Investigation of Plasmodium falciparum aminopeptidases and characterisation of the M17 leucine aminopeptidase
Citation:
Eithne Cunningham, 'Investigation of Plasmodium falciparum aminopeptidases and characterisation of the M17 leucine aminopeptidase', [thesis], Trinity College (Dublin, Ireland). Department of Microbiology, 2008, pp 213Download Item:
Abstract:
Plasmodium falciparum spends part of its life cycle residing in human erythrocytes,
during which time it digests much of the host cell haemoglobin to provide a source of
amino acids for synthesis of its own proteins. The final stages of digestion are thought to
be carried out by aminopeptidases that cleave amino acids from the N -termini of peptides.
The inhibition of aminopeptidase activity can disrupt parasite development, implicating
this group of enzymes as a possible drug target. Novel targets for antimalarial drugs are
greatly needed due to the high rate of mortality associated with the disease and the
emergence of resistance to existing treatments.
Author: Cunningham, Eithne
Advisor:
Bell, AngusPublisher:
Trinity College (Dublin, Ireland). Department of MicrobiologyNote:
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Full text availableKeywords:
Microbiology, Ph.D., Ph.D. Trinity College DublinMetadata
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