Mycobacterium smegmatis D-Alanine Racemase Mutants Are Not Dependent on D-Alanine for Growth.
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Structure of the Mycobacterium tuberculosis D-Alanine:D-Alanine Ligase, a Target of the Antituberculosis Drug D-CycloserineThe crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug designA point mutation in cycA partially contributes to the D-cycloserine resistance trait of Mycobacterium bovis BCG vaccine strainsAll four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasisGeneration and screening of a comprehensive Mycobacterium avium subsp. paratuberculosis transposon mutant bank.Mass spectrometry of the M. smegmatis proteome: protein expression levels correlate with function, operons, and codon bias.Use of the alr gene as a food-grade selection marker in lactic acid bacteriaExtensively Drug-Resistant Tuberculosis: A Sign of the Times and an Impetus for Antimicrobial Discovery.The alanine racemase of Mycobacterium smegmatis is essential for growth in the absence of D-alanineIdentifying feasible metabolic routes in Mycobacterium smegmatis and possible alterations under diverse nutrient conditions.Predicting the in vivo mechanism of action for drug leads using NMR metabolomicsMetabolomics analysis identifies d-Alanine-d-Alanine ligase as the primary lethal target of d-Cycloserine in mycobacteriaMolecular basis underlying Mycobacterium tuberculosis D-cycloserine resistance. Is there a role for ubiquinone and menaquinone metabolic pathways?Development of cyclobutene- and cyclobutane-functionalized fatty acids with inhibitory activity against Mycobacterium tuberculosis.Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for proficient utilization of alanine as a sole nitrogen source and sustained anaerobic growth.Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine.A Kinetic Study of In Vitro Lysis of Mycobacterium smegmatis.Addressing the Challenges of Tuberculosis: A Brief Historical Account.Use of NMR metabolomics to analyze the targets of D-cycloserine in mycobacteria: role of D-alanine racemase.Overexpression of a newly identified d-amino acid transaminase in Mycobacterium smegmatis complements glutamate racemase deletion.Knockout of the alanine racemase gene in Aeromonas hydrophila HBNUAh01 results in cell wall damage and enhanced membrane permeability.Auxotrophy to Xeno-DNA: an exploration of combinatorial mechanisms for a high-fidelity biosafety system for synthetic biology applications
P2860
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P2860
Mycobacterium smegmatis D-Alanine Racemase Mutants Are Not Dependent on D-Alanine for Growth.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@en
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@nl
type
label
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@en
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@nl
prefLabel
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@en
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@nl
P2093
P2860
P1476
Mycobacterium smegmatis D-Alan ...... ndent on D-Alanine for Growth.
@en
P2093
L Garry Adams
N Beth Harris
Nancy E Cáceres
Ofelia Chacon
Raúl G Barletta
Zhengyu Feng
P2860
P356
10.1128/AAC.46.2.47-54.2002
P407
P577
2002-01-01T00:00:00Z