Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A
about
SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeCharacterization of SH2D1A missense mutations identified in X-linked lymphoproliferative disease patientsA "three-pronged" binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndromeStructure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cellsCD6 regulates T-cell responses through activation-dependent recruitment of the positive regulator SLP-76The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62dok (Dok1) and activates NF-kappa BResponses to Microbial Challenges by SLAMF ReceptorsFine specificity and molecular competition in SLAM family receptor signallingCIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2Regulation of SLAM-mediated signal transduction by SAP, the X-linked lymphoproliferative gene productInteraction domains: from simple binding events to complex cellular behaviorHematopoietic progenitor kinase 1 associates physically and functionally with the adaptor proteins B cell linker protein and SLP-76 in lymphocytesDual functional roles for the X-linked lymphoproliferative syndrome gene product SAP/SH2D1A in signaling through the signaling lymphocyte activation molecule (SLAM) family of immune receptorsIdentification of UNC119 as a novel activator of SRC-type tyrosine kinasesPSD-95 is a negative regulator of the tyrosine kinase Src in the NMDA receptor complexAssociation between SAP and FynT: Inducible SH3 domain-mediated interaction controlled by engagement of the SLAM receptorSH2 Domains Recognize Contextual Peptide Sequence Information to Determine SelectivityThe adaptor protein SAP directly associates with CD3ζ chain and regulates T cell receptor signaling.Using a phage display library to identify basic residues in A-Raf required to mediate binding to the Src homology 2 domains of the p85 subunit of phosphatidylinositol 3'-kinase.A novel interaction between the SH2 domain of signaling adaptor protein Nck-1 and the upstream regulator of the Rho family GTPase Rac1 engulfment and cell motility 1 (ELMO1) promotes Rac1 activation and cell motility.Novel nonphosphorylated peptides with conserved sequences selectively bind to Grb7 SH2 domain with affinity comparable to its phosphorylated ligand.NTB-A, a new activating receptor in T cells that regulates autoimmune disease.Molecular dissection of 2B4 signaling: implications for signal transduction by SLAM-related receptors.Towards mimicking short linear peptide motifs: identification of new mixed α,β-peptidomimetic ligands for SLAM-Associated Protein (SAP) by confocal on-bead screening.Molecular and immunological basis of X-linked lymphoproliferative disease.SH2 and PTB domains in tyrosine kinase signaling.Characterization of Ly108 in the thymus: evidence for distinct properties of a novel form of Ly108Molecular and cellular pathogenesis of X-linked lymphoproliferative disease.Immune regulation by SLAM family receptors and SAP-related adaptors.NK cell regulation by SLAM family receptors and SAP-related adapters.The role of SLAM family receptors in immune cell signaling.Roles of CD48 in regulating immunity and tolerance.The phosphotyrosine interactome of the insulin receptor family and its substrates IRS-1 and IRS-2.The role of SAP and SLAM family molecules in the humoral immune response.Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Signaling lymphocytic activation molecule (SLAM) regulates T cellular cytotoxicity.DR1769, a protein with N-terminal beta propeller repeats and a low-complexity hydrophilic tail, plays a role in desiccation tolerance of Deinococcus radiodurans.The N-terminal SH2 domains of Syk and ZAP-70 mediate phosphotyrosine-independent binding to integrin beta cytoplasmic domains.SAP and Lessons Learned from a Primary Immunodeficiency.
P2860
Q21245515-C1B78031-43DC-4109-B067-FA81E403B148Q24291489-32B1C813-D3AC-4044-85A2-33FFE91CC470Q24292245-094BB27B-25BA-4E30-A24D-6C10174FD3CDQ24311589-7790CCFC-925D-4794-B02F-7A0A9FA8DF03Q24535874-DE4FA9CD-3385-44BA-B747-C38CA24C8F3EQ24670421-C6B1A0CC-5108-45D7-9ED5-E860249C6F3AQ24681336-8A358918-F743-4C7F-BEE3-36F73AB3328BQ26772707-1B847AB3-CD77-4268-BC93-76D27BE3DB69Q28118752-E69AC770-E51A-4C8A-A85D-6C3F38DD2114Q28140132-BEEFBDFD-B4F7-42DF-AF0A-DA30CD5051F2Q28209604-7F0C6219-D81E-4F22-ADC9-0AC9C9AAEB58Q28209614-9EC1E474-0B8F-43DE-9652-46D5AADEC6C5Q28211046-821ADD72-BB18-44F6-9ADA-11A54BBCB0C2Q28216360-71D01CC4-6099-420F-8479-B91773C56526Q28218689-A15FF1CB-D1E2-4F88-83F9-E509D2F4DCC9Q28512469-76391CA3-FAE3-4EE4-8565-D793BDAF8E23Q28585941-A8BFE5F1-3D7A-454A-B889-2F787D016642Q29038594-A045217F-0C35-44B8-9AFD-F81FD2F88E9BQ30010025-929A6FCB-C6D6-435D-BBF8-C17C2A417CB7Q30914495-D322C95B-CA30-4025-8C4A-E2863EC6A632Q34044748-73C14245-2CBA-45A1-906B-37E1DBCAD78FQ34130780-D1956FE0-CE13-4A1D-8CB5-4401CB766F14Q34301675-C074919F-7661-4642-8DA4-088A4D7B298BQ34345732-895BDFF3-EFD4-4636-A6B4-948CF9E75666Q34531331-6FA8BA12-E86B-4841-BDB7-20311D288D3EQ35096711-FE8ACE0F-FDA6-42AF-9472-62D505F93088Q35178872-D63810FE-BCBD-471A-A831-E5841A53D549Q35851005-5F76C1B6-E938-4660-AFFB-6935D4F3450EQ36015040-2DD01716-5AB2-4D81-919C-00CAE51C5308Q36403407-F5DE68D6-E0A3-4067-B971-7CB0A3510B48Q36652149-2FA140CD-79F4-455B-BB7F-A7D4D253680BQ36704486-74EE68F1-9BE3-4BD0-819F-2751D9575121Q36883146-76CD377D-7F3E-41F1-9B28-1F53CA8026D6Q37113882-DD83DBC1-9853-4357-9EB6-1C31EB1FF061Q37811046-4CEA9668-848E-47D2-BE8B-6B11F11B2548Q38167994-64A5A3C2-A10C-440F-BC89-4C89331AD448Q40782184-02855590-CD67-4853-862B-8F48FFB7817AQ42573437-2A024D8E-CF39-4B9B-A3F6-744E0AF9937AQ44097443-858FDB98-055F-4B36-B519-F1AAACA58976Q48208098-F8421AD9-83E7-482E-867A-064CC881281C
P2860
Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@ast
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@en
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@nl
type
label
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@ast
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@en
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@nl
prefLabel
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@ast
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@en
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@nl
P2093
P1433
P1476
Novel mode of ligand binding b ...... isease gene product SAP/SH2D1A
@en
P2093
A J Coffey
J D Forman-Kay
P304
P356
10.1016/S0960-9822(00)80080-9
P407
P577
1999-12-02T00:00:00Z