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Now showing items 1-10 of 10
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2016)
During infection with non-enveloped viruses, antibodies stimulate immunity from inside cells by activating the cytosolic Fc receptor TRIM21. This intracellular humoral response relies on opsonized viral particles reaching ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2015)
Antibodies are key molecules in the fight against infections. Although previously thought to mediate protection solely in the extracellular environment, recent research has revealed that antibody-mediated protection extends ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2015)
The remarkable clinical success of Fc-fusion proteins has driven intense investigation for even more potent replacements. Using quality-by-design (QbD) approaches, we generated hexameric-Fc (hexa-Fc), a ~20 nm oligomeric ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2014)
A major challenge for the therapeutic use of many peptides and proteins is their short circulatory half-life. Albumin has an extended serum half-life of 3 weeks because of its size and FcRn-mediated recycling that prevents ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2014)
Albumin is an abundant blood protein that acts as a transporter of a plethora of small molecules like fatty acids, hormones, toxins, and drugs. In addition, it has an unusual long serum half-life in humans of nearly 3 ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2014)
Albumin is the most abundant protein in blood and plays a pivotal role as a multitransporter of a wide range of molecules such as fatty acids, metabolites, hormones, and toxins. In addition, it binds a variety of drugs. ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2013)
FcRn is a key player in several immunological and non-immunological processes, as it mediates maternal-fetal transfer of IgG, regulates the serum persistence of IgG and albumin, and transports both ligands between different ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2013)
Albumin has a serum half-life of 3 weeks in humans. This has been utilized to extend the serum persistence of biopharmaceuticals that are fused to albumin. In light of the fact that the neonatal Fc receptor (FcRn) is a key ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2012)
Serum half-life of IgG is controlled by the neonatal Fc receptor (FcRn) that interacts with the IgG Fc region and may be increased or decreased as a function of altered FcRn binding. Preclinical evaluations of modified ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2010)
The neonatal Fc receptor (FcRn) regulates the serum half-life of both IgG and albumin through a pH-dependent mechanism that involves salvage from intracellular degradation. Therapeutics and diagnostics built on IgG, Fc, ...