Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding. - Wikidata - wikimedia - TriplyDB

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

http://www.wikidata.org/entity/Q33676732

about

Albumin-based drug delivery: harnessing nature to cure disease Fusion Proteins for Half-Life Extension of Biologics as a Strategy to Make Biobetters Unraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based Therapeutics Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokinetics The neonatal Fc receptor, FcRn, as a target for drug delivery and therapy Albumin-deficient mouse models for studying metabolism of human albumin and pharmacokinetics of albumin-based drugs Human mass balance study of TAS-102 using (14)C analyzed by accelerator mass spectrometry Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding.Stoichiometric and irreversible cysteine-selective protein modification using carbonylacrylic reagents Protein engineering: a new frontier for biological therapeutics.Albumin and its application in drug delivery.Direct demonstration of a neonatal Fc receptor (FcRn)-driven endosomal sorting pathway for cellular recycling of albumin.Half-life extended biotherapeutics.Biology of anti-TNF agents in immune-mediated inflammatory diseases: therapeutic implications.Half-Life Extension of Biopharmaceuticals using Chemical Methods: Alternatives to PEGylation.Albumin administration prevents neurological damage and death in a mouse model of severe neonatal hyperbilirubinemia.Interaction with both domain I and III of albumin is required for optimal pH-dependent binding to the neonatal Fc receptor (FcRn).An Albumin-Oligonucleotide Assembly for Potential Combinatorial Drug Delivery and Half-Life Extension Applications.Chemoselective Installation of Amine Bonds on Proteins through Aza-Michael Ligation.A human endothelial cell-based recycling assay for screening of FcRn targeted molecules.The bromocresol green assay, but not the modified bromocresol purple assay, overestimates the serum albumin concentration in nephrotic syndrome through reaction with α2-macroglobulin.Albumin-based drug delivery using cysteine 34 chemical conjugates - important considerations and requirements.Hematopoietic cells as site of first-pass catabolism after subcutaneous dosing and contributors to systemic clearance of a monoclonal antibody in mice.Roles of Fc domain and exudation in L2 antibody-mediated protection against human papillomavirus.Biomacromolecules as carriers in drug delivery and tissue engineering.The Investigation of the Use of Prealbumin as a Tool for Nutritional Assessment in Adults Coinfected with HIV and Intestinal Helminth Parasites in KwaZulu-Natal, South Africa Human and mouse albumin bind their respective neonatal Fc receptors differently

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P2860

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

http://www.wikidata.org/entity/Q33676732

description

2014 nî lūn-bûn

@nan

2014 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի մարտին հրատարակված գիտական հոդված

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2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@ast

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@en

type

label

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@ast

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@en

prefLabel

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@ast

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@en

P1433

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P356

JBC.M114.549832

P1433

Journal of Biological Chemistry

P1476

Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding.

@en

P2093

Andrew Plumridge

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

Birgitte Thue Ravn

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

Bjørn Dalhus

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

Darrell Sleep

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

Dorthe Viuff

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

Elizabeth Allan

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

Filipa Antunes

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

Jan Terje Andersen

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

Jason Cameron

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

Karen Bunting

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

P2860

Crystal structural analysis of human serum albumin complexed with hemin and fatty acid

Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites

A major histocompatibility complex class I-like Fc receptor cloned from human placenta: possible role in transfer of immunoglobulin G from mother to fetus

The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan

Crystal structure of human serum albumin at 2.5 A resolution

Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor(,)

Crystallographic Analysis of Human Serum Albumin Complexed with 4Z,15E-Bilirubin-IXα

Structural Insights into Neonatal Fc Receptor-based Recycling Mechanisms

Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface

Crystal structure of the complex of rat neonatal Fc receptor with Fc

P304

13492-13502

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scholarly article

P356

10.1074/JBC.M114.549832

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P407

P433

19

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P478

289

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P50

Magnar Bjørås

P577

2014-03-20T00:00:00Z

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24652290

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4036356

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