about
A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogasterMutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathwayCovalent structures of potato tuber lipases (patatins) and implications for vacuolar import.N-Glycan structures of squid rhodopsin.MALDI-TOF and ESI-MS analysis of oligosaccharides labeled with a new multifunctional oligosaccharide tag.Quantitative glycomics of human whole serum glycoproteins based on the standardized protocol for liberating N-glycans.Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation.A role for N-glycanase in the cytosolic turnover of glycoproteins.Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation.Detection and quantification of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidases.The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningosepticaDiscovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A.A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).Kinetic characterization of a novel endo-β-N-acetylglucosaminidase on concentrated bovine colostrum whey to release bioactive glycans.The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean. Determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation.Exo- and endoglycosidases revisited.Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans.Carbohydrate-binding property of peptide: N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides.Site-specific labeling of cytoplasmic peptide:N-glycanase by N,N'-diacetylchitobiose-related compounds.A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi.Generation and degradation of free asparagine-linked glycans.Structure-activity relationships of sulfated glycoproteins from Codium fragile on nitric oxide releasing capacity from RAW264.7 Cells.Recent advances in immobilization strategies for glycosidases.Prospective phenotyping of NGLY1-CDDG, the first congenital disorder of deglycosylation.A congenital disorder of deglycosylation: Biochemical characterization of N-glycanase 1 deficiency in patient fibroblastsPNGase F-mediated incorporation of (18)O into glycans for relative glycan quantitation.Characterization of N-glycosylation consensus sequences in the Kv3.1 channel.N-glycan structures from the major glycoproteins of pigeon egg white: predominance of terminal Galalpha(1)Gal.Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity.Fragmentation of negative ions from N-linked carbohydrates: part 6. Glycans containing one N-acetylglucosamine in the core.A novel probe to assess cytosolic entry of exogenous proteins
P2860
Q24535941-334A08B3-FEE8-4F7B-969F-0B581471E8FDQ28473876-516F4007-86D1-4D1A-B299-B711F071CE51Q29017135-064A32A3-7B9A-4266-802D-8A0C0A457096Q30486813-2BB728A6-7927-468B-92E7-B58D49506C7BQ31144625-E6602780-C765-4D33-B847-BA2C40D53F5CQ33231386-9C2343BE-4D52-47D0-B3F9-E92D7B8FFD64Q33285593-C25E6151-EED7-4E1D-8925-968821B330C3Q34111419-B1A0D415-C715-406C-AF8F-FDF97D757BA9Q34179944-D8D7AE7A-7CB5-408D-B874-259273E1C08AQ34327353-5BCE68A5-CD90-41E1-BAA9-DD3351C8AA28Q34392247-3C61DBE3-8B62-467F-8E24-1863905C531BQ34448040-8F693EB8-904C-4B36-AD0C-AA586E7AD7AAQ34459339-214DB742-13BF-4692-8D38-E36B9EADC03DQ34507845-3D4C6FE3-EBBF-4458-968A-435146A6BFDCQ35584921-30ADDE50-9826-4251-BF42-FB4FDAE19EDEQ36522437-09C8433B-9572-4BFC-99F2-6F0F2097A953Q36744094-2B039C19-02BA-4898-9B77-5732432F6FC2Q38087861-077037BF-7653-428B-BDA5-BED17846FFCCQ38252574-D536EEAF-84FE-4B03-BC8D-859E4B41B5F7Q38294156-00B988AC-84FE-412E-A876-1FCC6FFDA620Q38312709-E88C52F9-E259-4F22-A5D1-A624397A1EF3Q38344795-1857DDC9-330A-44A3-A698-D26C03FA5EA8Q38378683-350BB705-D840-4AB8-844B-98902CB32473Q38915832-808A4AED-0D79-467E-A135-E6817928C3BFQ38975625-480A3398-4204-47F6-A39F-67C615DA9F3AQ39623619-9FF5EE84-FCB7-4668-BFFA-1C484D6C95ECQ41546800-04ADA308-8298-4EF8-9A65-36B03763112DQ41672972-271CA271-EA11-48A2-AC35-B285FF664552Q42036961-15171FFA-898C-4B2D-9F64-AE3C2B609B93Q43564100-7DB6ACBE-BC85-4B9F-9BDA-582D32450A20Q47682496-D90F24F0-6654-4986-B4C9-B8F25F90D26EQ53264500-662FFDC3-0588-44D9-9608-004C344FDE91Q58799522-972D9675-9CE3-451F-A7D4-FF8A49DA5E3E
P2860
description
1977 nî lūn-bûn
@nan
1977 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年論文
@yue
1977年論文
@zh-hant
1977年論文
@zh-hk
1977年論文
@zh-mo
1977年論文
@zh-tw
1977年论文
@wuu
name
Demonstration of a new amidase acting on glycopeptides.
@ast
Demonstration of a new amidase acting on glycopeptides.
@en
Demonstration of a new amidase acting on glycopeptides.
@nl
type
label
Demonstration of a new amidase acting on glycopeptides.
@ast
Demonstration of a new amidase acting on glycopeptides.
@en
Demonstration of a new amidase acting on glycopeptides.
@nl
prefLabel
Demonstration of a new amidase acting on glycopeptides.
@ast
Demonstration of a new amidase acting on glycopeptides.
@en
Demonstration of a new amidase acting on glycopeptides.
@nl
P1476
Demonstration of a new amidase acting on glycopeptides.
@en
P2093
Takahashi N
P304
P356
10.1016/0006-291X(77)90982-2
P407
P577
1977-06-01T00:00:00Z