N-glycan modification in Aspergillus species. - Wikidata - awgldk - TriplyDB

N-glycan modification in Aspergillus species.

N-glycan modification in Aspergillus species.

http://www.wikidata.org/entity/Q33310581

about

Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2007-2008.N-glycoform diversity of cellobiohydrolase I from Penicillium decumbens and synergism of nonhydrolytic glycoform in cellulose degradation.Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway.GlycoFi's technology to control the glycosylation of recombinant therapeutic proteins.Making recombinant proteins in filamentous fungi- are we expecting too much?Engineering the supply chain for protein production/secretion in yeasts and mammalian cells.Putative stress sensors WscA and WscB are involved in hypo-osmotic and acidic pH stress tolerance in Aspergillus nidulans.Reexamining opportunities for therapeutic protein production in eukaryotic microorganisms.Xylan degradation improved by a combination of monolithic columns bearing immobilized recombinant β-xylosidase from Aspergillus awamori X-100 and Grindamyl H121 β-xylanase.

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N-glycan modification in Aspergillus species.

http://www.wikidata.org/entity/Q33310581

description

2007 nî lūn-bûn

@nan

2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

@nl

type

label

N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

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prefLabel

N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

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N-glycan modification in Aspergillus species.

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P1433

Applied and Environmental Microbiology

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N-glycan modification in Aspergillus species.

@en

P2093

Andreas Bernreiter

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

Andreas Gallmetzer

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

Christian Hatzl

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

Elke Kainz

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

Harald Berger

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

Huijuan Li

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

Juergen H Nett

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

Robert Pachlinger

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

Stefan Wildt

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

Thorsten Schinko

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

P2860

Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution

Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity.

Use of combinatorial genetic libraries to humanize N-linked glycosylation in the yeast Pichia pastoris.

Production of complex human glycoproteins in yeast.

A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis.

Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: production of complex humanized glycoproteins with terminal galactose.

Galactofuranoic-oligomannose N-linked glycans of alpha-galactosidase A from Aspergillus niger.

Structure and function of Class I alpha 1,2-mannosidases involved in glycoprotein synthesis and endoplasmic reticulum quality control.

Humanization of yeast to produce complex terminally sialylated glycoproteins.

Environmental effects on protein glycosylation.

P304

1076-1086

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scholarly article

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10.1128/AEM.01058-07

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4

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74

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2007-12-14T00:00:00Z

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5764658

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18083888

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2258586

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