Comparative N-Glycosylation Analysis of the Fc Portions of a Chimeric Human Coagulation Factor VIII and Immunoglobulin G1

about

Comparative N-Glycosylation Analysis of the Fc Portions of a Chimeric Human Coagulation Factor VIII and Immunoglobulin G1

Item

http://www.wikidata.org/entity/Q41512058

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Comparative N-Glycosylation An ...... tor VIII and Immunoglobulin G1

@en

type

Item

label

Comparative N-Glycosylation An ...... tor VIII and Immunoglobulin G1

@en

prefLabel

Comparative N-Glycosylation An ...... tor VIII and Immunoglobulin G1

@en

P1476

Comparative N-Glycosylation An ...... tor VIII and Immunoglobulin G1

@en

P2093

Barbara A Solecka-Witulska

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

Christoph Kannicht

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

Guido Kohla

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

Julia Rosenlöcher

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

Mario Kröning

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

P2860

Fusion Proteins for Half-Life Extension of Biologics as a Strategy to Make Biobetters

Recombinant factor VIII Fc (rFVIIIFc) fusion protein reduces immunogenicity and induces tolerance in hemophilia A mice

Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.

Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.

IgG subclasses and allotypes: from structure to effector functions.

The life cycle of coagulation factor VIII in view of its structure and function.

Symbol Nomenclature for Graphical Representations of Glycans

Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor.

Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles--part 1: separation-based methods

P31

scholarly article

P356

10.3390/BIOENGINEERING4020044

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

P433

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

P478

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

P577

2017-05-17T00:00:00Z

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

P698

28952523

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

P921

glycosylation

P932

5590467

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