about
PBDX is the XG blood group geneA CD317/tetherin-RICH2 complex plays a critical role in the organization of the subapical actin cytoskeleton in polarized epithelial cellsThe MIC2 gene product: epitope mapping and structural prediction analysis define an integral membrane proteinSpecificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomesMicrotubules depolymerization caused by the CK1 inhibitor IC261 may be not mediated by CK1 blockageDirect interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabinCK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesiclesIns(1,4,5)P3 metabolism and the family of IP3-3KinasesExpression of HIV-1 Vpu leads to loss of the viral restriction factor CD317/Tetherin from lipid rafts and its enhanced lysosomal degradationIn vivo dynamics of the F-actin-binding protein neurabin-IICasein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapinBst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topologySerine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complexIdentification and subcellular distribution of endogenous Ins(1,4,5)P(3) 3-kinase B in mouse tissuesIP3 3-kinase opposes NGF driven neurite outgrowthGAP1IP4BP contains a novel group I pleckstrin homology domain that directs constitutive plasma membrane association.Salmonella typhi uses CFTR to enter intestinal epithelial cells.CD317/tetherin is an organiser of membrane microdomainsPrimate homologues of rat TGN38: primary structure, expression and functional implications.Modular phosphoinositide-binding domains--their role in signalling and membrane trafficking.A new recombinant DNA strategy for the molecular cloning of rare membrane proteins.Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif.Hippocalcin functions as a calcium sensor in hippocampal LTDCloning an expressed gene shared by the human sex chromosomesIsolation and sequence of a full length cDNA encoding a novel rat inositol 1,4,5-trisphosphate 3-kinase.Expression of recombinant rat myo-inositol 1,4,5-trisphosphate 3-kinase B suggests a regulatory role for its N-terminus.Release of filamentous and spherical influenza A virus is not restricted by tetherin.HIV-1 antagonism of CD317 is species specific and involves Vpu-mediated proteasomal degradation of the restriction factor.Regions of human kidney anion exchanger 1 (kAE1) required for basolateral targeting of kAE1 in polarised kidney cells: mis-targeting explains dominant renal tubular acidosis (dRTA).Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surfaceEukaryotic membrane traffic: retrieval and retention mechanisms to achieve organelle residence.Effective formation of major histocompatibility complex class II-peptide complexes from endogenous antigen by thyroid epithelial cells.The arachidonate-activatable, NADPH oxidase-associated H+ channel is contained within the multi-membrane-spanning N-terminal region of gp91-phoxSorting sweet sorting. Protein secretion.TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology.The cytosolic N-terminus of CD317/tetherin is a membrane microdomain exclusion motif.Vacuolar ATPase inactivation blocks recycling to the trans-Golgi network from the plasma membrane.Calpain cleavage of the B isoform of Ins(1,4,5)P3 3-kinase separates the catalytic domain from the membrane anchoring domain.Herpes simplex virus 1 counteracts tetherin restriction via its virion host shutoff activity.
P50
Q24306714-CDDA4949-11B2-49B3-BF5A-5CC38165C50DQ24319113-09A975D8-44D9-4B94-9211-74085201D52CQ24339470-179F8678-7140-4DBA-A385-268604499800Q24531268-70B8ECAA-6FBB-439E-B45F-95E92885709BQ24548353-7663417C-377F-41F7-95B3-2C6068DB6EFCQ27322976-A948AFA4-7DAA-4D31-8A74-803D1928F43CQ28145652-9F2376CE-5A28-4A75-B3A0-58C4D08D697EQ28217432-AEE9E472-52B3-456D-9A41-DB63EC750D2FQ28257196-3DD4397D-C74C-4992-A99B-457C6D03DB32Q28533773-6FAF28E4-4232-4EC4-AC4F-AEDDE5F8BC70Q28565993-BE461839-21FF-411F-8979-FA01B26B166FQ28578963-183A219A-46E4-4259-88EA-0D1C7CED0F10Q28580409-7F4F3069-3B60-418F-8595-58C8F460C5CDQ28580569-4363C833-9ED4-49E4-9D66-8E1A5EE1BBC7Q28590407-34CDFABA-5D9B-48E1-AD44-159B47112C39Q28731851-25ABA56D-0FED-4184-9180-43C36EFEC5C7Q33907044-3712C7E6-0234-4456-ADFE-25A1AE12D7C1Q34066552-559637F6-23C1-4308-B9A4-499B75E9B71EQ34325965-46D5B22B-C560-432A-97DA-7BA14C3C0ADBQ34406497-74BFEB0F-6C45-4AF2-A4FF-019FF541DE5AQ34429734-5EA1A134-6301-4E24-B5A1-D0266605505DQ34582627-3B43D503-C29C-4D2D-B65B-8BAA7DFFFADDQ34701633-9B8CE90A-6F6A-4A9F-B8B3-97171377991FQ35022597-CA0B7CE3-49B2-4F32-B744-97261E22706DQ35584346-A5C25508-E379-4925-9F64-D1EEFFAC8D86Q36763098-0A50CFBA-52F3-42A8-9489-2CDABFF0C9F4Q38351821-3155267C-1C48-4D27-95EC-55E198671DC7Q39409944-6E223FFB-7610-4708-98FC-963C6B7CF1F3Q39872885-02631E4C-F176-4CE2-B089-665AC7D4C715Q40583048-059B719E-7287-496A-B55E-F3A190A4B9E7Q40675417-683424F5-91E2-47D3-97C5-C7E570C22B52Q40787998-69579CBF-897B-4E1B-B705-AF78A6491F1DQ40894590-B2AB6B3E-52C9-41C3-978C-54AB4490DE2CQ41096848-AF6FC932-7FD2-465B-B19C-7DBC4F42E7DFQ41110924-C89F438B-FC20-436B-920B-700EED75AA08Q41374887-1E7E9162-45A0-4584-9922-984DD8038D73Q41762850-4014F489-EB72-4943-82F9-718F89D96AB4Q41935351-9FFF0B91-9F8B-400C-9C06-AF79D4A177A3Q42046727-E198CC1A-342C-48E4-B304-B58DCA80CDC9Q42266919-174AE826-4EB7-47C0-9D43-22840AAC2FB2
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
George Banting
@ast
George Banting
@en
George Banting
@es
George Banting
@nl
George Banting
@sl
type
label
George Banting
@ast
George Banting
@en
George Banting
@es
George Banting
@nl
George Banting
@sl
prefLabel
George Banting
@ast
George Banting
@en
George Banting
@es
George Banting
@nl
George Banting
@sl
P106
P21
P31
P496
0000-0001-8249-1621