Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development
about
The genome of the sparganosis tapeworm Spirometra erinaceieuropaei isolated from the biopsy of a migrating brain lesionStructural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidaseStructure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidasesX-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparumDistribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolismEvidence for catalytic roles for Plasmodium falciparum aminopeptidase P in the food vacuole and cytosolStereoselective Synthesis of α-Amino-C-phosphinic Acids and DerivativesEssential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellaniiIdentification and Validation of a Potent Dual Inhibitor of the P. falciparum M1 and M17 Aminopeptidases Using Virtual ScreeningInvestigation of the Plasmodium falciparum food vacuole through inducible expression of the chloroquine resistance transporter (PfCRT)Insights into the gene expression profile of uncultivable hemotrophic Mycoplasma suis during acute infection, obtained using proteome analysis.Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors.The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases.Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum.Emerging principles in protease-based drug discovery.Screening the Medicines for Malaria Venture "Malaria Box" against the Plasmodium falciparum aminopeptidases, M1, M17 and M18.Molecular Characterization of Babesia bovis M17 Leucine Aminopeptidase and Inhibition of Babesia Growth by Bestatin.The aminopeptidase inhibitor CHR-2863 is an orally bioavailable inhibitor of murine malaria.Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitorsHeterologous expression of plasmodial proteins for structural studies and functional annotation.The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucineCharacterization of aspartyl aminopeptidase from Toxoplasma gondii.Plasmodium falciparum: new molecular targets with potential for antimalarial drug development.Proteases as regulators of pathogenesis: examples from the Apicomplexa.Dual-functioning antimalarials that inhibit the chloroquine-resistance transporter.The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum.Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation in Trypanosoma brucei.Selective inhibition of PfA-M1, over PfA-M17, by an amino-benzosuberone derivative blocks malaria parasites development in vitro and in vivo.Cloning, purification and preliminary crystallographic analysis of the Helicobacter pylori leucyl aminopeptidase-bestatin complex.Modeling of human M1 aminopeptidases for in silico screening of potential Plasmodium falciparum alanine aminopeptidase (PfA-M1) specific inhibitors.Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum.Characterization of a leucine aminopeptidase of Babesia gibsoni.Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.Characterization of biochemical properties of a selenium-independent glutathione peroxidase of Cryptosporidium parvum.Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.
P2860
Q56595702-483A575E-46C3-458C-AEB7-2E159F787E2FQ59919962-61F0B2E0-DADD-4B15-B463-50955B1CB7AAQ59990910-3B6BC4D5-6EEA-49F3-91C6-08FCEE8E18F2Q59995384-7582E1DE-47FD-4FFF-A911-7A8444919185Q59995411-27AD585E-B316-4FDB-9984-5E01B1343977Q59995420-76B8BDE8-B8F1-4A8E-B27C-DDC176FFEB2DQ61619444-0EABE81E-3B9F-4755-A3A4-8E9D83C35D3A
P1343
Q21146634-F668D825-7865-49FF-8F0E-E4EFDD849A9BQ27653672-C73B1FC6-31BE-465D-8EC9-AEC5CD62AC8FQ27659580-B60119E9-B2B7-4579-8BD9-11A8AD86431EQ27671783-5BC20BE4-F934-4F99-9E7D-A18A437E5320Q27697881-143E8EAA-4D16-4996-A30E-57D361705611Q27972941-0E1ADADB-0414-47C2-A691-E77E0D0557EFQ27973831-F5A0BC1E-4A4C-4402-9F51-18B840A68958Q27974445-8A416E8F-E696-47BC-AAF6-335803C5296AQ28075532-4A31E3CA-D718-465D-8F13-9A2F7FFDB9B0Q28548372-8CA0ECC8-96A9-425E-BC8F-DA7A53E4DA41Q28548496-3C85B374-23FF-4527-87BC-0350CA99215DQ28728498-329A9D92-A089-44D5-BD98-E96769FB1446Q30506460-F2936B70-DB89-4420-B0D1-26E61EB11847Q30932965-C82062A3-C137-4471-A570-F5ABCBE468E4Q34001253-DF139266-6D7F-4099-8024-677F0061324AQ34168471-AF5D5DF8-5F08-4314-B641-FFD0896AB6A3Q34282102-9F145FAA-A1C4-439F-A8A7-6F315D125623Q35564607-BD0AA48A-3F88-4430-B6C2-EC7D855846A6Q35658197-D8ADB33E-722E-43E6-A7DB-C0BF04C0086CQ36018855-E823658E-A051-4F21-AA7C-2CBFCC5C96EFQ36870833-E1E97BB0-6A05-42E8-9D1F-4623EDE16844Q36938795-396535FA-B5DD-48AF-941C-9DD24F989C5EQ37097064-DF9A86B1-02FB-467F-BF61-F28956A5BF34Q37291149-29EBEFBE-2185-4BFE-8D9A-A4C376E3EECDQ37626063-A6C61918-2572-40ED-984F-4EB965EC93E7Q37891227-B45306B3-5DC1-4962-AA82-84F8D5A04D25Q38093645-12961696-55E2-48C7-9740-F78B6443166CQ40180125-B6AC2C5C-AB75-42CA-8030-3222942A1CE8Q41416724-47F28114-BAEB-4F2E-AA4A-EBA4AB7D8757Q41693109-A2DF7235-45E3-4328-8013-BD289A453AAFQ41813823-D7D8E2B5-07FF-485B-8876-374836886AF2Q42038032-385C7FA7-ABB1-4E81-9106-46BD53D0E0A1Q42694678-7A14014C-952F-4C1F-8FEC-EFD3BC15150BQ45956686-76140EF0-132C-4DD8-BAC6-B48E9875320BQ47233305-B2D891D1-68AF-4E39-A366-CBF1B5EF4B84Q50692500-C4E9E052-90AF-4B4F-9A19-C096E7C04A18Q55283527-09BC51A6-7C93-4A7C-99DC-15BDC9C11CAB
P2860
Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Characterization of the Plasmo ...... antimalarial drug development
@ast
Characterization of the Plasmo ...... antimalarial drug development
@en
type
label
Characterization of the Plasmo ...... antimalarial drug development
@ast
Characterization of the Plasmo ...... antimalarial drug development
@en
prefLabel
Characterization of the Plasmo ...... antimalarial drug development
@ast
Characterization of the Plasmo ...... antimalarial drug development
@en
P2093
P2860
P50
P921
P3181
P356
P1476
Characterization of the Plasmo ...... antimalarial drug development
@en
P2093
Artur Mucha
Colin M Stack
Donald L Gardiner
Eithne Cunningham
Franka Teuscher
John P Dalton
Jolanta Grembecka
Jonathan Lowther
Katharine R Trenholme
Pawel Kafarski
P2860
P304
P3181
P356
10.1074/JBC.M609251200
P407
P577
2007-01-19T00:00:00Z