para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis - Wikidata - awgldk - TriplyDB

para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis

para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q34351796

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Evolution of drug resistance in tuberculosis: recent progress and implications for diagnosis and therapy Mycobacterium tuberculosis folate metabolism and the mechanistic basis for para-aminosalicylic acid susceptibility and resistance Mycobacterial dihydrofolate reductase inhibitors identified using chemogenomic methods and in vitro validation New antimycobacterial agents in the pre-clinical phase or beyond: recent advances in patent literature (2001-2016).New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria Pharmacokinetics of para-aminosalicylic acid in HIV-uninfected and HIV-coinfected tuberculosis patients receiving antiretroviral therapy, managed for multidrug-resistant and extensively drug-resistant tuberculosis.Genetic determinants involved in p-aminosalicylic acid resistance in clinical isolates from tuberculosis patients in northern China from 2006 to 2012 Mycobacterium tuberculosis metabolism Opposing effects of target overexpression reveal drug mechanisms Serum protein gamma-glutamyl hydrolase, Ig gamma-3 chain C region, and haptoglobin are associated with the syndromes of pulmonary tuberculosis in traditional Chinese medicine.A Focused Screen Identifies Antifolates with Activity on Mycobacterium tuberculosis.Mutations in genes for the F420 biosynthetic pathway and a nitroreductase enzyme are the primary resistance determinants in spontaneous in vitro-selected PA-824-resistant mutants of Mycobacterium tuberculosis Mycobacterium tuberculosis Arylamine N-Acetyltransferase Acetylates and Thus Inactivates para-Aminosalicylic Acid Targeting intracellular p-aminobenzoic acid production potentiates the anti-tubercular action of antifolates.Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosis.Characterizing the pocketome of Mycobacterium tuberculosis and application in rationalizing polypharmacological target selection.Deletion of sigB Causes Increased Sensitivity to para-Aminosalicylic Acid and Sulfamethoxazole in Mycobacterium tuberculosis.Antibiotic resistance mechanisms in M. tuberculosis: an update.Reversion of antibiotic resistance in Mycobacterium tuberculosis by spiroisoxazoline SMARt-420.Bioluminescence for assessing drug potency against nonreplicating Mycobacterium tuberculosis.Anti-folates potentiate bactericidal effects of other antimicrobial agents.Antimycobacterial Metabolism: Illuminating Mycobacterium tuberculosis Biology and Drug Discovery.In Silico Prediction of Antibiotic Resistance in Mycobacterium ulcerans Agy99 through Whole Genome Sequence Analysis.Evaluation of para-Aminosalicylic Acid as a Substrate of Multiple Solute Carrier Uptake Transporters and Possible Drug Interactions with Nonsteroidal Anti-inflammatory Drugs In Vitro.dfrA thyA Double Deletion in para-Aminosalicylic Acid-Resistant Mycobacterium tuberculosis Beijing Strains.Comparative Genomic Analysis of Two Clonally Related Multidrug Resistant Mycobacterium tuberculosis by Single Molecule Real Time Sequencing.Phylogenomics and antimicrobial resistance of the leprosy bacillus Mycobacterium leprae.Update of Antitubercular Prodrugs from a Molecular Perspective: Mechanisms of Action, Bioactivation Pathways, and Associated Resistance.Updated and standardized genome-scale reconstruction of Mycobacterium tuberculosis H37Rv, iEK1011, simulates flux states indicative of physiological conditions.Machine learning and structural analysis of Mycobacterium tuberculosis pan-genome identifies genetic signatures of antibiotic resistance Mycobacterial Cell Wall Synthesis Inhibitors Cause Lethal ATP Burst

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para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis

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2013 nî lūn-bûn

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P2860

Erasing the World's Slow Stain: Strategies to Beat Multidrug-Resistant Tuberculosis

Tuberculosis and trimethoprim-sulfamethoxazole

Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs

Structures ofMycobacterium tuberculosisfolylpolyglutamate synthase complexed with ADP and AMPPCP

Biochemical and structural characterization of the putative dihydropteroate synthase ortholog Rv1207 of Mycobacterium tuberculosis

Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase

Genes required for mycobacterial growth defined by high density mutagenesis

Para-aminosalicylic acid in the treatment of tuberculosis

Evaluating the sensitivity of Mycobacterium tuberculosis to biotin deprivation using regulated gene expression

Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli

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Mycobacterium tuberculosis

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