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Cited by 452

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine

Open access
Banerjee, Ritu, Liu, Jun, Beatty, Wandy, Pelosof, Lorraine, Klemba, Michael, Goldberg, Daniel E.·2002·Proceedings of the National Academy of Sciences

Abstract

Hemoglobin degradation is a metabolic process that is central to the growth and maturation of the malaria parasite Plasmodium falciparum. Two aspartic proteases that initiate degradation, plasmepsins (PMs) I and II, have been identified and extensively characterized. Eight additional PM genes are present in the P. falciparum genome. To better understand the enzymology of hemoglobin degradation, it is necessary to determine which of these genes are expressed when hemoglobin degradation is occurring, which encode active enzymes, and which gene products are found in the food vacuole where catabolism takes place. Our genome-wide analysis reveals that PM I, II, and IV and histo-aspartic protease encode hemoglobin-degrading food vacuole proteases. Despite having a histidine in place of one of the catalytic aspartic acids conserved in other aspartic proteases, histo-aspartic protease is an active hydrolase.

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Metadata

Authors
Banerjee, R., Liu, J., Beatty, W., Pelosof, L., Klemba, M., & Goldberg, D. E.
Venue
Proceedings of the National Academy of Sciences
Published
2002-01-08
Volume
99
Issue
2
Pages
990-995
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2165174924
Cited by
452
References
1
FWCI
28.99
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. https://app.cochat.ai/papers/10.1073/pnas.022630099
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Banerjee, R., Liu, J., Beatty, W., Pelosof, L., Klemba, M., & Goldberg, D. E. (2002). Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.022630099

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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