The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation.
about
N-linked sugar-regulated protein folding and quality control in the ERAnalysis of glycoprotein processing in the endoplasmic reticulum using synthetic oligosaccharidesDeciphering the roles of glycan processing in glycoprotein quality control through organic synthesisER chaperones in mammalian development and human diseasesMinor folding defects trigger local modification of glycoproteins by the ER folding sensor GTThe role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.Mechanisms of lipase maturation.UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality controlContext-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferaseA role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I moleculesTop-down chemoenzymatic approach to a high-mannose-type glycan library: synthesis of a common precursor and its enzymatic trimming.Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.Role of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of α1-antitrypsinAllele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality controlKRE5 Suppression Induces Cell Wall Stress and Alternative ER Stress Response Required for Maintaining Cell Wall Integrity in Candida glabrataProtein quality control in the early secretory pathwayN-glycosylation of enhanced aromatic sequons to increase glycoprotein stabilityStructural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality controlA cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoproteinGlycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.N-glycan structure dictates extension of protein folding or onset of disposal.How sugars convey information on protein conformation in the endoplasmic reticulumThe recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulumHepatic lipase maturation: a partial proteome of interacting factorsProtein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesLectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.A conserved basic residue cluster is essential for the protein quality control function of the Arabidopsis calreticulin 3.Protein secretion and the endoplasmic reticulum.Cell biology of the endoplasmic reticulum and the Golgi apparatus through proteomicsThe safety dance: biophysics of membrane protein folding and misfolding in a cellular contextEmerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function.Iminosugar antivirals: the therapeutic sweet spot.Hydrophobic Tagged Dihydrofolate Reductase for Creating Misfolded Glycoprotein Mimetics.Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT.Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: a frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase.Synthesis of misfolded glycoprotein dimers through native chemical ligation of a dimeric peptide thioester.
P2860
Q26827318-7117E9D7-16B1-414D-B735-0C6073A50837Q26864189-851C4E61-B967-4F2F-BBAE-E9D6092DC4AEQ27025401-602A2EA7-8F7D-48F2-A036-D6C088463035Q28300625-5AD95B3F-81A0-49C6-9F7B-C1806357E52CQ33841814-D0AF8DBF-D47D-4E0D-B9BD-F6C16955D712Q33886809-DA821EB7-B1BB-4BF0-824C-0D526762F33FQ33904125-78E4B013-B9F8-4CDC-9C66-27872059B15CQ33905782-843ECA35-DEA6-4C3D-887C-E05E18D74A54Q34249680-6D19FFFA-7D6E-4907-8075-C569A5F2DE99Q34628677-0036DF47-6223-4577-BE17-52B9093EFEE3Q34720949-94C34D88-CA37-4A99-A0D0-69BEBD4E7411Q34760228-4764673F-16A4-45B8-8249-6FF098284DBDQ35027539-7D8E1623-C467-4C6A-94E2-E2138EA64F60Q35241499-9CD87A6F-FD6F-4D54-891A-405F2226E60DQ35941035-011F5571-A7D8-42D9-A678-F9A110CCA390Q36109051-860D3A82-291C-4890-83CA-181A0848370FQ36446833-36C0B198-BFD2-418F-B19B-AC962704FDAAQ36515262-6D2B1E6F-099E-4588-BAA8-571D2D5F1BEEQ36548675-D8F6DB91-6EE7-47DB-ACA4-2D33F59AE72FQ36562925-73367473-27DE-4DA3-8493-001A85F260A3Q36820743-8E391310-DA80-4129-88AB-FFCADD515F90Q36825595-3F9F5889-F70E-42E4-A352-EAE1F02455A4Q36998731-DEFCFDF5-9968-4D65-845B-52C9D2AABACDQ37100233-33FF3EDB-AD33-4D4C-A002-F80D7966C00BQ37190381-E8D0099B-631E-4A70-AA8E-FFBAD517FBFBQ37235421-80D3E369-DC50-4C0A-ACE3-92D3491ABEFBQ37621073-43A3E2C7-FDA4-4542-B111-588F521F3FBAQ37627987-77FFC649-7C72-4139-8887-BBCFE4EE0B1FQ37641472-D8E36DF8-9E60-49BA-B0CC-86353B4F61BEQ38018918-9F3AE525-1CF9-473E-B43F-1B6EC3C43716Q38071282-5C7267DF-16E1-49EC-B94E-DF431B07244DQ38270911-4F67F3E4-566B-46C0-B020-90F724D64BBFQ38342650-56843C06-AC62-40B6-AC2E-6E2B923F7DC7Q38358222-3185F695-D178-4FCC-865B-D79F33FBCE0AQ38730551-BB2D8B04-66D2-4F14-9EE2-63BB51642159Q40209517-40FC7642-C29C-4082-BEC2-960E6077272BQ41596349-E9A208AB-5F8D-4850-B35D-335D7DFD9817Q41842252-89C01E7A-10C9-488D-8515-072C2AF9CCC7Q42810726-B1D73CEF-D748-4296-96D4-86E7E29E1AABQ46539398-6677ED31-92B3-4B1C-83F9-62F2C25A8A08
P2860
The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
The ER protein folding sensor ...... in glycoprotein conformation.
@en
The ER protein folding sensor ...... in glycoprotein conformation.
@nl
type
label
The ER protein folding sensor ...... in glycoprotein conformation.
@en
The ER protein folding sensor ...... in glycoprotein conformation.
@nl
prefLabel
The ER protein folding sensor ...... in glycoprotein conformation.
@en
The ER protein folding sensor ...... in glycoprotein conformation.
@nl
P2093
P2860
P356
P1476
The ER protein folding sensor ...... in glycoprotein conformation.
@en
P2093
Andrew D Ferguson
John J M Bergeron
Sean C Taylor
P2860
P2888
P304
P356
10.1038/NSMB715
P577
2004-01-04T00:00:00Z