Document Detail


The power of yeast to model diseases of the powerhouse of the cell.
MedLine Citation:
PMID:  23276920     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mitochondria participate in a variety of cellular functions. As such, mitochondrial diseases exhibit numerous clinical phenotypes. Because mitochondrial functions are highly conserved between humans and Saccharomyces cerevisiae, yeast are an excellent model to study mitochondrial disease, providing insight into both physiological and pathophysiological processes.
Authors:
Matthew G Baile; Steven M Claypool
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2013-01-01
Journal Detail:
Title:  Frontiers in bioscience (Landmark edition)     Volume:  18     ISSN:  1093-4715     ISO Abbreviation:  Front Biosci (Landmark Ed)     Publication Date:  2013  
Date Detail:
Created Date:  2013-01-01     Completed Date:  2013-06-12     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  101612996     Medline TA:  Front Biosci (Landmark Ed)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  241-78     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / genetics,  metabolism
Cardiolipins / biosynthesis
Carrier Proteins / genetics
DNA Replication
DNA, Mitochondrial / biosynthesis,  genetics
Electron Transport Complex II / genetics
Electron Transport Complex III / genetics
Electron Transport Complex IV / genetics
Humans
Membrane Proteins / genetics,  metabolism
Metalloendopeptidases / metabolism
Mitochondria / genetics,  physiology*
Mitochondrial ADP, ATP Translocases / genetics
Mitochondrial Diseases / genetics*
Mitochondrial Membrane Transport Proteins / metabolism
Mitochondrial Proteins / metabolism
Models, Biological*
Mutation
Oxidative Phosphorylation
Saccharomyces cerevisiae / genetics,  physiology*
Saccharomyces cerevisiae Proteins / metabolism
Succinate Dehydrogenase / genetics
Grant Support
ID/Acronym/Agency:
R00 HL089185/HL/NHLBI NIH HHS; R00HL089185/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Cardiolipins; 0/Carrier Proteins; 0/DNA, Mitochondrial; 0/Membrane Proteins; 0/Mitochondrial Membrane Transport Proteins; 0/Mitochondrial Proteins; 0/SYM1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/TOM7 protein, S cerevisiae; 9068-80-8/Mitochondrial ADP, ATP Translocases; EC 1.10.2.2/Electron Transport Complex III; EC 1.3.5.1/Electron Transport Complex II; EC 1.3.99.1/Succinate Dehydrogenase; EC 1.9.3.1/Electron Transport Complex IV; EC 3.4.24.-/Metalloendopeptidases; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/YTA12 protein, S cerevisiae; EC 3.6.3.14/oligomycin sensitivity-conferring protein
Comments/Corrections

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