Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q34645537

about

HDP-a novel heme detoxification protein from the malaria parasite Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum.Transition-state inhibitors of purine salvage and other prospective enzyme targets in malaria Identification of Chalcones as Fasciola hepatica Cathepsin L Inhibitors Using a Comprehensive Experimental and Computational Approach Asparagine requirement in Plasmodium berghei as a target to prevent malaria transmission and liver infections.Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in blood-stage Plasmodium falciparum Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.Synthesis of New (−)-Bestatin-Based Inhibitor Libraries Reveals a Novel Binding Mode in the S1 Pocket of the Essential Malaria M1 Metalloaminopeptidase Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum Protein complex directs hemoglobin-to-hemozoin formation in Plasmodium falciparum Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism The glutathione biosynthetic pathway of Plasmodium is essential for mosquito transmission Mining a cathepsin inhibitor library for new antiparasitic drug leads The Plasmodium falciparum malaria M1 alanyl aminopeptidase (PfA-M1): insights of catalytic mechanism and function from MD simulations A process similar to autophagy is associated with cytocidal chloroquine resistance in Plasmodium falciparum Metabolic QTL analysis links chloroquine resistance in Plasmodium falciparum to impaired hemoglobin catabolism Disulfide linkages in Plasmodium falciparum plasmepsin-i are essential elements for its processing activity and multi-milligram recombinant production yield Synergistic Malaria Parasite Killing by Two Types of Plasmodial Surface Anion Channel Inhibitors Enzymatic Characterization of Recombinant Food Vacuole Plasmepsin 4 from the Rodent Malaria Parasite Plasmodium berghei Symbiosis as an adaptive process and source of phenotypic complexity Branched tricarboxylic acid metabolism in Plasmodium falciparum Identification of inhibitors that dually target the new permeability pathway and dihydroorotate dehydrogenase in the blood stage of Plasmodium falciparum Cationic amino acid transporters play key roles in the survival and transmission of apicomplexan parasites A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast Plasmodium falciparum Maf1 Confers Survival upon Amino Acid Starvation PfPI3K, a phosphatidylinositol-3 kinase from Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking Esterase mutation is a mechanism of resistance to antimalarial compounds Validation of isoleucine utilization targets in Plasmodium falciparum Characterization of the chloroquine resistance transporter homologue in Toxoplasma gondii Gene disruption of Plasmodium falciparum p52 results in attenuation of malaria liver stage development in cultured primary human hepatocytes.Hemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3.Characterisation of hydrazides and hydrazine derivatives as novel aspartic protease inhibitors.A cell-based high-throughput screen validates the plasmodial surface anion channel as an antimalarial target.Plasmepsin 4-deficient Plasmodium berghei are virulence attenuated and induce protective immunity against experimental malaria.Antimalarial activity of azadipeptide nitriles Antimalarial drug targets in Plasmodium falciparum predicted by stage-specific metabolic network analysis Predictive Genomic Analyses Inform the Basis for Vitamin Metabolism and Provisioning in Bacteria-Arthropod Endosymbioses Uptake and metabolism of arginine impact Plasmodium development in the liver

P2860

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P2860

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

http://www.wikidata.org/entity/Q34645537

description

2006 nî lūn-bûn

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2006 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2006 թվականի մայիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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Plasmodium falciparum ensures ...... ant proteolytic enzyme systems

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Plasmodium falciparum ensures ...... ant proteolytic enzyme systems

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Plasmodium falciparum ensures ...... ant proteolytic enzyme systems

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PNAS.0601876103

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Plasmodium falciparum ensures ...... ant proteolytic enzyme systems

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P2093

Daniel E Goldberg

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Eva S Istvan

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Ilya Y Gluzman

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Julia Gross

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Jun Liu

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P2860

Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3

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

Retention and loss of amino acid biosynthetic pathways based on analysis of whole-genome sequences.

Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents.

A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum.

Amino acid metabolism and protein synthesis in malarial parasites

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

SERUM AMINO ACIDS IN KWASHIORKOR. I. RELATIONSHIP TO CLINICAL CONDITION.

Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum.

Inhibition of the peroxidative degradation of haem as the basis of action of chloroquine and other quinoline antimalarials

P304

8840-8845

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10.1073/PNAS.0601876103

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23

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103

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7050490

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16731623

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P921

Plasmodium falciparum

P932

1470969

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