Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Nurfilza Ahmat"'
Autor:
Joseph J. E. Caesar, Olga Lissina, Susanne Leonhartsberger, Isabelle Maillet, Pietro Roversi, Nurfilza Ahmat, Susan M. Lea, Guido C. Paesen, Miles A. Nunn, Mauro Martin Teixeira, Wilhelm Boland, Bernhard Ryffel, Kerstin Ploss, Dieudonnée Togbe
Publikováno v:
The Journal of Biological Chemistry
'Journal of Biological Chemistry ', vol: 288, pages: 18789-18802 (2013)
'Journal of Biological Chemistry ', vol: 288, pages: 18789-18802 (2013)
Background: OmCI is an ectoparasite-derived anti-inflammatory protein that binds LTB4 and prevents complement C5 activation. Results: The C5 and LTB4 binding activities of OmCI are functionally and structurally independent, and OmCI potently inhibits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebd4543ab49af754bb770bc28df92fe9
http://europepmc.org/articles/PMC3696655
http://europepmc.org/articles/PMC3696655
Autor:
Katarzyna Juszczyk, Aimee Smith, Colin R. Goding, Mehrnoush Dezfouli, Nurfilza Ahmat, Emanuela Bastonini, Megan Field, Philip Jordan, Howard Womersley, Aroul Ramadass, Magdalena Jeznach, Alexandre Akoulitchev, Emily Corfield
Publikováno v:
Pigment cellmelanoma research. 27(5)
The major barrier to effective cancer therapy is the presence of genetic and phenotypic heterogeneity within cancer cell populations that provides a reservoir of therapeutically resistant cells. As the degree of heterogeneity present within tumours w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27f3791b0047a0fa5a8f37709dd088bb
https://pubmed.ncbi.nlm.nih.gov/24807349
https://pubmed.ncbi.nlm.nih.gov/24807349
Autor:
Pietro Roversi, Dieudonee Togbe, Susanne Leonhartsberger, Olga Lissina, Isabelle Maillet, Wilhelm Boland, Nurfilza Ahmat, Valérie F. J. Quesniaux, Susan M. Lea, Miles A. Nunn, Mauro Martin Teixeira, Bernhard Ryffel, Kerstin Ploss
Publikováno v:
MOLECULAR IMMUNOLOGY. 47(13)
OmCI is an ectoparasite derived bifunctional lipocalin that inhibits complement (C) by binding to C5 and also captures the proinflammatory eicosanoid leukotriene B4 (LTB4). We present the crystal structure of recombinant bacterial bOmCI with and with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd61b54dec813923462adecd304892ed
http://ora.ox.ac.uk/objects/uuid:5c93694b-440c-4845-a36b-f1b69c5f06f1
http://ora.ox.ac.uk/objects/uuid:5c93694b-440c-4845-a36b-f1b69c5f06f1
Publikováno v:
Molecular Immunology. 44:234
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f00fff07567ab02c9aef67624acdedbb
https://doi.org/10.1016/j.molimm.2006.07.204
https://doi.org/10.1016/j.molimm.2006.07.204