Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum (Q27972941)

1 reference

aminopeptidase P, putative

25 September 2018

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25 September 2018

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19 December 2018

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20 December 2018

Journal of Biological Chemistry

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20 December 2018

Seema Dalal

1

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Michael Klemba

series ordinal

2

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language of work or name

English

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publication date

7 December 2007

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published in

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volume

282

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issue

49

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page(s)

35978-87

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Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems

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Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase

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A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages

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Plasmodium falciparum cysteine protease falcipain-1 is not essential in erythrocytic stage malaria parasites

21 January 2018

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Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum

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Genetic disruption of the Plasmodium falciparum digestive vacuole plasmepsins demonstrates their functional redundancy

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Drug resistance-associated pfCRT mutations confer decreased Plasmodium falciparum digestive vacuolar pH.

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Antimalarials increase vesicle pH in Plasmodium falciparum

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Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin

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A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast

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Proline specific peptidases

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Nutritional requirements of Plasmodium falciparum in culture. I. Exogenously supplied dialyzable components necessary for continuous growth

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