Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages
about
Hsp60-mediated T cell stimulation is independent of TLR4 and IL-12OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADStructures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperonesSpatiotemporal Regulation of Hsp90-Ligand Complex Leads to Immune ActivationHeat Shock Protein-Peptide and HSP-Based Immunotherapies for the Treatment of CancerGARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasingHeat Shock Proteins: A Review of the Molecular Chaperones for Plant ImmunityGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumIntracellular nucleic acid sensors and autoimmunityRegulatory functions of innate-like B cellsNucleic acids and endosomal pattern recognition: how to tell friend from foe?The Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsEndoplasmic reticulum stress in hepatic steatosis and inflammatory bowel diseasesTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingParalog-selective Hsp90 inhibitors define tumor-specific regulation of HER2Cellular stress response and innate immune signaling: integrating pathways in host defense and inflammation.The role of pattern-recognition receptors in innate immunity: update on Toll-like receptorsClients and Oncogenic Roles of Molecular Chaperone gp96/grp94Update on Inflammatory Biomarkers and Treatments in Ischemic StrokeRole of IGF-I signaling in muscle bone interactionsTarget identification by image analysisMapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Murine but not human basophil undergoes cell-specific proteolysis of a major endoplasmic reticulum chaperoneIdentification of new protein interactions between dengue fever virus and its hosts, human and mosquitoExploring the Functional Complementation between Grp94 and Hsp90CD14 controls the LPS-induced endocytosis of Toll-like receptor 4Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidaseRegulation of Toll-like receptor 2 interaction with Ecgp96 controls Escherichia coli K1 invasion of brain endothelial cellsDifferential contribution of beta-adrenergic receptors expressed on radiosensitive versus radioresistant cells to protection against inflammation and mortality in murine endotoxemiaGRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion.Toll-like receptors: structural pieces of a curve-shaped puzzle.Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex.Heat-shock responsive genes identified and validated in Atlantic cod (Gadus morhua) liver, head kidney and skeletal muscle using genomic techniques.Overexpression of the endoplasmic reticulum chaperone BiP3 regulates XA21-mediated innate immunity in rice.Heat shock protein 96 is elevated in rheumatoid arthritis and activates macrophages primarily via TLR2 signaling.Global survey of protein expression during gonadal sex determination in miceGp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control.Inhibition of inducible nitric oxide controls pathogen load and brain damage by enhancing phagocytosis of Escherichia coli K1 in neonatal meningitisThe endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis.
P2860
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P2860
Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Heat shock protein gp96 is a m ...... innate function of macrophages
@ast
Heat shock protein gp96 is a m ...... innate function of macrophages
@en
Heat shock protein gp96 is a m ...... innate function of macrophages
@nl
type
label
Heat shock protein gp96 is a m ...... innate function of macrophages
@ast
Heat shock protein gp96 is a m ...... innate function of macrophages
@en
Heat shock protein gp96 is a m ...... innate function of macrophages
@nl
prefLabel
Heat shock protein gp96 is a m ...... innate function of macrophages
@ast
Heat shock protein gp96 is a m ...... innate function of macrophages
@en
Heat shock protein gp96 is a m ...... innate function of macrophages
@nl
P2093
P2860
P921
P3181
P1433
P1476
Heat shock protein gp96 is a m ...... innate function of macrophages
@en
P2093
David J Zammit
Leo Lefrançois
Pramod K Srivastava
P2860
P304
P3181
P356
10.1016/J.IMMUNI.2006.12.005
P407
P577
2007-02-01T00:00:00Z