CD22 associates with the human surface IgM-B-cell antigen receptor complex
about
Tyrosine phosphorylation of a human killer inhibitory receptor recruits protein tyrosine phosphatase 1CCD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activationPhospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for SykHuman spleen tyrosine kinase p72Syk associates with the Src-family kinase p53/56Lyn and a 120-kDa phosphoproteinInhibition of the B cell by CD22: a requirement for LynSiglecs in the immune systemSiglecs as sensors of self in innate and adaptive immune responsesCD22 and Siglec-G in B cell function and toleranceSialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domainsCD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium fluxSHP-1 requires inhibitory co-receptors to down-modulate B cell antigen receptor-mediated phosphorylation of cellular substratesCD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1CD22: an inhibitory enigmaAnalysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signalingIn situ trans ligands of CD22 identified by glycan-protein photocross-linking-enabled proteomics.New functions for the sialic acid-binding adhesion molecule CD22, a member of the growing family of Siglecs.Regulation of CD45 engagement by the B-cell receptor CD22.Ig beta tyrosine residues contribute to the control of B cell receptor signaling by regulating receptor internalization.CD19, CD21, and CD22: multifaceted response regulators of B lymphocyte signal transduction.Molecular mechanisms for apoptosis induced by signaling through the B cell antigen receptor.ST6Gal-I restrains CD22-dependent antigen receptor endocytosis and Shp-1 recruitment in normal and pathogenic immune signalingThe alpha/beta sheath and its cytoplasmic tyrosines are required for signaling by the B-cell antigen receptor but not for capping or for serine/threonine-kinase recruitment.Revenge of the microbes. Superantigens of the T and B cell lineageEnhancement and suppression of signaling by the conserved tail of IgG memory-type B cell antigen receptorsAn extracatalytic function of CD45 in B cells is mediated by CD22.Deficiency in CD22, a B cell-specific inhibitory receptor, is sufficient to predispose to development of high affinity autoantibodies.Bispecific anti-CD20/22 antibodies inhibit B-cell lymphoma proliferation by a unique mechanism of action.Immune regulation by the ST6Gal sialyltransferase.Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes.Internalization of rituximab and the efficiency of B Cell depletion in rheumatoid arthritis and systemic lupus erythematosusNanoscale organization and dynamics of the siglec CD22 cooperate with the cytoskeleton in restraining BCR signalling.Sialic acids and autoimmune disease.CD19 and CD22 expression reciprocally regulates tyrosine phosphorylation of Vav protein during B lymphocyte signaling.CD22 expression mediates the regulatory functions of peritoneal B-1a cells during the remission phase of contact hypersensitivity reactionsRegulation of B-cell entry into the cell cycleDendritic cell-dependent inhibition of B cell proliferation requires CD22CD22 and autoimmune disease.The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22.Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding.
P2860
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P2860
CD22 associates with the human surface IgM-B-cell antigen receptor complex
description
1993 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 1993
@ast
im April 1993 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1993/04/15)
@sk
vědecký článek publikovaný v roce 1993
@cs
wetenschappelijk artikel (gepubliceerd op 1993/04/15)
@nl
наукова стаття, опублікована у квітні 1993
@uk
name
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@ast
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@en
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@nl
type
label
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@ast
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@en
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@nl
prefLabel
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@ast
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@en
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@nl
P2093
P2860
P356
P1476
CD22 associates with the human surface IgM-B-cell antigen receptor complex
@en
P2093
C. Leprince
E. A. Clark
J. A. Ledbetter
K. E. Draves
R. L. Geahlen
P2860
P304
P356
10.1073/PNAS.90.8.3236
P407
P577
1993-04-15T00:00:00Z