Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates-Reference-Cited by-同舟云学术

Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates

Published:2004 Issue:2 Volume:42 Page:61
ISSN:0023-4001
Container-title:The Korean Journal of Parasitology
language:en
Short-container-title:Korean J Parasitol

Author:

Na Byoung-Kuk¹,Lee Eung-Goo¹,Lee Hyeong-Woo²,Cho Shin-Hyeong²,Bae Young-An¹,Kong Yoon¹,Lee Jong-Koo³,Kim Tong-Soo²

Affiliation:

1. Department of Molecular Parasitology and Center for Molecular Medicine Sungkyunkwan University School of Medicine and Samsung Biomedical Research Institute, Suwon 440-746, Korea.

2. Department of Tropical and Endemic Parasitic Diseases, National Institute of Health, Seoul 122-701, Korea.

3. Bureau of Health Promotion, Ministry of Health and Welfare, Gwacheon 427-721, Korea.

Publisher

Korean Society for Parasitology

Subject

Infectious Diseases,Parasitology

Link

http://parasitol.kr/upload/pdf/kjp-42-61.pdf

Reference18 articles.

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

2. Analysis of the Plasmodium vivax apical membrane antigen-1 gene from re-emerging Korean isolates

3. Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets

4. Plasmepsin 4, the food vacuole aspartic proteinase found in all Plasmodium spp. infecting man

5. Identification and Characterization of Falcilysin, a Metallopeptidase Involved in Hemoglobin Catabolism within the Malaria Parasite Plasmodium falciparum

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