Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy.

about

Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1.Restricted processing of CD16a/Fc γ receptor IIIa N-glycans from primary human NK cells impacts structure and function.

P2860

Q48097716-44AF55D6-01CB-47E2-A08D-CB82101490DA Q50058989-42D12136-286E-4A40-84EB-731B9495F59B

P2860

Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy.

Item

http://www.wikidata.org/entity/Q48278565

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@en

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@nl

type

Item

label

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@en

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@nl

prefLabel

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@en

Carbohydrate-Polypeptide Conta ...... ugh Solution NMR Spectroscopy.

@nl

P1476

Carbohydrate-Polypeptide Conta ...... ough Solution NMR Spectroscopy

@en

P2093

Daniel J Falconer

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

Ganesh P Subedi

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

P2860

Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc RIII and antibodies lacking core fucose

Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans

Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database

Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line

Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding.

Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX.

The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability

The Structural Role of Antibody N-Glycosylation in Receptor Interactions

NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation.

P304

3174-3177

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

P31

scholarly article

P356

10.1021/ACS.BIOCHEM.7B00392

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

P407

English

P433

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

P478

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

P50

Adam W Barb

P577

2017-06-16T00:00:00Z

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

P698

28613884

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

P932

5925738

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

Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy.

about

P2860

P2860

Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932