Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages - Wikidata - awgldk - TriplyDB

Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages

Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages

http://www.wikidata.org/entity/Q28486818

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Identification of Mycobacterium tuberculosis adherence-mediating components: a review of key methods to confirm adhesin function An essential nonredundant role for mycobacterial DnaK in native protein folding Multiple chaperonins in bacteria--novel functions and non-canonical behaviors Mycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2 Physical Features of Intracellular Proteins that Moonlight on the Cell Surface An overview of protein moonlighting in bacterial infection.A PubMed-wide associational study of infectious diseases.Direct visualization by cryo-EM of the mycobacterial capsular layer: a labile structure containing ESX-1-secreted proteins.Proteomic profile of culture filtrate from the Brazilian vaccine strain Mycobacterium bovis BCG Moreau compared to M. bovis BCG Pasteur Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis.Comparison of the moonlighting actions of the two highly homologous chaperonin 60 proteins of Mycobacterium tuberculosis.Streptococcus pneumoniae ClpL modulates adherence to A549 human lung cells through Rap1/Rac1 activation.Enhanced priming of adaptive immunity by Mycobacterium smegmatis mutants with high-level protein secretion.Decrease in penicillin susceptibility due to heat shock protein ClpL in Streptococcus pneumoniae.The francisella tularensis proteome and its recognition by antibodies.Characterization of a novel heat shock protein (Hsp22.5) involved in the pathogenesis of Mycobacterium tuberculosis.Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease Selective enrichment of mycobacterial proteins from infected host macrophages.Systematic review on the proteomic profile of Mycobacterium tuberculosis exposed to drugs.Anaplasma phagocytophilum Asp14 is an invasin that interacts with mammalian host cells via its C terminus to facilitate infection The MprB extracytoplasmic domain negatively regulates activation of the Mycobacterium tuberculosis MprAB two-component system.Technologies for Proteome-Wide Discovery of Extracellular Host-Pathogen Interactions.Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.Non-proteolytic functions of microbial proteases increase pathological complexity.The application of terminomics for the identification of protein start sites and proteoforms in bacteria.Interaction of the CD43 Sialomucin with the Mycobacterium tuberculosis Cpn60.2 Chaperonin Leads to Tumor Necrosis Factor Alpha Production.An analysis of surface proteomics results reveals novel candidates for intracellular/surface moonlighting proteins in bacteria.Dancing to another tune-adhesive moonlighting proteins in bacteria.Secretome profile analysis of hypervirulent Mycobacterium tuberculosis CPT31 reveals increased production of EsxB and proteins involved in adaptation to intracellular lifestyle.Mitochondria chaperone GRP75 moonlighting as a cell cycle controller to derail endocytosis provides an opportunity for nanomicrosphere intracellular delivery.Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.Profiling the surfacome of Staphylococcus aureus.Immunoproteomic identification of 11 novel immunoreactive proteins of Riemerella anatipestifer serotype 2.A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Mycobacterium tuberculosis GroEL2 modulates dendritic cell responses.Identification of Cross Reactive Antigens of C. botulinum Types A, B, E & F by Immunoproteomic Approach.The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.Unraveling Gardnerella vaginalis Surface Proteins Using Cell Shaving Proteomics.

P2860

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P2860

Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages

http://www.wikidata.org/entity/Q28486818

description

2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2009

@ast

im August 2009 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2009/08/01)

@sk

vědecký článek publikovaný v roce 2009

@cs

wetenschappelijk artikel (gepubliceerd op 2009/08/01)

@nl

наукова стаття, опублікована в серпні 2009

@uk

مقالة علمية (نشرت في أغسطس 2009)

@ar

name

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@ast

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@en

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@nl

type

label

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@ast

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@en

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@nl

prefLabel

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@ast

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@en

Mycobacterium tuberculosis Cpn ...... l association with macrophages

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Infection and Immunity

P1476

Mycobacterium tuberculosis Cpn ...... l association with macrophages

@en

P2093

David P. Speert

http://www.w3.org/2001/XMLSchema#string

Lisa M. Thorson

http://www.w3.org/2001/XMLSchema#string

Richard W. Stokes

http://www.w3.org/2001/XMLSchema#string

Tyler B. M. Hickey

http://www.w3.org/2001/XMLSchema#string

P2860

Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells

The glycan-rich outer layer of the cell wall of Mycobacterium tuberculosis acts as an antiphagocytic capsule limiting the association of the bacterium with macrophages

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Genes required for mycobacterial growth defined by high density mutagenesis

The receptor-mediated uptake, survival, replication, and drug sensitivity of Mycobacterium tuberculosis within the macrophage-like cell line THP-1: a comparison with human monocyte-derived macrophages

Dectin-1 is a major beta-glucan receptor on macrophages

Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages

The search for the chaperonin 60 receptors.

Expression of a Mycobacterium tuberculosis arabinomannan antigen in vitro and in vivo

Glucan is a component of the Mycobacterium tuberculosis surface that is expressed in vitro and in vivo.

P304

3389–3401

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scholarly article

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10.1128/IAI.00143-09

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8

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77

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2009-08-01T00:00:00Z

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19470749

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P921

Mycobacterium tuberculosis

P932

2715658

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