Tags

Type your tag names separated by a space and hit enter

Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity.
Prion. 2011 Oct-Dec; 5(4):250-7.P

Abstract

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.

Authors+Show Affiliations

Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, MD, USA. Dmitry.Kryndushkin@usuhs.milNo affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

22052354

Citation

Kryndushkin, Dmitry, and Frank Shewmaker. "Modeling ALS and FTLD Proteinopathies in Yeast: an Efficient Approach for Studying Protein Aggregation and Toxicity." Prion, vol. 5, no. 4, 2011, pp. 250-7.
Kryndushkin D, Shewmaker F. Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity. Prion. 2011;5(4):250-7.
Kryndushkin, D., & Shewmaker, F. (2011). Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity. Prion, 5(4), 250-7. https://doi.org/10.4161/pri.17229
Kryndushkin D, Shewmaker F. Modeling ALS and FTLD Proteinopathies in Yeast: an Efficient Approach for Studying Protein Aggregation and Toxicity. Prion. 2011 Oct-Dec;5(4):250-7. PubMed PMID: 22052354.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity. AU - Kryndushkin,Dmitry, AU - Shewmaker,Frank, Y1 - 2011/10/01/ PY - 2011/11/5/entrez PY - 2011/11/5/pubmed PY - 2013/4/5/medline SP - 250 EP - 7 JF - Prion JO - Prion VL - 5 IS - 4 N2 - 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. SN - 1933-690X UR - https://www.unboundmedicine.com/medline/citation/22052354/Modeling_ALS_and_FTLD_proteinopathies_in_yeast:_an_efficient_approach_for_studying_protein_aggregation_and_toxicity_ L2 - https://www.tandfonline.com/doi/full/10.4161/pri.17229 DB - PRIME DP - Unbound Medicine ER -