Humanization of yeast to produce complex terminally sialylated glycoproteins. - Wikidata - awgldk - TriplyDB

Humanization of yeast to produce complex terminally sialylated glycoproteins.

Humanization of yeast to produce complex terminally sialylated glycoproteins.

http://www.wikidata.org/entity/Q34564538

about

Yeast: an experimental organism for 21st Century biology Properties, production, and applications of camelid single-domain antibody fragments Approaches to improve tumor accumulation and interactions between monoclonal antibodies and immune cells Glycotherapy: new advances inspire a reemergence of glycans in medicine Crystal Structure and Carbohydrate Analysis of Nipah Virus Attachment Glycoprotein: a Template for Antiviral and Vaccine Design Streptococcus pneumoniae Endohexosaminidase D, Structural and Mechanistic Insight into Substrate-assisted Catalysis in Family 85 Glycoside Hydrolases Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies Total synthesis of glycosylated proteins A phenylalanine to serine substitution within an O-protein mannosyltransferase led to strong resistance to PMT-inhibitors in Pichia pastoris A dual-mode surface display system for the maturation and production of monoclonal antibodies in glyco-engineered Pichia pastoris Efforts to make and apply humanized yeast Engineering of complex protein sialylation in plants.Pharmacy and pharmacology of biosimilars.Genome, secretome and glucose transport highlight unique features of the protein production host Pichia pastoris.Open access to sequence: browsing the Pichia pastoris genome.Expression, intracellular targeting and purification of HIV Nef variants in tobacco cells.N-glycan modification in Aspergillus species.Recombinant human lactoferrin expressed in glycoengineered Pichia pastoris: effect of terminal N-acetylneuraminic acid on in vitro secondary humoral immune response.Expression of a recombinant elastin-like protein in pichia pastoris.Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy Tuning microbial hosts for membrane protein production.Erythropoietin derived by chemical synthesis.A visual method for direct selection of high-producing Pichia pastoris clones Genome-scale metabolic reconstructions of Pichia stipitis and Pichia pastoris and in silico evaluation of their potentials Production of biopharmaceutical proteins by yeast: advances through metabolic engineering.Generation of diploid Pichia pastoris strains by mating and their application for recombinant protein production.Fed-batch fermentation of GM-CSF-producing glycoengineered Pichia pastoris under controlled specific growth rate.Comprehensive structural annotation of Pichia pastoris transcriptome and the response to various carbon sources using deep paired-end RNA sequencing.Essential role of YlMPO1, a novel Yarrowia lipolytica homologue of Saccharomyces cerevisiae MNN4, in mannosylphosphorylation of N- and O-linked glycans.Structural answers and persistent questions about how nicotinic receptors work.Characterization of the Pichia pastoris protein-O-mannosyltransferase gene family.Human recombinant truncated RNASET2, devoid of RNase activity; A potential cancer therapeutic agent.Directed evolution of a yeast-displayed HIV-1 SOSIP gp140 spike protein toward improved expression and affinity for conformational antibodies.In vitro enzymatic treatment to remove O-linked mannose from intact glycoproteins.Improving industrial yeast strains: exploiting natural and artificial diversity.Expression and analysis of the glycosylation properties of recombinant human erythropoietin expressed in Pichia pastoris.The insertion Green Monster (iGM) method for expression of multiple exogenous genes in yeast.Emerging technologies for making glycan-defined glycoproteins A new glycoengineered insect cell line with an inducibly mammalianized protein N-glycosylation pathway.Expression and purification of non-N-glycosylated porcine interleukin 3 in yeast Pichia pastoris.

P2860

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P2860

Humanization of yeast to produce complex terminally sialylated glycoproteins.

http://www.wikidata.org/entity/Q34564538

description

2006 nî lūn-bûn

@nan

2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

@zh-hk

2006年論文

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2006年論文

@zh-tw

2006年论文

@wuu

name

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@ast

Humanization of yeast to produce complex terminally sialylated glycoproteins.

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Humanization of yeast to produce complex terminally sialylated glycoproteins.

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type

label

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@ast

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@en

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@nl

prefLabel

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@ast

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@en

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@nl

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SCIENCE.1130256

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P1476

Humanization of yeast to produce complex terminally sialylated glycoproteins.

@en

P2093

Byung-Kwon Choi

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

Daniel Hopkins

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

Harry Wischnewski

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

Huijuan Li

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

Jack Hoopes

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

Jessica Roser

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

Juergen H Nett

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

Natarajan Sethuraman

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

Piotr Bobrowicz

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

Rendall R Strawbridge

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

P2860

Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells.

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

Production of complex human glycoproteins in yeast.

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

Carbohydrate-specific receptors of the liver.

Optimization of humanized IgGs in glycoengineered Pichia pastoris.

P304

1441-1443

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scholarly article

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10.1126/SCIENCE.1130256

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313

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16960007

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