The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics

The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics

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http://www.wikidata.org/entity/Q27641305
Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domainsStructural basis for leucine sensing by the Sestrin2-mTORC1 pathwayStructure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila.Adaptations to High Salt in a Halophilic Protist: Differential Expression and Gene Acquisitions through Duplications and Gene TransfersCrystal structure of alkyl hydroperoxidase D like protein PA0269 from Pseudomonas aeruginosa: homology of the AhpD-like structural family.Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis.Inhibition of Mycobacterium tuberculosis AhpD, an element of the peroxiredoxin defense against oxidative stress.Dihydrophenylalanine: a prephenate-derived Photorhabdus luminescens antibiotic and intermediate in dihydrostilbene biosynthesis.Analysis of the complete genome sequence of Nocardia seriolae UTF1, the causative agent of fish nocardiosis: The first reference genome sequence of the fish pathogenic Nocardia species.The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster.Expression of magA in Legionella pneumophila Philadelphia-1 is developmentally regulated and a marker of formation of mature intracellular forms.Development of new antituberculous agents based on new drug targets and structure-activity relationship.Extracytoplasmic function σ factors of the widely distributed group ECF41 contain a fused regulatory domain.Proteomics of the organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans adapted to tetrachloroethene and other energy substratesThe structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?A novel alkyl hydroperoxidase (AhpD) of Anabaena PCC7120 confers abiotic stress tolerance in Escherichia coli.Insights into organohalide respiration and the versatile catabolism of Sulfurospirillum multivorans gained from comparative genomics and physiological studies.
P2860

The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics

Item
http://www.wikidata.org/entity/Q27641305
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年论文
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name
The mechanism of Mycobacterium ...... crystallography, and kinetics
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The mechanism of Mycobacterium ...... crystallography, and kinetics
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The mechanism of Mycobacterium ...... crystallography, and kinetics
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type
label
The mechanism of Mycobacterium ...... crystallography, and kinetics
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The mechanism of Mycobacterium ...... crystallography, and kinetics
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The mechanism of Mycobacterium ...... crystallography, and kinetics
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prefLabel
The mechanism of Mycobacterium ...... crystallography, and kinetics
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The mechanism of Mycobacterium ...... crystallography, and kinetics
@en
The mechanism of Mycobacterium ...... crystallography, and kinetics
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P1476
P2093
P2860
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P1433
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The mechanism of Mycobacterium ...... crystallography, and kinetics
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P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921