The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. - Wikidata - awgldk - TriplyDB

The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.

The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.

http://www.wikidata.org/entity/Q33880105

about

Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein Identification 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 Erv46 The 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 ATPase Assembly, organization, and function of the COPII coat Combined deficiency of coagulation factors V and VIII: an update N-linked sugar-regulated protein folding and quality control in the ER Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36 Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency Structural 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 VIP36 Erv26p 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 vesicles Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae Structures 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-arrestin Functional 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-1 Secretory bulk flow of soluble proteins is efficient and COPII dependent Mice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver accumulation of α1-antitrypsin Lectins and traffic in the secretory pathway Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI Protein 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-exit Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly Quality 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-BAE3-3C1BFAAC39DC Q24298436-A2E6B84C-38AB-484F-871D-E85C9CF1CF35 Q24301091-EC715D70-B770-4C12-84C3-489D5BBE784C Q24315827-D1058171-53E0-4479-995B-1644C93E4DFA Q24562034-9E6F37D7-7105-48E5-B728-A39999FF5F0C Q24655263-279D232C-1D5B-4FA4-8792-4B79F6454038 Q26820265-88355B22-0CCD-4EFA-932D-B8154489A75E Q26827318-AA45BC23-D2F4-47C8-98F4-67F67F7E63F9 Q27637854-B3FCF448-8209-4448-823B-0BE5F9C8BC04 Q27646866-4DA10AC3-EF66-4427-9C99-C7D64B263D8F Q27659623-2E9B6108-49AA-4170-B6A5-8B904D53BA33 Q27659667-8A7BC014-878C-4462-A768-7C4B80A2F877 Q27678322-F7F3AF5F-B3B5-4E29-8E22-99D21A2E7AC6 Q27681589-C5A08A02-A435-4720-A2F0-0D99AA6D8DF4 Q27931806-8CC81EC5-9DD2-40AB-A855-71A6867D4D18 Q27935140-B65ACA9B-979B-4C5F-B4B5-BF77EC0BC0A1 Q27936925-67A9A844-4899-4A6D-BB14-70518FC5823A Q27938892-88218E39-CBEF-4737-B06E-B2353E9994C1 Q27939316-0C14900C-6EEF-42BA-B000-C18720D20C59 Q28215231-90AB2928-F7BC-4B8D-8920-581F8BC0F7D6 Q28245013-3AD48450-D9BC-4806-BAEA-F67830CA5C02 Q28350951-D19C928F-22ED-4B4E-A564-7E07CC15B382 Q28592631-5A858300-EAB4-458F-AD7B-E9A047A32E54 Q28610116-861252E0-C9BD-4253-8B55-5B8CBACE6007 Q28742686-1E6CA56D-E714-4932-B026-94BA27C79B1C Q30274646-9BE75B37-3509-43CD-9D02-0390DC0AE83B Q30476638-CC4FD2B9-4752-476B-8A71-B8C0BA120164 Q30525331-FB3BFBBC-8CAF-4B7E-9BDA-ED005CFEA01E Q33222548-A121EAC8-5B15-4D2C-AC58-6E612CBF6674 Q33306323-DFCC73EB-67FB-4BC7-AAA5-086605F5167C Q33320261-DDFA971D-5D7E-4FA8-BA04-9CF516EF83D8 Q33365290-A4F59049-CEAD-483F-B4EF-D0FD43281986 Q33418319-789A345C-B88C-4CF5-BDFD-BF3086EE2271 Q33634437-9F750870-3B65-4A3D-B2FC-6768966F3D41 Q33758366-C1F70B5D-3CA0-48B8-9B49-F97B39F8BF65 Q33809330-AB0BFE94-DBEC-49F7-A992-50A3272EB089 Q33913865-7E79A45A-D0C4-418B-BE01-76E1F0884611 Q33956910-D1BE8276-BEA4-4A20-9A19-E2CB718BB4E6 Q34090425-242B6659-904B-420E-B9D5-135D0F1E64C2 Q34156628-EFC5D6C1-8DF1-4C74-BBF4-5E01EF5C0BE8

P2860

The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.

http://www.wikidata.org/entity/Q33880105

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

P1433

Q33880105-7B4B7C9D-9D5C-44FD-89F8-8E871DADA9DA

P1476

Q33880105-86D751B1-972C-44A8-ABCA-72A0C346A0DD

P2093

Q33880105-2695D14D-E384-46B9-B1F3-DAB7002F38CB

Q33880105-2F6B8F29-35B9-44E4-A37A-CB1BAC2F4C94

Q33880105-2FACCDA6-31B1-4459-B459-9AFB5081A541

Q33880105-9DCDC930-8BE1-4399-B8F2-64998DB377FA

P2860

Q33880105-08D2ADED-9306-40DF-B72A-EB503AE8A26B

Q33880105-0D72EEFB-0F6C-49B5-952D-A716AF49A4C6

Q33880105-228C7C3E-70D7-44D1-8A9F-2708CF3638A7

Q33880105-26768264-2FBA-4C91-8353-99BB668BD3D9

Q33880105-441199B7-1AFD-4A39-A7F2-24192EF48CB3

Q33880105-495E217D-59E0-4F1C-BA4C-D4F5242FB849

Q33880105-4A5E5EFF-F96D-48C4-B0A9-A231AC5B9160

Q33880105-4E6D5EF9-0C05-4C2F-8471-99D10AA165CC

Q33880105-5038FE72-DF9F-4110-8A98-303A8CAAD6BE

Q33880105-512866C7-D7A5-4E74-AE08-38BCE8B47381

P2888

Q33880105-F492F2E2-8143-4422-9620-F22FA56AC390

P304

Q33880105-00D9EE63-31FA-44C1-AF73-1C76A1F49C19

P31

Q33880105-FDD04598-E9CD-451F-A327-F2660C36CBFE

P356

Q33880105-53957AE2-6C06-4B4E-A665-8FE01CA83279

P433

Q33880105-54FAB0E7-696F-446E-ACDA-E21AFE51915C

P478

Q33880105-F443ADEA-E6FA-4581-BD1A-FEF5D36B8260

P577

Q33880105-CC523C23-923F-43DC-8110-6094E7B8E726

P6179

Q33880105-72914BA9-7DF4-4A04-AC78-33CAC3D9539D

P698

Q33880105-B03ABA17-6109-4055-B701-22A056B9BFA1

P356

P1433

Nature Cell Biology

P1476

The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.

@en

P2093

Andersson H

http://www.w3.org/2001/XMLSchema#string

Appenzeller C

http://www.w3.org/2001/XMLSchema#string

Hauri HP

http://www.w3.org/2001/XMLSchema#string

Kappeler F

http://www.w3.org/2001/XMLSchema#string

P2860

Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors

Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location

Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins

Transport of axl2p depends on erv14p, an ER-vesicle protein related to the Drosophila cornichon gene product.

A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins

Bimodal interaction of coatomer with the p24 family of putative cargo receptors

The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII

gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer

Coat proteins and vesicle budding

P2888

P304

330-334

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/14020

http://www.w3.org/2001/XMLSchema#string

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

1

http://www.w3.org/2001/XMLSchema#string

P577

1999-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1029951936

http://www.w3.org/2001/XMLSchema#string

P698

10559958

http://www.w3.org/2001/XMLSchema#string