The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
about
Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum proteinIdentification of novel ryanodine receptor 1 (RyR1) protein interaction with calcium homeostasis endoplasmic reticulum protein (CHERP)Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.Role of Vma21p in assembly and transport of the yeast vacuolar ATPaseAssembly, organization, and function of the COPII coatCombined deficiency of coagulation factors V and VIII: an updateN-linked sugar-regulated protein folding and quality control in the ERCrystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulumStructural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIIIStructural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiencyStructural Characterization of Carbohydrate Binding by LMAN1 Protein Provides New Insight into the Endoplasmic Reticulum Export of Factors V (FV) and VIII (FVIII)Structural Basis for Disparate Sugar-Binding Specificities in the Homologous Cargo Receptors ERGIC-53 and VIP36Erv26p directs pro-alkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles.Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesiclesEmp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiaeStructures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p.ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestinFunctional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1Secretory bulk flow of soluble proteins is efficient and COPII dependentMice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver accumulation of α1-antitrypsinLectins and traffic in the secretory pathwaySorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPIProtein interaction profiling of the p97 adaptor UBXD1 points to a role for the complex in modulating ERGIC-53 trafficking.Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules.Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor.Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36.Identification of ERGIC-53 as an intracellular transport receptor of alpha1-antitrypsin.A Non-Classical Member of the Protein Disulfide Isomerase Family, PDI7 of Arabidopsis thaliana, Localizes to the cis-Golgi and Endoplasmic Reticulum Membranes.Phosphorylation modification of wheat lectin VER2 is associated with vernalization-induced O-GlcNAc signaling and intracellular motility.EF-hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII.Capturing protein interactions in the secretory pathway of living cells.ReCLIP (reversible cross-link immuno-precipitation): an efficient method for interrogation of labile protein complexes.Carbohydrate- and conformation-dependent cargo capture for ER-exitEndoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assemblyQuality and quantity control at the endoplasmic reticulum.Control of MHC class I traffic from the endoplasmic reticulum by cellular chaperones and viral anti-chaperones.
P2860
Q24296321-334ECAC7-78F9-400F-BAE3-3C1BFAAC39DCQ24298436-A2E6B84C-38AB-484F-871D-E85C9CF1CF35Q24301091-EC715D70-B770-4C12-84C3-489D5BBE784CQ24315827-D1058171-53E0-4479-995B-1644C93E4DFAQ24562034-9E6F37D7-7105-48E5-B728-A39999FF5F0CQ24655263-279D232C-1D5B-4FA4-8792-4B79F6454038Q26820265-88355B22-0CCD-4EFA-932D-B8154489A75EQ26827318-AA45BC23-D2F4-47C8-98F4-67F67F7E63F9Q27637854-B3FCF448-8209-4448-823B-0BE5F9C8BC04Q27646866-4DA10AC3-EF66-4427-9C99-C7D64B263D8FQ27659623-2E9B6108-49AA-4170-B6A5-8B904D53BA33Q27659667-8A7BC014-878C-4462-A768-7C4B80A2F877Q27678322-F7F3AF5F-B3B5-4E29-8E22-99D21A2E7AC6Q27681589-C5A08A02-A435-4720-A2F0-0D99AA6D8DF4Q27931806-8CC81EC5-9DD2-40AB-A855-71A6867D4D18Q27935140-B65ACA9B-979B-4C5F-B4B5-BF77EC0BC0A1Q27936925-67A9A844-4899-4A6D-BB14-70518FC5823AQ27938892-88218E39-CBEF-4737-B06E-B2353E9994C1Q27939316-0C14900C-6EEF-42BA-B000-C18720D20C59Q28215231-90AB2928-F7BC-4B8D-8920-581F8BC0F7D6Q28245013-3AD48450-D9BC-4806-BAEA-F67830CA5C02Q28350951-D19C928F-22ED-4B4E-A564-7E07CC15B382Q28592631-5A858300-EAB4-458F-AD7B-E9A047A32E54Q28610116-861252E0-C9BD-4253-8B55-5B8CBACE6007Q28742686-1E6CA56D-E714-4932-B026-94BA27C79B1CQ30274646-9BE75B37-3509-43CD-9D02-0390DC0AE83BQ30476638-CC4FD2B9-4752-476B-8A71-B8C0BA120164Q30525331-FB3BFBBC-8CAF-4B7E-9BDA-ED005CFEA01EQ33222548-A121EAC8-5B15-4D2C-AC58-6E612CBF6674Q33306323-DFCC73EB-67FB-4BC7-AAA5-086605F5167CQ33320261-DDFA971D-5D7E-4FA8-BA04-9CF516EF83D8Q33365290-A4F59049-CEAD-483F-B4EF-D0FD43281986Q33418319-789A345C-B88C-4CF5-BDFD-BF3086EE2271Q33634437-9F750870-3B65-4A3D-B2FC-6768966F3D41Q33758366-C1F70B5D-3CA0-48B8-9B49-F97B39F8BF65Q33809330-AB0BFE94-DBEC-49F7-A992-50A3272EB089Q33913865-7E79A45A-D0C4-418B-BE01-76E1F0884611Q33956910-D1BE8276-BEA4-4A20-9A19-E2CB718BB4E6Q34090425-242B6659-904B-420E-B9D5-135D0F1E64C2Q34156628-EFC5D6C1-8DF1-4C74-BBF4-5E01EF5C0BE8
P2860
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին 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
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@ast
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@en
type
label
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@ast
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@en
prefLabel
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@ast
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@en
P2093
P2860
P356
P1433
P1476
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
@en
P2093
Andersson H
Appenzeller C
Kappeler F
P2860
P2888
P304
P356
10.1038/14020
P577
1999-10-01T00:00:00Z
P6179
1029951936