Zobrazeno 1 - 10
of 77
pro vyhledávání: '"P M, Hogarth"'
Autor:
Emre Soyer, Robin M. Hogarth
Publikováno v:
Judgment and Decision Making, Vol 6, Pp 616-628 (2011)
Whereas much literature exists on “choice overload”, less is known about effects of numbers of alternatives in donation decisions. We hypothesize that donations increase with the number of recipients, albeit at a decreasing rate, and reflect dono
Externí odkaz:
https://doaj.org/article/241b6b92d0eb468593fa6e719806aa8e
Publikováno v:
Journal of Hypertension. 39:e394
Objective: COVID-19 caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), utilises the catalytic site of membrane-bound angiotensin converting enzyme 2 (ACE2) for cell entry. It is thought that endocytosis of ACE2 results in a d
Publikováno v:
Infection and Immunity. 68:3019-3022
Merozoite surface protein 1 (MSP-119) is a leading malaria vaccine candidate. Specific antibodies contribute to immunity; binding to macrophages is believed to represent the main action of malaria antibodies. We show that an MSP-119-specific immunogl
Publikováno v:
Immunogenetics. 51:206-211
The mouse Fcgr1 gene encoding the high-affinity IgG receptor (FcgammaRI) exists as two known alleles, FcgammaRI-BALB and FcgammaRI-NOD, and these alleles exhibit functional differences. To determine whether other alleles exist in mouse strains, Fcgr1
Autor:
M. S. Powell, Mark D. Hulett, T. P.J. Garrett, Peter A. Barton, Ian F. C. McKenzie, K. F. Maxwell, P. M. Hogarth
Publikováno v:
Nature Structural Biology. 6:437-442
Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 A resolution providing a structural basis for th
Publikováno v:
Journal of Biological Chemistry. 269:15287-15293
Fc receptor-antibody interactions are key mechanisms through which antibody effector functions are mediated. The low affinity receptor for IgG, Fc gamma RII, is expressed on most hematopoietic cells, and through the binding of immune complexes mediat
Publikováno v:
The Journal of Experimental Medicine
A recombinant soluble form of human Fc gamma RII (rsFc gamma RII) was genetically engineered by the insertion of a termination codon 5' of sequences encoding the transmembrane domain of a human Fc gamma RII cDNA. Chinese hamster ovary cells were tran
Publikováno v:
The Journal of Immunology. 150:1794-1803
Fc gamma RII is a low affinity FcR for IgG with two Ig-like extracellular domains (D1 gamma and D2 gamma), a transmembrane domain, and a cytoplasmic domain. The production, characterization, and epitope analysis of four anti-human Fc gamma RII mAb (8
Publikováno v:
Immunologic Research. 11:217-225
Molecular studies of murine Fc gamma R have revealed much exciting new information about the structure and regulation of Fc gamma RI and Fc gamma RII genes and of the Fc gamma RI protein. The Fc gamma RI gene is composed of six exons, whereas the Fc
Publikováno v:
Genes, Chromosomes and Cancer. 5:286-298
Several cytogenetic lesions in chromosomes 2, 5, 12, and 16 have been repeatedly coselected with in vitro macrophage differentiation in a clonal murine thymic tumor cell line. Parental-type subclones, which show an extremely immature hemopoietic phen