Document Detail

Hemoglobin metabolism in the malaria parasite Plasmodium falciparum.
MedLine Citation:
PMID:  9343345     Owner:  NLM     Status:  MEDLINE    
Hemoglobin degradation in intraerythrocytic malaria parasites is a vast process that occurs in an acidic digestive vacuole. Proteases that participate in this catabolic pathway have been defined. Studies of protease biosynthesis have revealed unusual targeting and activation mechanisms. Oxygen radicals and heme are released during proteolysis and must be detoxified by dismutation and polymerization, respectively. The quinoline antimalarials appear to act by preventing sequestration of this toxic heme. Understanding the disposition of hemoglobin has allowed identification of essential processes and metabolic weakpoints that can be exploited to combat this scourge of mankind.
S E Francis; D J Sullivan; D E Goldberg
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Annual review of microbiology     Volume:  51     ISSN:  0066-4227     ISO Abbreviation:  Annu. Rev. Microbiol.     Publication Date:  1997  
Date Detail:
Created Date:  1997-12-12     Completed Date:  1997-12-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372370     Medline TA:  Annu Rev Microbiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  97-123     Citation Subset:  IM    
Howard Hughes Medical Institute, Department of Molecular Microbiology and Barnes-Jewish Hospital, St. Louis, Missouri 63110, USA.
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MeSH Terms
Antimalarials / pharmacology
Aspartic Acid Endopeptidases / biosynthesis,  genetics,  metabolism
Cysteine Endopeptidases / biosynthesis,  genetics,  metabolism
Endopeptidases / metabolism*
Heme / chemistry,  metabolism
Hemoglobins / metabolism*
Molecular Structure
Oxidative Stress
Plasmodium falciparum / enzymology,  metabolism*
Grant Support
Reg. No./Substance:
0/Antimalarials; 0/Hemoglobins; 14875-96-8/Heme; EC 3.4.-/Endopeptidases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.-/falcipain; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC

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

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