Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes.
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Respiratory health hazards in agricultureDetection of 65 kD heat shock protein in cerebrospinal fluid of tuberculous meningitis patientsAn overview of protein moonlighting in bacterial infection.Porphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats.Comparison of the moonlighting actions of the two highly homologous chaperonin 60 proteins of Mycobacterium tuberculosis.Chaperonin 60 unfolds its secrets of cellular communicationBacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious diseaseMycobacterial 65-kilodalton heat shock protein induces tumor necrosis factor alpha and interleukin 6, reactive nitrogen intermediates, and toxoplasmastatic activity in murine peritoneal macrophagesRole of heat shock proteins in diseases and their therapeutic potential.Spinal TLR4 mediates the transition to a persistent mechanical hypersensitivity after the resolution of inflammation in serum-transferred arthritis.A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection.Heat shock proteins and immune system.Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants.Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases Are Immunogenic, Alter Cytokine Profile and Aid in Intracellular Survival.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.Interleukin-4 inhibits secretion of interleukin-1beta in the response of human cells to mycobacterial heat shock proteins.Cytokine and adhesion molecule expression in human monocytes and endothelial cells stimulated with bacterial heat shock proteins.Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL.Self-heat shock protein 60 induces tumour necrosis factor-alpha in monocyte-derived macrophage: possible role in chronic inflammatory periodontal disease.Do reciprocal interactions between cell stress proteins and cytokines create a new intra-/extra-cellular signalling nexus?Therapeutic vaccine comprising Mycobacterium HSP70.Induction of Porphyromonas gingivalis GroEL signaling via binding to Toll-like receptors 2 and 4.Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures. Implications for its diverse biological activities.
P2860
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P2860
Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@en
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@nl
type
label
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@en
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@nl
prefLabel
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@en
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@nl
P2093
P2860
P1476
Mycobacterial heat-shock prote ...... human mononuclear phagocytes.
@en
P2093
Langermans JA
Peetermans WE
van Furth R
P2860
P304
P356
10.1111/J.1365-3083.1994.TB03421.X
P577
1994-06-01T00:00:00Z