The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
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Antimicrobial mechanism of action of transferrins: selective inhibition of H+-ATPaseStructure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.Variations of Subunit of the Mycobacterium tuberculosis F1Fo ATP Synthase and a Novel Model for Mechanism of Action of the Tuberculosis Drug TMC207Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthaseDiarylquinolines target subunit c of mycobacterial ATP synthaseDelayed bactericidal response of Mycobacterium tuberculosis to bedaquiline involves remodelling of bacterial metabolism.High-resolution definition of the Vibrio cholerae essential gene set with hidden Markov model-based analyses of transposon-insertion sequencing dataPolymyxin B identified as an inhibitor of alternative NADH dehydrogenase and malate: quinone oxidoreductase from the Gram-positive bacterium Mycobacterium smegmatis.The low-affinity phosphate transporter PitA is dispensable for in vitro growth of Mycobacterium smegmatisUnique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia.An obligately aerobic soil bacterium activates fermentative hydrogen production to survive reductive stress during hypoxia.A Mycobacterium tuberculosis cytochrome bd oxidase mutant is hypersensitive to bedaquiline.Analysis of intracellular expressed proteins of Mycobacterium tuberculosis clinical isolates.Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria.The alanine racemase of Mycobacterium smegmatis is essential for growth in the absence of D-alanineMenaquinone synthesis is critical for maintaining mycobacterial viability during exponential growth and recovery from non-replicating persistencePhysiology of mycobacteriaThe Mycobacterium tuberculosis MEP (2C-methyl-d-erythritol 4-phosphate) pathway as a new drug target.Energy metabolism and drug efflux in Mycobacterium tuberculosisBedaquiline - The first ATP synthase inhibitor against multi drug resistant tuberculosis.Oxidative Phosphorylation as a Target Space for Tuberculosis: Success, Caution, and Future Directions.Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis.Targeting Energy Metabolism in Mycobacterium tuberculosis, a New Paradigm in Antimycobacterial Drug Discovery.Novel antibiotics targeting respiratory ATP synthesis in Gram-positive pathogenic bacteria.Bactericidal mode of action of bedaquiline.The ATP synthase inhibitor bedaquiline interferes with small-molecule efflux in Mycobacterium smegmatis.Three different [NiFe] hydrogenases confer metabolic flexibility in the obligate aerobe Mycobacterium smegmatis.A structure-based strategy toward the development of novel candidates for antimycobacterial activity: Synthesis, biological evaluation, and docking study.Mycobacterial Membrane Proteins QcrB and AtpE: Roles in Energetics, Antibiotic Targets, and Associated Mechanisms of Resistance.Bioenergetics of Mycobacterium: An Emerging Landscape for Drug Discovery.Emerging drugs and drug targets against tuberculosis.
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P2860
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@en
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@nl
type
label
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@en
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@nl
prefLabel
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@en
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@nl
P2860
P1476
The F1Fo-ATP synthase of Mycobacterium smegmatis is essential for growth.
@en
P2093
Gregory M Cook
Sieu L Tran
P2860
P304
P356
10.1128/JB.187.14.5023-5028.2005
P577
2005-07-01T00:00:00Z