Two cutinase-like proteins secreted by Mycobacterium tuberculosis show very different lipolytic activities reflecting their physiological function
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Bacterial Sphingomyelinases and Phospholipases as Virulence FactorsDiscovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosisExperimental Models of Foamy Macrophages and Approaches for Dissecting the Mechanisms of Lipid Accumulation and Consumption during Dormancy and Reactivation of TuberculosisMmPPOX inhibits Mycobacterium tuberculosis lipolytic enzymes belonging to the hormone-sensitive lipase family and alters mycobacterial growthHemolytic phospholipase Rv0183 of Mycobacterium tuberculosis induces inflammatory response and apoptosis in alveolar macrophage RAW264.7 cellsMycobacterium tuberculosis lipolytic enzymes as potential biomarkers for the diagnosis of active tuberculosisLipC (Rv0220) is an immunogenic cell surface esterase of Mycobacterium tuberculosis.Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis.Gene expression profiling of Mycobacterium avium subsp. paratuberculosis in simulated multi-stress conditions and within THP-1 cells reveals a new kind of interactive intramacrophage behaviour.The PE16 (Rv1430) of Mycobacterium tuberculosis is an esterase belonging to serine hydrolase superfamily of proteins.Identification of residues involved in substrate specificity and cytotoxicity of two closely related cutinases from Mycobacterium tuberculosisHeterogeneity among Homologs of Cutinase-Like Protein Cut5 in Mycobacteria.Identification of Mycobacterium avium subsp. hominissuis secreted proteins using an in vitro system mimicking the phagosomal environment.The first structure of a mycobacteriophage, the Mycobacterium abscessus subsp. bolletii phage AraucariaReversible lipid accumulation and associated division arrest of Mycobacterium avium in lipoprotein-induced foamy macrophages may resemble key events during latency and reactivation of tuberculosisRoles of Triolein and Lipolytic Protein in the Pathogenesis and Survival of Mycobacterium tuberculosis: a Novel Therapeutic Approach.Interaction of alveolar epithelial cells with CFP21, a mycobacterial cutinase-like enzyme.Shared characteristics between Mycobacterium tuberculosis and fungi contribute to virulence.Systematic survey of clonal complexity in tuberculosis at a populational level and detailed characterization of the isolates involved.Characterization of a secretory hydrolase from Mycobacterium tuberculosis sheds critical insight into host lipid utilization by M. tuberculosis.The role of red blood cells in enhancing or preventing HIV infection and other diseases.An Invertron-Like Linear Plasmid Mediates Intracellular Survival and Virulence in Bovine Isolates of Rhodococcus equiA honey trap for the treatment of acne: manipulating the follicular microenvironment to control Propionibacterium acnes.Cyclipostins and Cyclophostin analogs as promising compounds in the fight against tuberculosis.Tuberculosis alters pancreatic enzymes in the absence of pancreatitisDetection of potential suberinase-encoding genes in Streptomyces scabiei strains and other actinobacteria.B cells response directed against Cut4 and CFP21 lipolytic enzymes in active and latent tuberculosis infections.Human lysosomal acid lipase inhibitor lalistat impairs Mycobacterium tuberculosis growth by targeting bacterial hydrolasesDelineating the Physiological Roles of the PE and Catalytic Domains of LipY in Lipid Consumption in Mycobacterium-Infected Foamy Macrophages
P2860
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P2860
Two cutinase-like proteins secreted by Mycobacterium tuberculosis show very different lipolytic activities reflecting their physiological function
description
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2010
@ast
im Juni 2010 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/06/01)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/06/01)
@nl
наукова стаття, опублікована в червні 2010
@uk
مقالة علمية (نشرت في يونيو 2010)
@ar
name
Two cutinase-like proteins sec ...... g their physiological function
@ast
Two cutinase-like proteins sec ...... g their physiological function
@en
Two cutinase-like proteins sec ...... g their physiological function
@nl
type
label
Two cutinase-like proteins sec ...... g their physiological function
@ast
Two cutinase-like proteins sec ...... g their physiological function
@en
Two cutinase-like proteins sec ...... g their physiological function
@nl
prefLabel
Two cutinase-like proteins sec ...... g their physiological function
@ast
Two cutinase-like proteins sec ...... g their physiological function
@en
Two cutinase-like proteins sec ...... g their physiological function
@nl
P2093
P3181
P356
P1433
P1476
Two cutinase-like proteins sec ...... g their physiological function
@en
P2093
Damien Maurin
Frédéric Carrière
Gérard Lambeau
Jean-Claude Bakala N'Goma
Mathieu Schué
Rabeb Dhouib
Stéphane Canaan
Vincent Delorme
P304
P3181
P356
10.1096/FJ.09-144766
P407
P577
2010-06-01T00:00:00Z