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Cited by 436

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Plasmodium Hemozoin Formation Mediated by Histidine-Rich Proteins

Sullivan, David J., Gluzman, Ilya Y., Goldberg, Daniel E.·1996·Science

Abstract

The digestive vacuole of Plasmodium falciparum is the site of hemoglobin degradation, heme polymerization into crystalline hemozoin, and antimalarial drug accumulation. Antibodies identified histidine-rich protein II (HRP II) in purified digestive vacuoles. Recombinant or native HRP II promoted the formation of hemozoin, and chloroquine inhibited the reaction. The related HRP III also polymerized heme, and an additional HRP was identified in vacuoles. It is proposed that after secretion by the parasite into the host erythrocyte cytosol, HRPs are brought into the acidic digestive vacuole along with hemoglobin. After hemoglobin proteolysis, HRPs bind the liberated heme and mediate hemozoin formation.

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Metadata

Authors
Sullivan, D. J., Gluzman, I. Y., & Goldberg, D. E.
Venue
Science
Published
1996-01-12
Volume
271
Issue
5246
Pages
219-222
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2006250595
Cited by
436
References
2
FWCI
26.41
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Plasmodium Hemozoin Formation Mediated by Histidine-Rich Proteins. https://app.cochat.ai/papers/10.1126/science.271.5246.219
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Sullivan, D. J., Gluzman, I. Y., & Goldberg, D. E. (1996). Plasmodium Hemozoin Formation Mediated by Histidine-Rich Proteins. Science. https://doi.org/10.1126/science.271.5246.219

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.