O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1.
about
Hijacking the Hexosamine Biosynthetic Pathway to Promote EMT-Mediated Neoplastic PhenotypesThe protein O-glucosyltransferase Rumi modifies eyes shut to promote rhabdomere separation in DrosophilaNegative regulation of notch signaling by xyloseFringe-mediated extension of O-linked fucose in the ligand-binding region of Notch1 increases binding to mammalian Notch ligandsMolecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notchO-fucosylation of the notch ligand mDLL1 by POFUT1 is dispensable for ligand functionProtein O-Glucosyltransferase 1 (POGLUT1) Promotes Mouse Gastrulation through Modification of the Apical Polarity Protein CRUMBS2A POGLUT1 mutation causes a muscular dystrophy with reduced Notch signaling and satellite cell loss.Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptorsA mutation in EGF repeat-8 of Notch discriminates between Serrate/Jagged and Delta family ligandsO-fucose monosaccharide of Drosophila Notch has a temperature-sensitive function and cooperates with O-glucose glycan in Notch transport and Notch signaling activationGalactose differentially modulates lunatic and manic fringe effects on Delta1-induced NOTCH signaling.Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeatsJagged1 heterozygosity in mice results in a congenital cholangiopathy which is reversed by concomitant deletion of one copy of Poglut1 (Rumi)6-alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin type-1 repeats by protein O-fucosyltransferases 1 and 2.Notch signaling at a glance.Intrinsic selectivity of Notch 1 for Delta-like 4 over Delta-like 1.Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.Vertebrate protein glycosylation: diversity, synthesis and function.Significance of glycosylation in Notch signaling.The multiple roles of epidermal growth factor repeat O-glycans in animal development.Mapping Sites of O-Glycosylation and Fringe Elongation on Drosophila Notch.Deciphering the Fringe-Mediated Notch Code: Identification of Activating and Inhibiting Sites Allowing Discrimination between Ligands.Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1).O-Glycosylation modulates the stability of epidermal growth factor-like repeats and thereby regulates Notch trafficking.Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity.Novel roles for O-linked glycans in protein folding.Inhibition of Delta-induced Notch signaling using fucose analogs.Analysis of mammalian O-glycopeptides - we have made a good start, but there is a long way to go.Generation of an induced pluripotent stem cell line (CSCRMi001-A) from a patient with a new type of limb-girdle muscular dystrophy (LGMD) due to a missense mutation in POGLUT1 (Rumi).Congenital diseases caused by defective -glycosylation of Notch receptors
P2860
Q26752391-F6D57BCB-1686-4D4B-A2B5-DF7379D769A9Q27311710-0CF0346D-A3D8-44E7-9CBB-C804252402B2Q27322467-733E9918-BA79-4FA8-A9D0-1B25B9BF8F96Q27683660-7344F1DF-CE53-4DD7-9337-4BA99BFB53BCQ28119076-30838A99-745E-4DA0-96DE-9B92D4D3748EQ28539733-3C473187-603A-4E6F-996D-041606199E1BQ28550463-6E0CD08C-C1FF-47F4-96C1-7B05D74CBE17Q29347528-D6FDFB6B-31CE-4966-92E1-729D4D72BC88Q34216999-53B453E4-FBB3-452A-BB8D-1AF913A95C1BQ34314581-802C9DF0-B15F-449A-824B-8CD7FF6CB757Q34801607-F43D7958-B40A-42DE-B1E5-E9B90ACD7988Q35643741-769EADC7-3C5E-42ED-8CEF-4AC890ADFC28Q36298276-01849BE8-3E65-4854-B420-3C0115C629ECQ36479429-56EFA1D2-574D-4A48-A5C1-F3556343EAD3Q36491772-5CB27C17-58DA-4380-904E-D1A0F0A6D893Q36903753-269077CC-887D-4B6D-8CE8-AC17590A0F4EQ37132158-2D24C201-ECFF-4DD0-8F9B-4B02F1791EA4Q37187965-DCC20015-F808-4D51-A869-158549D88929Q37601831-0F9D81DD-9E45-428D-9CC4-F6AD6F13450DQ38218592-0C011090-3087-478D-821D-3243105133FDQ38547337-63980D6E-14B8-4CF2-9F50-B5C3E788E386Q38766248-A11D300B-E2BA-49E5-A0E2-70DB2104CA89Q40036216-DB538980-C7DE-4BED-86CC-3484DC18C041Q41243556-DDA70134-84BD-40A2-9883-9EC30513ABFBQ41685413-DE0086BD-8B63-4AA2-97E0-71FD41EB9083Q42207653-4C1BABAF-8958-42A2-B9FA-FDA14CD37E0DQ42220831-C9D5773A-35A2-4D97-80E9-C8D8141396E0Q42254297-D198FC2B-37F0-46A8-9982-0576828D7E18Q46670439-AF984C6A-7292-4213-BB90-0A8454BF36B1Q46846034-FBCE6F5A-A435-466F-9DF4-C5615E0CDB12Q47649427-CBCC31CE-548E-4000-A8C6-8CA953110B83Q58804709-BB57D68B-5FB2-4661-8F67-B836A71C1024
P2860
O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@ast
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@en
type
label
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@ast
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@en
prefLabel
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@ast
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@en
P2093
P2860
P356
P1476
O-glucose trisaccharide is pre ...... ultiple sites on mouse Notch1.
@en
P2093
Aleksandra Nita-Lazar
Hideyuki Takeuchi
Kelvin B Luther
Nadia A Rana
Robert S Haltiwanger
Shinako Kakuda
P2860
P304
31623-31637
P356
10.1074/JBC.M111.268243
P407
P577
2011-07-08T00:00:00Z