Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases-Reference-Cited by-同舟云学术

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Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases

Published:2011-08-15 Issue:34 Volume:108 Page:E526-E534
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Harbut M. B.,Velmourougane G.,Dalal S.,Reiss G.,Whisstock J. C.,Onder O.,Brisson D.,McGowan S.,Klemba M.,Greenbaum D. C.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference55 articles.

1. The global distribution of clinical episodes of Plasmodium falciparum malaria

2. The pathogenic basis of malaria

3. Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite

4. Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum

5. Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials

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4. Chemoproteomics validates selective targeting of Plasmodium M1 alanyl aminopeptidase as an antimalarial strategy;eLife;2024-07-08

5. Chemoproteomics validates selective targeting of Plasmodium M1 alanyl aminopeptidase as an antimalarial strategy;eLife;2024-07-08

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