Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals. - sprookjes - yvandenbroek - TriplyDB

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

http://www.wikidata.org/entity/Q37327323

about

Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase Polycystin-1: a master regulator of intersecting cystic pathways N-linked sugar-regulated protein folding and quality control in the ER Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle A genetic interaction network of five genes for human polycystic kidney and liver diseases defines polycystin-1 as the central determinant of cyst formation UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.Role of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of α1-antitrypsin Glucosidase II and MRH-domain containing proteins in the secretory pathway.Sec63 and Xbp1 regulate IRE1α activity and polycystic disease severity.Hepatocystin is Essential for TRPM7 Function During Early Embryogenesis.Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.Sorting things out through endoplasmic reticulum quality control.Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.Intracellular lectins are involved in quality control of glycoproteins.α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Diverse effects of macromolecular crowding on the sequential glycan-processing pathway involved in glycoprotein quality control.Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe.The conundrum of UDP-Glc entrance into the yeast ER lumen.

P2860

Q24324179-0404BDE4-AC26-4308-8B38-16D5D1FFA7AA Q26826955-D7217686-C0C5-4505-85B0-1C7482FFC915 Q26827318-5D059FC2-3973-4E17-B97F-485DD4A68D21 Q27677498-40296FCD-2DC5-40D3-BD95-027243882D1F Q27727968-420999C5-E32E-4436-8131-CFC3FC69683D Q28085581-2565EC90-F42D-4595-B62C-B8AB141E7BDC Q28590393-4DEBDDD2-B43E-423F-90BC-5F37054AEB4F Q33905782-1340134C-16C9-4943-9609-8EEA5031D48A Q34328488-A7060EEE-5868-40AC-B129-FEC6934E0C09 Q34543638-FD4B28AD-864B-4942-9B07-2FE05278BCAB Q35011206-EA668797-ED41-4DFB-83E6-23167C87769D Q35241499-46C584FD-771D-4EDE-9EAB-E4AA374F4B8F Q35542842-D407BB9A-70C3-4B9A-9145-13333B06AC73 Q35719978-04D1D592-EEE6-4E34-A78D-C60EA4704CFE Q36376131-80418142-2E62-49F0-A58B-1BBE74355EF0 Q36548675-39289456-0FC8-43EC-9DB3-F8AE0E77D193 Q37627987-312EA064-B862-41BC-8649-B400DF2137F3 Q37765593-810AD631-CFA0-48FB-AFD4-58D568F3DD66 Q37896955-D008CCFD-42AD-4E44-8D6E-63C016FCC5F7 Q38187545-2486DBB0-CA53-428F-B9DB-F3556863C562 Q38823312-7D0C5FB4-49FA-45C4-B071-844660124F0B Q38996383-3E1D6CFF-E57F-4F5E-B887-ACB5064188D9 Q44520260-9F669198-7874-45A9-8AA6-BCEA22A6F016 Q51020900-C84EAEF8-E2C8-479D-986A-F8D1FC4BF153 Q51537373-C44EF605-9CAF-43DA-A9C7-C5BF085534E0

P2860

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

http://www.wikidata.org/entity/Q37327323

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 15 July 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@en

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@nl

type

label

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@en

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@nl

prefLabel

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@en

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@nl

P1433

Q37327323-B1166B97-136F-44DA-9819-48DCFED49986

P1476

Q37327323-B256B634-7030-4C0E-BA6D-B536D1DEF3ED

P2093

Q37327323-804F9788-B80D-4D78-9F70-9303F5EFE228

Q37327323-98F6A37D-C78F-4D9E-A71D-825063EB5CFA

Q37327323-AA91DF02-7CA4-4F29-BCFD-938ABBCA54A2

Q37327323-EBF9E31C-0409-4302-BCCF-5EF3E6D7A315

Q37327323-F2FD199C-511E-492D-BC9C-1724F5460125

P2860

Q37327323-0A75965F-9BF2-40B6-8699-08963E563C3F

Q37327323-1C57BFB8-E45D-4DEC-B5A8-516DEE245512

Q37327323-27E9E181-E6F4-4D31-8DA3-07048313D355

Q37327323-2DDBC4BF-9A37-4B48-A2CC-B43DE2A0BF6A

Q37327323-45F4EE24-8DEA-48FD-8F2F-3389B9BD9FBD

Q37327323-4D4D8EA7-CE15-4A09-AEE8-8EEAD625D03A

Q37327323-4E3D192F-4A7D-4A95-9C72-5DD1020DA6DE

Q37327323-562836AE-D1C4-4066-BD81-7BB5FB3BF914

Q37327323-59FF3021-7ED1-4499-84BC-81651731E20D

Q37327323-63667C01-B19B-450C-B682-5AB23D0A2360

P304

Q37327323-C9DF4501-84B4-4454-9ADB-8E77E5235E88

P31

Q37327323-03E20486-F0C0-4711-BED8-CFD94C148771

P356

Q37327323-9D433504-E1E4-4B2D-B3B4-B6A0BE47B0A6

P433

Q37327323-5B708A3E-0996-4DCB-88C7-1920263CF522

P478

Q37327323-98DBF319-1634-4808-8E84-96EE588A1E73

P577

Q37327323-9CC0BE32-34A8-4C33-A234-AE5A1AD10D6C

P5875

Q37327323-87C869DC-5A03-434A-A354-71CDECF8D4B1

P698

Q37327323-2B169F28-0E46-4DE9-873E-7C6AD3FD39DE

P932

Q37327323-69752E0B-C9D3-4794-81A0-2762ECCC72A6

P356

MBC.E09-04-0316

P1433

Molecular Biology of the Cell

P1476

Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.

@en

P2093

Armando J Parodi

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

Carlos A Labriola

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

Cecilia D'Alessio

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

Ivan D Stigliano

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

Julio J Caramelo

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

P2860

Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis

Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.

Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Saccharomyces cerevisiae

A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli

The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver

The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo

Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease

Mutations in SEC63 cause autosomal dominant polycystic liver disease

Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit

Molecular genetic analysis of fission yeast Schizosaccharomyces pombe

P304

3974-3984

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

P31

scholarly article

P356

10.1091/MBC.E09-04-0316

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

P433

17

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

P478

20

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

P577

2009-07-15T00:00:00Z

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

P5875

26673990

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

P698

19605557

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

P932

2735495

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