%D8%BA%D9%84%D9%83%D8%B2%D8%A9Glicosilaci%C3%B3GlycosyleringGlykosylierungGlycosylationGlucosilaci%C3%B3nGl%C3%BCkos%C3%BC%C3%BClimine%DA%AF%D9%84%DB%8C%DA%A9%D9%88%D8%B2%DB%8C%D9%84%D8%A7%D8%B3%DB%8C%D9%88%D9%86GlykosylaatioGlycosylationGlicosilaci%C3%B3n%D7%92%D7%9C%D7%99%D7%A7%D7%95%D7%96%D7%99%D7%9C%D7%A6%D7%99%D7%94Glicosilazione%E3%82%B0%E3%83%AA%E3%82%B3%E3%82%B7%E3%83%AB%E5%8C%96%E1%83%92%E1%83%9A%E1%83%98%E1%83%99%E1%83%9D%E1%83%96%E1%83%98%E1%83%9A%E1%83%98%E1%83%A0%E1%83%94%E1%83%91%E1%83%90%EB%8B%B9%ED%99%94PengglikosilanGlycosyleringGlykosyleringGlikozylacjaGlicosila%C3%A7%C3%A3oGlicozilare%D0%93%D0%BB%D0%B8%D0%BA%D0%BE%D0%B7%D0%B8%D0%BB%D0%B8%D1%80%D0%BE%D0%B2%D0%B0%D0%BD%D0%B8%D0%B5GlikozilacijaGlikozilacijaGlikozilacijaGlykosyleringGlikozilasyon%D0%93%D0%BB%D1%96%D0%BA%D0%BE%D0%B7%D0%B8%D0%BB%D1%8E%D0%B2%D0%B0%D0%BD%D0%BD%D1%8FQ898365%E9%86%A3%E5%9F%BA%E5%8C%96
about
Component of oligomeric golgi complex 6CLN5 intracellular trafficking proteinCeroid-lipofuscinosis, neuronal 5CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2Component of oligomeric golgi complex 6Component of oligomeric golgi complex 6N-acetylneuraminic acid synthase Dmel_CG52323-oxo-5-alpha-steroid 4-dehydrogenase, putativeGDP-mannose pyrophosphorylaseenoyl-CoA reductase, putative3-oxo-5-alpha-steroid 4-dehydrogenase, putativeGDP-mannose pyrophosphorylaseGDP-mannose pyrophosphorylase3-oxo-5-alpha-steroid 4-dehydrogenase, putative
P682
ERK8 is a negative regulator of O-GalNAc glycosylation and cell migrationGlycosylation of glycolipids in cancer: basis for development of novel therapeutic approachesIdentification of critical residues in Gap3 of Streptococcus parasanguinis involved in Fap1 glycosylation, fimbrial formation and in vitro adhesionGlycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1)--distinct characteristics in neuronsSimilarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotesN-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESKThree proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathwayC1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activityN-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cellsA novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substratesCalreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteinsStress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylationStress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cellsIdentification of distinct surface-expressed and intracellular CXC-chemokine receptor 2 glycoforms in neutrophils: N-glycosylation is essential for maintenance of receptor surface expressionAnalysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation IcIndirect homologous competitive enzyme-linked immunosorbent assay for the detection of a class of glycosylated dihydrochalconesProtein glycosylation and advanced glycosylated endproducts (AGEs) accumulation: an avian solution?Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylationDynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brainMPDU1 mutations underlie a novel human congenital disorder of glycosylation, designated type IfCloning and expression of a cell surface receptor for advanced glycosylation end products of proteinsBIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in the endoplasmic reticulumGlycosylation of fibroblast growth factor receptor 4 is a key regulator of fibroblast growth factor 19-mediated down-regulation of cytochrome P450 7A1Ribophorin I acts as a substrate-specific facilitator of N-glycosylationInitial glycosylation and acidic pH in the Golgi apparatus are required for multimerization of von Willebrand factorCongenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferaseThe relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteinsO-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulationKinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidaseIntracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278FPhosphofructokinase 1 glycosylation regulates cell growth and metabolismColorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activityProteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolismA new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesisMHCII glycosylation modulates Bacteroides fragilis carbohydrate antigen presentationIdentification of sites of mannose 6-phosphorylation on lysosomal proteinsCOG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylationMutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylationInsulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells
