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Studies of protein A and herpes simplex virus-1 induced Fc gamma-binding specificities. Different binding patterns for IgG3 from Caucasian and Oriental subjects

Human immunoglobulin class and subclass specificity of Fc receptors induced by herpes simplex virus type 1

Fractionation of rat IgG subclasses and screening for IgG Fc-binding to bacteria

Absence of host-cell influence on binding specificity of herpes simplex virus type 1 induced Fc receptor

Herpes simplex type 1-induced Fc receptor binds to the Cgamma2-Cgamma3 interface region of IgG in the area that binds staphylococcal protein A

Binding of human and animal immunoglobulins to the IgG Fc receptor induced by human cytomegalovirus

The Functional Polymorphism 844 A>G in Fc{alpha}RI (CD89) Does Not Contribute to Systemic Sclerosis or Rheumatoid Arthritis Susceptibility.

Identification of the site on IgG Fc for interaction with streptococci of groups A, C and G

Interaction between herpes simplex type 1-induced Fc receptor and human and rabbit immunoglobulin G (IgG) domains

Protective Non-neutralizing anti-N-terminal Domain mAb Maintains Fc-mediated Function against SARS-COV-2 Variants up to BA.2.86-JN.1 with Superfluous In Vivo Protection against JN.1 Due to Attenuated Virulence

Subclass-switched anti-Spike IgG3 oligoclonal cocktails strongly enhance Fc-mediated opsonization

Protective non-neutralizing mAbs Ab94 and Ab81 retain high-affinity and potent Fc-mediated function against SARS-CoV-2 variants from Omicron to XBB1.5

False positive results in class-specific rheumatoid factor (RF) assays due to interaction between RF and Fc fragments of anti-immunoglobulin indicator reagents

Pool boiling heat transfer of FC-72 on pin-fin silicon surfaces with nanoparticle deposition

In the present study, two types of micro-pin–fin configurations were fabricated on silicon surfaces by a dry etching method, i.e., staggered pin fins (#1) and aligned pin fins with empty areas (#2). The micro-pin–fin surfaces were then further modified by depositing FeMn oxide nanoparticles (∼35 nm) electrostatically for 8 h and 16 h, respectively, namely #1-8h, #1-16h, #2-8h and #2-16h. Subcooled

Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors

Streptococcal beta protein has separate binding sites for human factor H and IgA-Fc.

EndoS and EndoS2 hydrolyze Fc-glycans on therapeutic antibodies with different glycoform selectivity and can be used for rapid quantification of high-mannose glycans.

Enzymes that affect glycoproteins of the human immune system, and thereby modulate defense responses, are abundant among bacterial pathogens. Two endoglycosidases from the human pathogen Streptococcus pyogenes, EndoS and EndoS2, have recently been shown to hydrolyze N-linked glycans of human IgG. However, detailed characterization and comparison of the hydrolyzing activities have not been performe

FC Versatile

This project is an collaboration with Höganäs AB, with the goal to design a light vehicle that meets the demands of the modern commuter, in function as well as in quality and sustainability. The result of the project is a light scooter using Höganäs E-Drive system, with Hydrogen Fuel Cells as the power source. The vehicle is designed to be adaptable to the user, while still being comfortable and e

First Administration of the Fc-Attenuated Anti-β Amyloid Antibody GSK933776 to Patients with Mild Alzheimer's Disease: A Randomized, Placebo-Controlled Study.

Heat production in different populations of human blood cells exposed to immune complexes in vitro : The importance of the Fc parts of immunoglobulins and the influence of active complement

By use of a batch microcalorimeter of the thermopile type, heat production was measured in isolated populations of human peripheral blood cells exposed to defined immune complexes formed in vitro. It was found that most of the heat production recorded in whole blood after admixture of immune complexes occurs in the granulocytes. Under these conditions small but constantly higher activation values