Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease
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The therapeutic potential of metal-based antimalarial agents: implications for the mechanism of actionArtemisinin, an Endoperoxide Antimalarial, Disrupts the Hemoglobin Catabolism and Heme Detoxification Systems in Malarial ParasitePotencies of human immunodeficiency virus protease inhibitors in vitro against Plasmodium falciparum and in vivo against murine malariaHemoglobin Digestion in Blood-Feeding Ticks: Mapping a Multipeptidase Pathway by Functional ProteomicsRecombinant Plasmepsin 1 from the Human Malaria Parasite Plasmodium falciparum : Enzymatic Characterization, Active Site Inhibitor Design, and Structural AnalysisA Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradationA role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplastIdentification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparumFour plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine.Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton.Malarial hemozoin: from target to toolThe neutral lipid composition present in the digestive vacuole of Plasmodium falciparum concentrates heme and mediates β-hematin formation with an unusually low activation energy.Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site.Active site contribution to specificity of the aspartic proteases plasmepsins I and II.Antimalarial synergy of cysteine and aspartic protease inhibitors.Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria.Computational perspectives into plasmepsins structure-function relationship: implications to inhibitors design.Order and specificity of the Plasmodium falciparum hemoglobin degradation pathwayPfCRT and the trans-vacuolar proton electrochemical gradient: regulating the access of chloroquine to ferriprotoporphyrin IX.Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase.Schistosomiasis chemotherapy.Chloroquine resistance in the malarial parasite, Plasmodium falciparum.Addressing the malaria drug resistance challenge using flow cytometry to discover new antimalarials.Antimalarial effects of vinyl sulfone cysteine proteinase inhibitors.Safety evaluation of the drugs available to prevent malaria.Defining the morphology and mechanism of the hemoglobin transport pathway in Plasmodium falciparum-infected erythrocytes.Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase.Human antiprotozoal therapy: past, present, and future.Cathepsin Gene Family Reveals Transcriptome Patterns Related to the Infective Stages of the Salmon Louse Caligus rogercresseyi.Phenotypic reversal of the btn1 defects in yeast by chloroquine: a yeast model for Batten disease.Pore size of the malaria parasite's nutrient channelAntimalarial drugs: current status and new developments.Inhibition of hemozoin formation in Plasmodium falciparum trophozoite extracts by heme analogs: possible implication in the resistance to malaria conferred by the beta-thalassemia trait.Inhibitory effects of pepstatin A and mefloquine on the growth of Babesia parasitesGene sequence tags from Plasmodium falciparum genomic DNA fragments prepared by the "genease" activity of mung bean nuclease.Hemoglobin degradation in malaria-infected erythrocytes determined from live cell magnetophoresisProteases of malaria parasites: new targets for chemotherapy.Prodrugs for the treatment of neglected diseases.The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum.Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum.
P2860
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P2860
Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease
description
1991 nî lūn-bûn
@nan
1991 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Hemoglobin degradation in the ...... y a specific aspartic protease
@ast
Hemoglobin degradation in the ...... y a specific aspartic protease
@en
type
label
Hemoglobin degradation in the ...... y a specific aspartic protease
@ast
Hemoglobin degradation in the ...... y a specific aspartic protease
@en
prefLabel
Hemoglobin degradation in the ...... y a specific aspartic protease
@ast
Hemoglobin degradation in the ...... y a specific aspartic protease
@en
P2093
P2860
P921
P356
P1476
Hemoglobin degradation in the ...... y a specific aspartic protease
@en
P2093
P2860
P356
10.1084/JEM.173.4.961
P407
P577
1991-04-01T00:00:00Z