Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin - Test2 - elhamkhani - TriplyDB

Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

http://www.wikidata.org/entity/Q27690745

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Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases Structural and functional attributes of malaria parasite diadenosine tetraphosphate hydrolase.Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase Crystal structures of Entamoeba histolytica lysyl-tRNA synthetase reveal conformational changes upon lysine binding and a specific helix bundle domain Protein Translation Enzyme lysyl-tRNA Synthetase Presents a New Target for Drug Development against Causative Agents of Loiasis and Schistosomiasis Three-dimensional structures in the design of therapeutics targeting parasitic protozoa: reflections on the past, present and future.A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens.Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP Competitive Inhibitor.Natural products as probes in pharmaceutical research.Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts.Production of New Cladosporin Analogues by Reconstitution of the Polyketide Synthases Responsible for the Biosynthesis of this Antimalarial Agent.Genetic Validation of Leishmania donovani Lysyl-tRNA Synthetase Shows that It Is Indispensable for Parasite Growth and Infectivity.The growing pipeline of natural aminoacyl-tRNA synthetase inhibitors for malaria treatment.Using in Vitro Evolution and Whole Genome Analysis To Discover Next Generation Targets for Antimalarial Drug Discovery.Evaluation of Current and Emerging Antimalarial Medicines for Inhibition of Toxoplasma gondii Growth in Vitro

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P2860

Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

http://www.wikidata.org/entity/Q27690745

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2014 nî lūn-bûn

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2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Journal of Structural and Functional Genomics

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Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin

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Amit Sharma

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Hassan Belrhali

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Sameena Khan

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P2860

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation

Crystal Structure of Soluble Domain of Malaria Sporozoite Protein UIS3 in Complex with Lipid

Crystal Structure of Malaria Parasite Nucleosome Assembly Protein: DISTINCT MODES OF PROTEIN LOCALIZATION AND HISTONE RECOGNITION

Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses

Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design

An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase

Structural analysis of malaria-parasite lysyl-tRNA synthetase provides a platform for drug development

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Manickam Yogavel

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