(Q36618429)

English

Long-chain multiple methyl-branched fatty acid-containing lipids of Mycobacterium tuberculosis: biosynthesis, transport, regulation and biological activities

scientific article published on 9 October 2006

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scholarly article

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Europe PubMed Central

PubMed publication ID

15 August 2017

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Europe PubMed Central

Long-chain multiple methyl-branched fatty acid-containing lipids of Mycobacterium tuberculosis: biosynthesis, transport, regulation and biological activities (English)

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Europe PubMed Central

PubMed publication ID

15 August 2017

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Mycobacterium tuberculosis

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methyl-branched fatty acid

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ChEBI release 2020-05-28

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Brigitte Gicquel

3

object named as

Brigitte Gicquel

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object named as

Mary Jackson

1

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author name string

Gustavo Stadthagen

2

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Europe PubMed Central

PubMed publication ID

15 August 2017

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publication date

9 October 2006

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Europe PubMed Central

PubMed publication ID

15 August 2017

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Europe PubMed Central

PubMed publication ID

15 August 2017

87

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Europe PubMed Central

PubMed publication ID

15 August 2017

2

1 reference

Europe PubMed Central

PubMed publication ID

15 August 2017

78-86

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Europe PubMed Central

PubMed publication ID

15 August 2017

The envelope layers of mycobacteria with reference to their pathogenicity.

1 reference

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The dimycocerosate ester polyketide virulence factors of mycobacteria.

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Structural elucidation of a novel family of acyltrehaloses from Mycobacterium tuberculosis

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Occurrence of an antigenic triacyl trehalose in clinical isolates and reference strains of Mycobacterium tuberculosis

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Polyphthienoyl trehalose, glycolipids specific for virulent strains of the tubercle bacillus

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Biochemical function of msl5 (pks8 plus pks17) in Mycobacterium tuberculosis H37Rv: biosynthesis of monomethyl branched unsaturated fatty acids

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A family of diacyltrehaloses isolated from Mycobacterium fortuitum

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Mycobacterium tuberculosis pks12 produces a novel polyketide presented by CD1c to T cells

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Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species

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Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation

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The methyl-branched fortifications of Mycobacterium tuberculosis

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Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis

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Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv

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Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria

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An acyl-CoA synthase (acoas) gene adjacent to the mycocerosic acid synthase (mas) locus is necessary for mycocerosyl lipid synthesis in Mycobacterium tuberculosis var. bovis BCG.

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Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis

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Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice

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Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid

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Inactivation of polyketide synthase and related genes results in the loss of complex lipids in Mycobacterium tuberculosis H37Rv

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Interaction studies on proteins encoded by the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis

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The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis

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Three pathways for trehalose biosynthesis in mycobacteria

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Trehalose is required for growth of Mycobacterium smegmatis

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Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis

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The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis

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Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier

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A glycolipid of hypervirulent tuberculosis strains that inhibits the innate immune response

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Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis

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MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence

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The role of MmpL8 in sulfatide biogenesis and virulence of Mycobacterium tuberculosis

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LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis

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Production of phthiocerol dimycocerosates protects Mycobacterium tuberculosis from the cidal activity of reactive nitrogen intermediates produced by macrophages and modulates the early immune response to infection

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Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the Mycobacterium tuberculosis complex. Evidence that all strains synthesize glycosylated p-hydroxybenzoic methyl esters and that strains devoid of phenolglycolipids harbor a frame

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Molecular dissection of the role of two methyltransferases in the biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the Mycobacterium tuberculosis complex

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p-Hydroxybenzoic acid synthesis in Mycobacterium tuberculosis

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Virulence of selected Mycobacterium tuberculosis clinical isolates in the rabbit model of meningitis is dependent on phenolic glycolipid produced by the bacilli.

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Comparative investigation of the pathogenicity of three Mycobacterium tuberculosis mutants defective in the synthesis of p-hydroxybenzoic acid derivatives

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cDNA-RNA subtractive hybridization reveals increased expression of mycocerosic acid synthase in intracellular Mycobacterium bovis BCG.

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Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling

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SULFOLIPID FROM VIRULENT TUBERCLE BACILLI.

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Sulfolipid deficiency does not affect the virulence of Mycobacterium tuberculosis H37Rv in mice and guinea pigs

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The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis

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VIRULENCE AND MORPHOLOGICAL CHARACTERISTICS OF MAMMALIAN TUBERCLE BACILLI

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Neutral red staining of cells of a sulfolipid-deficient Mycobacterium tuberculosis pks2 mutant proves that sulfolipids are not responsible for this cytochemical reaction

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Virulence attenuation of two Mas-like polyketide synthase mutants of Mycobacterium tuberculosis

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Identifiers

10.1016/J.TUBE.2006.05.003

1 reference

Europe PubMed Central

PubMed publication ID

15 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 August 2017

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