P921
Q21106849-9DC374D6-A633-4038-B958-96B55273FFF8Q21109783-308462DE-C7FF-4C1E-89E3-40AEED3F0CBCQ21422940-5B9C506A-F404-460E-A2C8-109316F76059Q21495057-D711B88C-EF94-4302-A85C-9B1303DC10BEQ21497368-024EEC12-C65D-4224-8DF9-68FE812C64F9Q28560727-B99D9496-3171-4933-B4A8-2B823C6C2172Q29818853-BBC152D4-7E0E-49AE-86A1-5D029B74E594Q61495081-F2687CF2-AB66-4FFC-81AA-BCC616696981Q61513163-BC54FE8E-B13E-465D-AA7A-8DE1B0E08928Q61518191-8F6C2F85-CE0E-4E6F-825F-5FE712F8BDA2Q62416602-B2BAFD8D-EF48-4302-A125-E89D9C5874B6Q62424657-A35A7176-DCEC-425F-8F1E-5B3581E4E072Q62458818-20DC0C34-B536-4B9A-8D05-B78CB36F9C11Q62460218-E9B2B804-AF0D-4063-9D9D-BD9FE03CD2CE
P682
Q21128777-DE73E993-F8B9-4A4E-82B1-CEDCCD8835C4Q21129299-B03727D2-3B81-4CC2-AD88-9F2C1C970DDCQ21263061-5F8A4264-5F40-499A-9A1A-D6707E2D5D4FQ21284156-02850BA0-B3C6-40AE-A45C-28D5886FAE08Q21328693-8E19489B-C42B-4CF4-8C6C-EAEC91E4BF14Q22001515-45E55A8C-14E9-4633-AFCF-7A1599434857Q22008748-C4ADD790-5A63-472B-8D4C-4D6F5C6735B7Q22009093-31DBF3B5-5E89-4052-A04F-92FE873BB52DQ22010709-D9A1608E-461F-4C4D-9DAB-602DD7DF14D1Q22010732-654DF02E-65A5-4934-A081-E9073E768D3DQ22010871-1F794903-A0EF-428D-9179-B55F12790BF7Q22010942-E17F72CE-D05A-4A86-B7D7-482CBC0E6C53Q22253872-7BAC7E97-DDF9-431E-9975-5760F1FB03EBQ22254459-56CD6E94-F771-46BC-A9C2-31D21A6DF917Q22254725-38B81260-7AE2-4207-8EB1-FA24081C7890Q23910070-3EBCA091-8C80-4C2D-A684-95089070A1F8Q23918618-9A59B79C-0145-4A92-B53E-15D2F19D5085Q24290592-2E8D59D1-0A15-4239-A02F-D6F0EB5E2BEAQ24290716-DE04DAD8-279C-4A61-BE7C-72C0879EB22DQ24291964-DF861DA5-02CA-4473-820F-C87F053B580CQ24292994-2893ADFA-6271-436B-B1BB-768B17C0C3F4Q24293210-80A8C666-6970-4132-835F-CD93D5EF47B2Q24293348-B3F045C7-B0CA-42AB-B1B7-C130D522B456Q24294403-B0DA293D-282D-4FE4-AE47-6051574B4C1CQ24294887-2EA55B0F-651A-4BEC-B9E2-DD212D85E8EDQ24295998-748D7BC7-DD05-4D26-8064-F0CCD5479779Q24296242-7E1B043F-568F-4285-9E8E-C7A580886C3EQ24296449-2FF71BCB-65C0-4A53-9042-D67D22266881Q24296741-DDB15DC6-11E1-4220-B69A-02A978AD9998Q24296929-B65F3F0B-E9B5-4A0C-BA6A-CA80D123A634Q24297195-76DC013D-CFC8-48FA-8FD1-EEBA616F9C24Q24297510-39723AF7-B3B5-48C8-AB83-81782DA38D4CQ24298102-6604CBDD-1ABD-4FD5-8350-8040E567FF26Q24299352-282B920E-BBD0-4AE2-832F-A8701465E98AQ24299581-496434E7-C860-43BC-A4F2-99FECC8AB9FAQ24299980-DE2F3A3D-6998-4736-A891-289DBF41FF21Q24300525-4BB1FF85-194F-4B4A-86E8-5BC67BE0583AQ24301433-97E93AC1-AE92-494C-8FCA-313FE795B583Q24301443-B7C01B68-176F-4B3A-A13B-53E17929F8FEQ24301972-B111ADE5-42DD-4F0D-B2A1-60E5CA3F4005
P921
description
Proceso bioquímico en el que se adiciona un glúcido a otra molécula
@es
The covalent attachment and fu ...... idues to a substrate molecule.
@en
biologisch proces
@nl
réaction enzymatique
@fr
ферментативный процесс присоед ...... нсляционной модификации белков
@ru
name
Glicosilación
@gl
Glicozilare
@ro
Glikozilacija
@sh
Glikozilacija
@sl
Glikozilacija
@sr
Glikozilacija
@sr-el
Glikozilasyon
@tr
Glucosilació
@ca
Glycosylering
@da
Glykosylaatio
@fi
type
label
Glicosilación
@gl
Glicozilare
@ro
Glikozilacija
@sh
Glikozilacija
@sl
Glikozilacija
@sr
Glikozilacija
@sr-el
Glikozilasyon
@tr
Glucosilació
@ca
Glycosylering
@da
Glykosylaatio
@fi
altLabel
Glicosilacion
@es
Glikozilacija histonov
@sl
Glucosilacion proteica
@es
Glucosilacion
@es
Glucosilación proteica
@es
Glucosilación
@es
Glycosylierung
@de
Glykolysering
@sv
N-Glycosylierung
@de
N-Glykosylierung
@de
prefLabel
Glicosilación
@gl
Glicozilare
@ro
Glikozilacija
@sh
Glikozilacija
@sl
Glikozilacija
@sr
Glikozilacija
@sr-el
Glikozilasyon
@tr
Glucosilació
@ca
Glycosylering
@da
Glykosylaatio
@fi
P486
P6366
P646
P1417
science/glycosylation
P279
P2888
P3222
glykosylering
P3417
Glycosylation
P486
P5082
glykosidering
P6366
2777313579
2910902860
P646
P686
GO:0070085