Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.

Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.

Item
http://www.wikidata.org/entity/Q45261036
Structures ofMycobacterium tuberculosisfolylpolyglutamate synthase complexed with ADP and AMPPCPMetabolic network analysis-based identification of antimicrobial drug targets in category A bioterrorism agentsTargeting purine and pyrimidine metabolism in human apicomplexan parasitesComparative genomics of bacterial and plant folate synthesis and salvage: predictions and validationsConcentration-dependent processivity of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetase.para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosisStreptococcus pneumoniae folate biosynthesis responds to environmental CO2 levelsGenetic determinants involved in p-aminosalicylic acid resistance in clinical isolates from tuberculosis patients in northern China from 2006 to 2012An integrated structural proteomics approach along the druggable genome of Corynebacterium pseudotuberculosis species for putative druggable targetsSynthesis of (6R)- and (6S)-5,10-dideazatetrahydrofolate oligo-gamma-glutamates: kinetics of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetasePurification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosisfolylpolyglutamate synthase (MtbFPGS).Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosis.Utility of the Biosynthetic Folate Pathway for Targets in Antimicrobial Discovery.Characterisation of the bifunctional dihydrofolate synthase-folylpolyglutamate synthase from Plasmodium falciparum; a potential novel target for antimalarial antifolate inhibition.A single amino acid substitution in the MurF UDP-MurNAc-pentapeptide synthetase renders Streptococcus pneumoniae dependent on CO2 and temperature.
P2860

Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.

Item
http://www.wikidata.org/entity/Q45261036
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@en
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@nl
type
label
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@en
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@nl
prefLabel
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@en
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Escherichia coli FolC structur ...... et for anti-microbial therapy.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698