Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Øistein Ihle"'
Autor:
Øistein Ihle, Diane Lynn Bryant Bratlie, Inger Sandlie, Beathe Kiland Granerud, Sidsel Emilsen, Terje E. Michaelsen, Randi Sandin
Publikováno v:
Scandinavian Journal of Immunology
IgM molecules circulate in serum as large polymers, mainly pentamers, which can be transported by the poly-Ig receptor (pIgR) across epithelial cells to mucosal surfaces and released as secretory IgM (SIgM). The mucosal SIgM molecules have non-covale
Autor:
Bjørn Skogen, Tor B. Stuge, Terje E. Michaelsen, Øistein Ihle, Maria Averina, Mette Kjaer, Anne Husebekk, Gøril Heide, Cedric Ghevaert, Mariana Eksteen, Heidi Tiller
Publikováno v:
The Journal of Immunology. 194:5751-5760
Human platelet Ag (HPA)-1a, located on integrin β3, is the main target for alloantibodies responsible for fetal and neonatal alloimmune thrombocytopenia (FNAIT) in the white population. There are ongoing efforts to develop an Ab prophylaxis and ther
Autor:
Peter T. Beernink, Dan M. Granoff, Diane Lynn Bryant Bratlie, Terje E. Michaelsen, Serena Giuntini, Øistein Ihle
Publikováno v:
Clinical and vaccine immunology : CVI. 23(8)
We compared the bactericidal activity of recombinant sets of chimeric IgG monoclonal antibodies against two important outer membrane meningococcal vaccine antigens: PorA and factor H binding protein (FHbp). The sets contained human Fc portions from I
Publikováno v:
Hybridoma. 30:1-9
Glycophorins comprise the major sialoglycoproteins of the human erythrocyte membrane. Several years ago we described a murine monoclonal antibody (MAb), designated 124,D-7 (IgM), developed by in vitro immunization with human erythrocyte membranes as
Publikováno v:
Scandinavian Journal of Immunology
The C1q binding epicentre on IgG molecules involves residues Asp(270), Lys(322), Pro(329) and Pro(331) in the C(H)2 domain. IgG1 and IgG3 are usually the most efficient of the four human IgG subclasses in activating complement and they both share all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ef3650befaf9a40b446f545a0c4d3f
http://hdl.handle.net/11250/2507790
http://hdl.handle.net/11250/2507790
Autor:
John E. Thommesen, Ole Henrik Brekke, Randi Sandin, Inger Sandlie, Tone F. Gregers, Øistein Ihle, Terje E. Michaelsen
Publikováno v:
European Journal of Immunology
There are potentially two binding sites for C1q on IgG, one on each C(H)2 domain of the gamma heavy chains, close to the lower hinge region. It is not clear whether the presence and involvement of both the C1q binding sites is necessary to induce the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31f8ebf3e16ac89a37531c11e1c7c036
http://hdl.handle.net/11250/2507797
http://hdl.handle.net/11250/2507797
Autor:
Øistein Ihle, Jan Kolberg, Tove Karin Herstad, Audun Aase, E. Arne Høiby, Karen Johanne Beckstrøm, Terje E. Michaelsen
We studied the in vitro protective activities of human immunoglobulin G1 (IgG1), IgG3, and IgM antibodies against group B meningococci by constructing sets of chimeric mouse-human antibodies (chIgG1, chIgG3, and chIgM, respectively) with identical bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33ac451c0e50d8686dffd4db03dd9541
https://europepmc.org/articles/PMC201080/
https://europepmc.org/articles/PMC201080/
Publikováno v:
Scandinavian journal of immunology. 57(5)
The P1.7 and P1.16 epitopes on the PorA protein on the outer membrane of Neisseria meningitidis can induce protective antibodies upon vaccination. Structural analysis of antibodies to these targets can give information on the immune response induced
Autor:
Øistein Ihle, Terje E. Michaelsen
A novel and efficient method has been developed for isolation of correctly digested DNA fragments without the use of classic size-dependent electrophoretic separation methods. To achieve this, DNA fragments are end-labelled by haptens. After specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a3cb7a6b118d685a203026c6c295c8
https://europepmc.org/articles/PMC108460/
https://europepmc.org/articles/PMC108460/
Publikováno v:
Biological chemistry. 378(12)
Five phage displayed peptide libraries were screened for binders to C1q, the recognition subunit of the classical complement pathway. Two rounds of panning resulted in the isolation and characterisation of several different phage displayed C1q-bindin