Document Detail


Cytochrome c as an experimental model protein.
MedLine Citation:
PMID:  21264390     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mitochondrial cytochrome c is among the most intensively studied of all proteins. Initial interest was in its role in the respiratory chain and as a model for studies of protein structure, folding and electron transfer. The function of cytochrome c in signalling apoptosis has brought a new wave of research into the protein. Bacterial cytochromes c are more complex and varied in function. This review highlights some of these roles and expands on systems for producing holocytochrome c proteins.
Authors:
Julie M Stevens
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2011-01-24
Journal Detail:
Title:  Metallomics : integrated biometal science     Volume:  3     ISSN:  1756-591X     ISO Abbreviation:  Metallomics     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-04-05     Completed Date:  2011-07-25     Revised Date:  2011-09-16    
Medline Journal Info:
Nlm Unique ID:  101478346     Medline TA:  Metallomics     Country:  England    
Other Details:
Languages:  eng     Pagination:  319-22     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cytochromes c / chemistry*,  genetics*,  isolation & purification,  metabolism
Escherichia coli / genetics
Gene Expression
Humans
Models, Molecular
Protein Conformation
Recombinant Fusion Proteins / chemistry,  genetics,  isolation & purification,  metabolism
Grant Support
ID/Acronym/Agency:
BB/H017887/1//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Recombinant Fusion Proteins; 9007-43-6/Cytochromes c

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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