PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta
about
PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein BIdentification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping systemPILR and PILR have a siglec fold and provide the basis of binding to sialic acidIREM-1 is a novel inhibitory receptor expressed by myeloid cellsmSiglec-E, a novel mouse CD33-related siglec (sialic acid-binding immunoglobulin-like lectin) that recruits Src homology 2 (SH2)-domain-containing protein tyrosine phosphatases SHP-1 and SHP-2Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptorAn essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR)The myeloid receptor PILRβ mediates the balance of inflammatory responses through regulation of IL-27 productionAlzheimer's Disease Risk Polymorphisms Regulate Gene Expression in the ZCWPW1 and the CELF1 Loci.Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains. Critical roles of residues beyond the pY+3 position.Temporal induction of immunoregulatory processes coincides with age-dependent resistance to viral-induced type 1 diabetesModulation of paired immunoglobulin-like type 2 receptor signaling alters the host response to Staphylococcus aureus-induced pneumoniaIdentification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs.Extraordinary variation in a diversified family of immune-type receptor genesA single-amino-acid substitution in herpes simplex virus 1 envelope glycoprotein B at a site required for binding to the paired immunoglobulin-like type 2 receptor alpha (PILRalpha) abrogates PILRalpha-dependent viral entry and reduces pathogenesisEvolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands.Survey of the year 2000 commercial optical biosensor literature.Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: duplication, conversion, and the birth of new genes.Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor alpha (PILRalpha).Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha.Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry.Molecular evidence for increased expression of genes related to immune and chaperone function in the prefrontal cortex in schizophrenia.Paired Ig-Like Type 2 Receptor-Derived Agonist Ligands Ameliorate Inflammatory Reactions by Downregulating β1 Integrin Activity.Cross-regulation between herpesviruses and the TNF superfamily membersDAP10- and DAP12-associated receptors in innate immunity.Immune inhibitory receptors: essential regulators of phagocyte function.Regulation of neutrophil functions through inhibitory receptors: an emerging paradigm in health and disease.Nonmuscle myosin heavy chain IIb mediates herpes simplex virus 1 entryInitial Contact: The First Steps in Herpesvirus Entry.Deoxynivalenol- and zearalenone-contaminated feeds alter gene expression profiles in the livers of piglets.Alzheimer disease (AD) specific transcription, DNA methylation and splicing in twenty AD associated lociThe Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion.Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion.Biophysical characterization of O-glycosylated CD99 recognition by paired Ig-like type 2 receptors.A mega-analysis of expression quantitative trait loci (eQTL) provides insight into the regulatory architecture of gene expression variation in liver.Negative regulation of DSS-induced experimental colitis by PILRα.
P2860
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P248
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P2860
PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@ast
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en-gb
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@nl
type
label
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@ast
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en-gb
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@nl
prefLabel
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@ast
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en-gb
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@nl
P2093
P2860
P921
P3181
P356
P1476
PILRalpha, a novel immunorecep ...... truncated counterpart PILRbeta
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.275.6.4467
P407
P577
2000-02-11T00:00:00Z