Polymeric human Fc-fusion proteins with modified effector functions. - sprookjes - yvandenbroek - TriplyDB

Polymeric human Fc-fusion proteins with modified effector functions.

Polymeric human Fc-fusion proteins with modified effector functions.

http://www.wikidata.org/entity/Q35551564

about

Molecular engineering and plant expression of an immunoglobulin heavy chain scaffold for delivery of a dengue vaccine candidate Developing the IVIG biomimetic, hexa-Fc, for drug and vaccine applications Surface displaying of swine IgG1 Fc enhances baculovirus-vectored vaccine efficacy by facilitating viral complement escape and mammalian cell transduction.Recombinant IgG2a Fc (M045) multimers effectively suppress experimental autoimmune myasthenia gravis.Expression of a Human Prostatic Acid Phosphatase (PAP)-IgM Fc Fusion Protein in Plants Using In vitro Tissue Subculture.CFP10: mFcγ2 as a novel tuberculosis vaccine candidate increases immune response in mouse Fc-fusion proteins: new developments and future perspectives.Modulating immunogenicity of factor IX by fusion to an immunoglobulin Fc domain: a study using a hemophilia B mouse model.Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors.Improving Antibody-Based Cancer Therapeutics Through Glycan Engineering.APC targeting enhances immunogenicity of a novel multistage Fc-fusion tuberculosis vaccine in mice.Multivalent Fcγ-receptor engagement by a hexameric Fc-fusion protein triggers Fcγ-receptor internalisation and modulation of Fcγ-receptor functions.Plant-expressed Fc-fusion protein tetravalent dengue vaccine with inherent adjuvant properties.Fc-based delivery system enhances immunogenicity of a tuberculosis subunit vaccine candidate consisting of the ESAT-6:CFP-10 complex.rIgG1 Fc Hexamer Inhibits Antibody-Mediated Autoimmune Disease via Effects on Complement and FcγRs.Overexpression of cryoglobulin-like single-chain antibody induces morular cell phenotype via liquid-liquid phase separation in the secretory pathway organelles.Immunization With Fc-Based Recombinant Epstein-Barr Virus gp350 Elicits Potent Neutralizing Humoral Immune Response in a BALB/c Mice Model.Engineered hexavalent Fc proteins with enhanced Fc-gamma receptor avidity provide insights into immune-complex interactions

P2860

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P2860

Polymeric human Fc-fusion proteins with modified effector functions.

http://www.wikidata.org/entity/Q35551564

description

2011 nî lūn-bûn

@nan

2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Polymeric human Fc-fusion proteins with modified effector functions.

@ast

Polymeric human Fc-fusion proteins with modified effector functions.

@en

type

label

Polymeric human Fc-fusion proteins with modified effector functions.

@ast

Polymeric human Fc-fusion proteins with modified effector functions.

@en

prefLabel

Polymeric human Fc-fusion proteins with modified effector functions.

@ast

Polymeric human Fc-fusion proteins with modified effector functions.

@en

P1433

Q35551564-D12AFEB7-D20A-4967-9B3B-836250BCDDC2

P1476

Q35551564-AC60FC78-1145-47D1-9AF5-7D3C190C692D

P2093

Q35551564-5A79983C-2D68-458C-A0B3-FD6C35AC77F9

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P2860

Q35551564-0ACDAEBE-394D-41A0-853A-D8AB2D3178CE

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P2888

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P31

Q35551564-6389FBB2-462C-49DB-A375-AEE9C902AA35

P356

Q35551564-632E8877-2E16-4EEA-9722-274491DB7EB0

P407

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P478

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P50

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P932

Q35551564-0FE1E9C7-7E81-425B-98AE-88377B819410

P356

P1433

Scientific Reports

P1476

Polymeric human Fc-fusion proteins with modified effector functions.

@en

P2093

Daniel M Czajkowsky

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

David N A Mekhaiel

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

Jianfeng He

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

Jianguo Shi

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

Jun Hu

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

Marwa El-Faham

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

Richard S McIntosh

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

Zhifeng Shao

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

P2860

The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties

Activating and inhibitory IgG Fc receptors on human DCs mediate opposing functions

Comparison of simple potential functions for simulating liquid water

The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex

Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding

Crystal structure of a Fab complex formed with PfMSP1-19, the C-terminal fragment of merozoite surface protein 1 from Plasmodium falciparum: a malaria vaccine candidate

Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution

Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG

All-atom empirical potential for molecular modeling and dynamics studies of proteins

VMD: visual molecular dynamics

P2888

P304

124

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

P31

scholarly article

P356

10.1038/SREP00124

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

P407

P478

1

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

P50

Jan Terje Andersen

Michael J. Doenhoff

Richard J. Pleass

P577

2011-10-19T00:00:00Z

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

P5875

221852426

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

P6179

1017690842

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

P698

22355641

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

P932

3216605

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