Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins. - sprookjes - yvandenbroek - TriplyDB

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

http://www.wikidata.org/entity/Q34109974

about

Neonatal Fc receptor and IgG-based therapeutics Expression and bioactivity of recombinant human serum albumin and dTMP fusion proteins in CHO cells.Fusion protein of single-chain variable domain fragments for treatment of myasthenia gravis.Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor.Prostaglandin E₂ protects murine lungs from bleomycin-induced pulmonary fibrosis and lung dysfunction.New pathogen-specific immunoPET/MR tracer for molecular imaging of a systemic bacterial infection.Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding.Pharmacokinetics and PET imaging properties of two recombinant anti-PSMA antibody fragments in comparison to their parental antibody.Extending the serum half-life of G-CSF via fusion with the domain III of human serum albumin.Human and mouse albumin bind their respective neonatal Fc receptors differently

P2860

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P2860

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

http://www.wikidata.org/entity/Q34109974

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

@wuu

name

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@ast

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@en

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@nl

type

label

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@ast

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@en

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@nl

prefLabel

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@ast

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@en

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@nl

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Protein Engineering Design and Selection

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Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

@en

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Anna M Wu

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Felix B Salazar

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Lawrence E Williams

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Scott Knowles

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Tove Olafsen

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Vania E Kenanova

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P2860

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

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

The crystal structure of an anti-CEA scFv diabody assembled from T84.66 scFvs in V(L)-to-V(H) orientation: implications for diabody flexibility

Analyses of the recycling receptor, FcRn, in live cells reveal novel pathways for lysosomal delivery.

From combinatorial chemistry to cancer-targeting peptides.

Ligand efficiency and fragment-based drug discovery.

Tailoring the pharmacokinetics and positron emission tomography imaging properties of anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments.

Pharmacokinetic and pharmacodynamic studies of a human serum albumin-interferon-alpha fusion protein in cynomolgus monkeys.

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789-798

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scholarly article

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10.1093/PROTEIN/GZQ054

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10

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23

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20802234

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2935312

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