Literature DB >> 18228539

Yeast as a model for studying human neurodegenerative disorders.

Leonor Miller-Fleming1, Flaviano Giorgini, Tiago F Outeiro.   

Abstract

Protein misfolding and aggregation are central events in many disorders including several neurodegenerative diseases. This suggests that alterations in normal protein homeostasis may contribute to pathogenesis, but the exact molecular mechanisms involved are still poorly understood. The budding yeast Saccharomyces cerevisiae is one of the model systems of choice for studies in molecular medicine. Modeling human neurodegenerative diseases in this simple organism has already shown the incredible power of yeast to unravel the complex mechanisms and pathways underlying these pathologies. Indeed, this work has led to the identification of several potential therapeutic targets and drugs for many diseases, including the neurodegenerative diseases. Several features associated with these diseases, such as formation of protein aggregates, cellular toxicity mediated by misfolded proteins, oxidative stress and hallmarks of apoptosis have been faithfully recapitulated in yeast, enabling researchers to take advantage of this powerful model to rapidly perform genetic and compound screens with the aim of identifying novel candidate therapeutic targets and drugs. Here we review the work undertaken to model human brain disorders in yeast, and how these models provide insight into novel therapeutic approaches for these diseases.

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Year:  2008        PMID: 18228539     DOI: 10.1002/biot.200700217

Source DB:  PubMed          Journal:  Biotechnol J        ISSN: 1860-6768            Impact factor:   4.677


  25 in total

Review 1.  Polyglutamine misfolding in yeast: toxic and protective aggregation.

Authors:  Martin L Duennwald
Journal:  Prion       Date:  2011-10-01       Impact factor: 3.931

Review 2.  How to bake a brain: yeast as a model neuron.

Authors:  Isabella Sarto-Jackson; Lubomir Tomaska
Journal:  Curr Genet       Date:  2016-01-18       Impact factor: 3.886

3.  Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process.

Authors:  Chai-Jui Tsai; Kiran Aslam; Holli M Drendel; Josephat M Asiago; Kourtney M Goode; Lake N Paul; Jean-Christophe Rochet; Tony R Hazbun
Journal:  J Biol Chem       Date:  2015-08-25       Impact factor: 5.157

Review 4.  Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities.

Authors:  Neena Singh; Swati Haldar; Ajai K Tripathi; Katharine Horback; Joseph Wong; Deepak Sharma; Amber Beserra; Srinivas Suda; Charumathi Anbalagan; Som Dev; Chinmay K Mukhopadhyay; Ajay Singh
Journal:  Antioxid Redox Signal       Date:  2013-08-15       Impact factor: 8.401

5.  The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.

Authors:  Lucía F Zacchi; Hui-Chuan Wu; Samantha L Bell; Linda Millen; Adrienne W Paton; James C Paton; Philip J Thomas; Michal Zolkiewski; Jeffrey L Brodsky
Journal:  J Biol Chem       Date:  2014-03-13       Impact factor: 5.157

6.  Saccharomyces cerevisiae as a model organism: a comparative study.

Authors:  Hiren Karathia; Ester Vilaprinyo; Albert Sorribas; Rui Alves
Journal:  PLoS One       Date:  2011-02-02       Impact factor: 3.240

7.  Praja1 ubiquitin ligase facilitates degradation of polyglutamine proteins and suppresses polyglutamine-mediated toxicity.

Authors:  Baijayanti Ghosh; Susnata Karmakar; Mohit Prasad; Atin K Mandal
Journal:  Mol Biol Cell       Date:  2021-06-23       Impact factor: 4.138

Review 8.  Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.

Authors:  Maria Carmela Di Rosa; Francesca Guarino; Stefano Conti Nibali; Andrea Magrì; Vito De Pinto
Journal:  Front Physiol       Date:  2021-05-19       Impact factor: 4.566

9.  Mitochondrion-mediated cell death: dissecting yeast apoptosis for a better understanding of neurodegeneration.

Authors:  Ralf J Braun
Journal:  Front Oncol       Date:  2012-11-28       Impact factor: 6.244

10.  Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model.

Authors:  Ekaterina Eremenko; Anat Ben-Zvi; Ludmilla A Morozova-Roche; Dina Raveh
Journal:  PLoS One       Date:  2013-03-06       Impact factor: 3.240

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