of disease-related proteotoxicity.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1933-6896eISSN: 1933-690XDOI: 10.4161/pri.17229Titel-ID: cdi_proquest_miscellaneous_1039036715
- Format
- –
- Schlagworte
- Amyloid - chemistry, Amyloid - metabolism, Amyotrophic Lateral Sclerosis - metabolism, Amyotrophic Lateral Sclerosis - pathology, Binding, Biology, Bioscience, Calcium, Cancer, Cell, Cycle, DNA-Binding Proteins, Frontotemporal Lobar Degeneration - metabolism, Frontotemporal Lobar Degeneration - pathology, Humans, Landes, Models, Molecular, Organogenesis, Prions - chemistry, Prions - metabolism, Proteins, RNA-Binding Protein FUS - chemistry, RNA-Binding Protein FUS - metabolism, Saccharomyces cerevisiae - metabolism, Saccharomyces cerevisiae Proteins - metabolism, Superoxide Dismutase - chemistry, Superoxide Dismutase - metabolism, Superoxide Dismutase-1