Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1.
about
The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreadingThe Structure of the Tiam1 PDZ Domain/ Phospho-Syndecan1 Complex Reveals a Ligand Conformation that Modulates Protein DynamicsConstitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzymeProtein kinase C delta and eta isoenzymes control the shedding of the interleukin 6 receptor alpha in myeloma cellsVanadate from air pollutant inhibits hrs-dependent endosome fusion and augments responsiveness to toll-like receptorsInhibition of PDGF-B induction and cell growth by syndecan-1 involves the ubiquitin and SUMO-1 ligase, ToporsSyndecan-1 - A new piece in B-cell puzzle.Syndecans and the lymphoid system.PTPIP51 in protein interactions: regulation and in situ interacting partners.Regulation of syndecan-4 phosphorylation in vivo.Shed Syndecan-1 is involved in chemotherapy resistance via the EGFR pathway in colorectal cancerHeparan sulfate chains of syndecan-1 regulate ectodomain shedding.Large-scale phosphotyrosine proteomic profiling of rat renal collecting duct epithelium reveals predominance of proteins involved in cell polarity determination.Molecular and cellular mechanisms of ectodomain sheddingShedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase.Constitutive and accelerated shedding of murine syndecan-1 is mediated by cleavage of its core protein at a specific juxtamembrane siteThe syndecan family of proteoglycans. Novel receptors mediating internalization of atherogenic lipoproteins in vitro.The heparanase/syndecan-1 axis in cancer: mechanisms and therapies.The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading.Tyrosine dephosphorylation of the syndecan-1 PDZ binding domain regulates syntenin-1 recruitment.Syndecan-1 ectodomain shedding is regulated by the small GTPase Rab5Role of tyrosine phosphorylation in the regulation of cleavage secretion of angiotensin-converting enzyme.Signals mediating cleavage of intercellular adhesion molecule-1.Syndecan-1 transmembrane and extracellular domains have unique and distinct roles in cell spreading.Noncompetitive, chemokine-mediated inhibition of basic fibroblast growth factor-induced endothelial cell proliferation.Chemotherapy stimulates syndecan-1 shedding: a potentially negative effect of treatment that may promote tumor relapseMechanical strain regulates syndecan-4 expression and shedding in smooth muscle cells through differential activation of MAP kinase signaling pathways.Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin.The myeloma cell antigen syndecan-1 is lost by apoptotic myeloma cells.Characterization of potential CD138 negative myeloma "stem cells".Syndecan 3 intramembrane proteolysis is presenilin/gamma-secretase-dependent and modulates cytosolic signaling.The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1.Syndecan-4 is a signaling molecule for stromal cell-derived factor-1 (SDF-1)/ CXCL12.Dually modified transmembrane proteoglycans in development and disease.
P2860
Q24669779-2F9B5A9B-D068-492D-9EC7-27F2EC01B89FQ27676266-B67F567F-5723-4FA2-BE7A-FEFF50D5671FQ28344424-B3D87B2A-8AB1-4E9F-9585-A50AC8704527Q28345234-F2DF1728-D907-4725-B864-41A9C9A647EDQ28658722-3507568D-416D-47A4-981D-4FECC515F02BQ31086903-28B47F95-F3DC-41D4-992C-86F2AF489C4CQ33345574-9C1697E5-A1F8-4018-B670-16ACDD3F1339Q33929819-E63A2FB8-CEEE-41C0-A16F-A21776C5E8CAQ34271712-C19E87A0-5CB3-4C94-BCDE-C44206C306FFQ34465265-A127468A-C195-453F-9B73-D02F9FB02D80Q34499650-3CD55DE4-34AC-4E7F-90EC-67C47988E046Q35879934-FFD7CB19-9EA9-49FB-A428-D929FD38C51DQ35895719-453B57B3-A81C-489D-AAD4-C9F770AFA5FCQ36210626-B4B812BF-E0FB-41F1-B98E-8C0074EA3F98Q36316404-D84F8E11-02DE-42C8-99FA-D813883C320EQ36898627-18DF31CC-3CCE-4FBA-8649-49B2C0CD703FQ37372758-21195B01-9762-491B-9687-80E786F52DD4Q38078480-79A2F58D-1855-4CA2-AEE4-970D74099378Q38320220-C2619565-AA1E-4040-85A7-7330FDD4DFC6Q39882042-1EF87DEA-085F-4C49-A563-D83A0D041994Q39924133-2771FA10-657F-47DD-8DCB-44322100F07EQ40536167-A8AF28F3-D69B-48D7-940F-879002E9F903Q40588017-AD575839-9FC8-4F07-BD78-977611D023CFQ40634419-17C9AC35-ECA9-435C-9F71-B836BC94CB5AQ41045856-B193A3AC-8288-4E6A-ABBD-21EB7CEC9A1AQ42021140-8BFF3E30-AE9F-41CE-A041-6B4231D4B9C0Q42497881-F5CFF257-FECE-4CE4-8B71-888E16AB29ABQ42540708-222A1493-CEC2-4CBD-AED8-E2E80E8EA554Q42543880-1D07E238-8CC8-46EF-801D-E23D2BF3E866Q42917504-52DCFC50-598A-44FC-A9BA-92359745F221Q44592816-D38D0A04-3A13-44C9-A1BD-F96EBE421907Q44691513-096A2914-2C28-4D39-BA9D-E1620AFFA5E5Q46429171-15E27D91-CEEC-4D64-BDCE-A89042F17743Q47240245-050A0FAE-616C-4136-A46C-9EA7F753F45C
P2860
Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Pervanadate activation of intr ...... on and shedding of syndecan-1.
@en
type
label
Pervanadate activation of intr ...... on and shedding of syndecan-1.
@en
prefLabel
Pervanadate activation of intr ...... on and shedding of syndecan-1.
@en
P2093
P2860
P356
P1433
P1476
Pervanadate activation of intr ...... on and shedding of syndecan-1.
@en
P2093
A C Rapraeger
C S Lebakken
J McCarthy
P2860
P356
10.1042/BJ3190039
P407
P478
319 ( Pt 1)
P577
1996-10-01T00:00:00Z