Results 31 to 40 of about 8,130 (203)

Electron tomography of late stages of FcRn-mediated antibody transcytosis in neonatal rat small intestine [PDF]

open access: yes, 2012
The neonatal Fc receptor (FcRn) transports maternal immunoglobulin (IgG) across epithelia to confer passive immunity to mammalian young. In newborn rodents, FcRn transcytoses IgG from ingested milk across the intestinal epithelium for release into the ...
Bjorkman, Pamela J.   +2 more
core   +2 more sources

Structure of a Pheromone Receptor-Associated MHC Molecule with an Open and Empty Groove [PDF]

open access: yes, 2005
Neurons in the murine vomeronasal organ (VNO) express a family of class Ib major histocompatibility complex (MHC) proteins (M10s) that interact with the V2R class of VNO receptors.
Bjorkman, Pamela J.   +3 more
core   +6 more sources

Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG [PDF]

open access: yes, 1995
The neonatal Fc receptor (FcRn) transports maternal IgG from ingested milk in the gut to the bloodstream of newborn mammals. An FcRn dimer was observed in crystals of the receptor alone and of an FcRn-Fc complex, but its biological relevance was unknown.
Bjorkman, Pamela J.   +2 more
core   +1 more source

Dissection of the Neonatal Fc Receptor (FcRn)-Albumin Interface Using Mutagenesis and Anti-FcRn Albumin-blocking Antibodies [PDF]

open access: yesJournal of Biological Chemistry, 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. Its role as distributor is supported by its extraordinary serum half-life of 3 weeks.
Sand, Kine Marita Knudsen   +10 more
openaire   +4 more sources

Human FcRn Tissue Expression Profile and Half-Life in PBMCs

open access: yesBiomolecules, 2019
System-wide quantitative characterization of human neonatal Fc receptor (FcRn) properties is critical for understanding and predicting human PK (pharmacokinetics) as well as the distribution of mAbs and Fc-fusion proteins using PBPK (physiologically ...
Yao-Yun Fan   +5 more
doaj   +1 more source

Extending Serum Half-life of Albumin by Engineering Neonatal Fc Receptor (FcRn) Binding [PDF]

open access: yesJournal of Biological Chemistry, 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 intracellular degradation, properties shared with IgG antibodies.
Andersen, Jan Terje   +16 more
openaire   +4 more sources

Targeting the neonatal Fc receptor (FcRn) is not beneficial in an animal model of chronic neuritis. [PDF]

open access: yesImmunol Res
AbstractThe inhibition of the neonatal Fc receptor (FcRn) is a promising therapeutic pathway in certain autoimmune disorders to reduce the amount of circulating pathogenic IgG autoantibodies by interfering with their recycling system. FcRn antibodies are currently being tested in chronic inflammatory demyelinating polyradiculoneuropathy (CIDP).
Mausberg AK   +6 more
europepmc   +4 more sources

Neonatal Fc receptor (FcRn) and maternal‐to‐newborn IgE absorption [PDF]

open access: yesClinical & Experimental Allergy, 2012
From 1949-1966, a series of experimental studies by Professor F. W. Rogers Brambell (1901-1970; memoirs (1)) revealed the transmission of immunoglobulin from the mother to the fetus and newborn (2-4). In 1966, he published a review article in The Lancet describing that the selective transmission of γ-globulin from the mother to the offspring could ...
openaire   +2 more sources

The influence of antibody engineering on Fc conformation and Fc receptor binding properties: Analysis of FcRn-binding engineered antibodies and an Fc fusion protein

open access: yesmAbs, 2021
Therapeutic immunoglobulin G (IgG) antibodies have comparatively long half-lives because the neonatal Fc receptor (FcRn) binds to the IgG Fc at acidic pH in the endosome and protects IgG from degradation.
Takuo Suzuki   +3 more
doaj   +1 more source

Human IgE does not bind to human FcRn

open access: yesScientific Reports, 2022
The neonatal Fc receptor (FcRn) is known to mediate placental transfer of IgG from mother to unborn. IgE is widely known for triggering immune responses to environmental antigens.
Maximilian Brinkhaus   +6 more
doaj   +1 more source

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