gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection.
about
Emerging and Novel Functions of Complement Protein C1qSOCS1 and SOCS3 are targeted by hepatitis C virus core/gC1qR ligation to inhibit T-cell functionDifferential regulation of SOCS-1 signalling in B and T lymphocytes by hepatitis C virus core proteinRole of the Receptor for the Globular Domain of C1q Protein in the Pathogenesis of Hepatitis C Virus-Related Cryoglobulin Vascular DamageStructure of the T. brucei p22 protein, a cytochrome oxidase subunit II (COII) specific RNA editing accessory factorTim-3 negatively regulates IL-12 expression by monocytes in HCV infection.Direct binding of hepatitis C virus core to gC1qR on CD4+ and CD8+ T cells leads to impaired activation of Lck and Akt.Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol.Hepatic gene expression profiling reveals protective responses in Atlantic salmon vaccinated against furunculosisHIV gp41 engages gC1qR on CD4+ T cells to induce the expression of an NK ligand through the PIP3/H2O2 pathway.C1QBP suppresses cell adhesion and metastasis of renal carcinoma cellsEvidence that a C1q/C1qR system regulates monocyte-derived dendritic cell differentiation at the interface of innate and acquired immunity.beta 1 Integrin-dependent cell adhesion to EMILIN-1 is mediated by the gC1q domain.A gC1qR prevents white spot syndrome virus replication in the freshwater crayfish Pacifastacus leniusculusSpecific interactions between gC1qR and alpha1-adrenoceptor subtypes.gC1qR/p33 blockade reduces Staphylococcus aureus colonization of target tissues in an animal model of infective endocarditisCell-surface receptor for complement component C1q (gC1qR) is a key regulator for lamellipodia formation and cancer metastasis.Structure-function studies using deletion mutants identify domains of gC1qR/p33 as potential therapeutic targets for vascular permeability and inflammation.The mitochondrial protein C1qbp promotes cell proliferation, migration and resistance to cell death.Genetic analysis in Drosophila reveals a role for the mitochondrial protein p32 in synaptic transmissionStructural and functional anatomy of the globular domain of complement protein C1q.The C1q family of proteins: insights into the emerging non-traditional functionsProteomic Profile of Brucella abortus-Infected Bovine Chorioallantoic Membrane Explants.The contribution of gC1qR/p33 in infection and inflammationgC1qR expression in normal and pathologic human tissues: differential expression in tissues of epithelial and mesenchymal origin.Cytoadhesion to gC1qR through Plasmodium falciparum Erythrocyte Membrane Protein 1 in Severe Malaria.Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death.Crosstalk between the alpha2beta1 integrin and c-met/HGF-R regulates innate immunityEpstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.Soluble gC1qR in Blood and Body Fluids: Examination in a Pancreatic Cancer Patient Cohort.Pancreatic expression and mitochondrial localization of the progestin-adipoQ receptor PAQR10.A proteomic approach to identification of plutonium-binding proteins in mammalian cellsThe exosporium of B. cereus contains a binding site for gC1qR/p33: implication in spore attachment and/or entry.Platelet mediated complement activationIdentification of the gC1qR sites for the HIV-1 viral envelope protein gp41 and the HCV core protein: Implications in viral-specific pathogenesis and therapy.Analysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR.Complement Protein C1q Interacts with DC-SIGN via Its Globular Domain and Thus May Interfere with HIV-1 Transmission.Targeting and crossing of the human maternofetal barrier by Listeria monocytogenes: role of internalin interaction with trophoblast E-cadherin.Rubella virus capsid protein: a small protein with big functions.Mechanisms of oral bacteria-induced platelet activation.
P2860
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P2860
gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection.
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@ast
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@en
type
label
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@ast
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@en
prefLabel
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@ast
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@en
P2093
P1476
gC1q-R/p33, a member of a new ...... in inflammation and infection.
@en
P2093
P356
10.1034/J.1600-065X.2001.1800106.X
P577
2001-04-01T00:00:00Z