About: Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals

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About: Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals Goto Sponge NotDistinct Permalink

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scientific article (publication date: 15 November 2002)

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rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) наукова стаття, опублікована в листопаді 2002 (uk) 2002 թվականի նոյեմբերին հրատարակված գիտական հոդված (hy) 2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2002/11/15) (sk) wetenschappelijk artikel (gepubliceerd op 2002/11/15) (nl) مقالة علمية (نشرت في 15-11-2002) (ar) scientific article (publication date: 15 November 2002) (en) article scientifique publié en novembre 2002 (fr) im November 2002 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28215227-DD885549-9A9A-4593-A473-A35FB807B39F
publication date	2002-11-15 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28215227-C7D489E0-4185-4C61-8FC9-7FA7DFCD26CC
language of work or name	English
cites work	wds:Q28215227-0570A96F-62C0-40E8-891B-CFD6BE8040F0 wds:Q28215227-0A62EE38-F26C-4FB1-9C3E-0B8259E06B2C wds:Q28215227-16C473B6-263E-447F-986E-F9832D664584 wds:Q28215227-1820889E-9C83-4E66-AB36-A2E77943146E wds:Q28215227-1FBF2DC6-48AA-48BB-A6A9-66A89B73C7F3 wds:Q28215227-257B4DA6-31E5-4FB6-8F2C-359B60BF6976 wds:Q28215227-272A14F6-DD51-498D-A61D-451320F03348 wds:Q28215227-2896F252-4EDC-4EB2-AEA3-559A8DA48D49 wds:Q28215227-292DD88F-18F6-4D4E-8A38-19174B5D69F6 wds:Q28215227-299C3539-9EEB-44B3-B1B3-7E9D73888941 wds:Q28215227-308C28F4-E691-4520-BC2E-406242400EAA wds:Q28215227-35040A51-B86C-4555-907C-4198A078A8CF wds:Q28215227-36EDC258-E48A-4DCD-B7D7-E0D164032B17 wds:Q28215227-40A2E795-B29B-414E-974F-E6D2FB4317E9 wds:Q28215227-41F71276-E6C1-45A3-8F7C-A6C872F8F341 wds:Q28215227-44188A98-E183-4ABF-B2D3-1EDE9CE8045B wds:Q28215227-4DF4832B-572E-442E-9028-91E074D8CBB1 wds:Q28215227-4E70C363-5881-4184-B92F-C77B28902421 wds:Q28215227-52DEBA7A-E05B-4A23-BFE2-A55A4044C0C0 wds:Q28215227-57B8650B-14C6-43B9-99D5-02F3AB0259FB wds:Q28215227-599CABF4-A421-4A7E-B423-18A8C39FFC89 wds:Q28215227-5BFA5447-A2A0-40D9-B2D1-311B12FBAA9A wds:Q28215227-5EA0CEF1-3CBD-4A12-8E33-89BECF93CC7E wds:Q28215227-5F7B8C1D-E599-41F8-964D-BCE169BE8DF5 wds:Q28215227-64ACDDC9-C21E-4DE2-AE1D-73F7A06ABC4F wds:Q28215227-66ACD881-C4D1-4378-B413-3CADC9D53FA1 wds:Q28215227-6F782950-D26A-43B4-8F2E-4DCFBE114E68 wds:Q28215227-757F637D-84AF-474A-AF0B-274E442A907C wds:Q28215227-83E7B7D2-FAE0-43A6-B2A8-8D8E000A0120 wds:Q28215227-8B8A2BCA-3795-43F3-B5CF-D16884137C05 wds:Q28215227-8F858EFE-0BA0-440D-A491-F261F8226C9A wds:Q28215227-9751A5F1-EA32-42CF-9B36-9DF67641D5E4 wds:Q28215227-A782626D-3EF2-414F-AE10-2581EE22EB74 wds:Q28215227-B1DBBA8E-36EA-4716-A061-E456BAF8A9A1 wds:Q28215227-B8E7A968-1A5F-43D8-AF6B-60CA8075B03C wds:Q28215227-BA689EED-69CB-4A2F-B2E7-382570D32A7D wds:Q28215227-BC475C83-97D2-4018-84EC-CE96AB65AA48 wds:Q28215227-BE9D3C39-C587-4D0B-BCB3-00724D332F38 wds:Q28215227-BF3EC685-52B5-4BED-B3DE-54C31373F750 wds:Q28215227-C4665235-EB40-4995-B2D8-3013CBC3130E wds:Q28215227-CAEA37B8-E3BA-4D9C-81F6-9AF53DE5BE64 wds:Q28215227-CC6C825A-86B7-4645-83B1-A224DD4EA529 wds:Q28215227-CCF6842D-56FC-4F1E-AC32-E355D3D20C81 wds:Q28215227-D617B1FA-BFDB-49FA-82A6-F9DD688984F2 wds:Q28215227-EBE93441-4652-4518-B2CE-004ECCD5C41D wds:Q28215227-EF11E537-27C7-43A4-BEA5-A85250CEE3B3 wds:Q28215227-F2CD1C3B-6A34-4609-A478-F4EB2ED01D38 wds:Q28215227-F6F32A38-668C-4CA4-928B-B0B0AE657EC1 wds:Q28215227-FC668D16-D92C-4201-9F47-CD723F89977A wds:Q28215227-FCD0C1E7-AD3D-4C1B-A5BB-9BD29CC529C9
cites work	Analysis of endoplasmic reticulum trafficking signals by combinatorial screening in mammalian cells Invariant chain distinguishes between the exogenous and endogenous antigen presentation pathways Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation Regulation of human alpha4beta2 neuronal nicotinic acetylcholine receptors by cholinergic channel ligands and second messenger pathways. 14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner Setting the standards: quality control in the secretory pathway Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae The retention signal for soluble proteins of the endoplasmic reticulum The road taken: past and future foundations of membrane traffic 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum Assembly, transport, and function of MHC class II molecules The T cell antigen receptor: insights into organelle biology TASK-1, a two-pore domain K+ channel, is modulated by multiple neurotransmitters in motoneurons A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel complex in Drosophila presynaptic nerve terminals. Slob, a novel protein that interacts with the Slowpoke calcium-dependent potassium channel. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Inhalational anesthetics activate two-pore-domain background K+ channels KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel Potassium leak channels and the KCNK family of two-P-domain subunits A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels PDZ Domain Suppression of an ER Retention Signal in NMDA Receptor NR1 Splice Variants 14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding The structural basis for 14-3-3:phosphopeptide binding specificity 14-3-3 proteins: structure, function, and regulation 14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation Association of polyomavirus middle tumor antigen with 14-3-3 proteins Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum

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