Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Bourdon, Paul R."'
Autor:
Bourdon Paul R, Jonathan D. Rich, Jack Hirsh, Burt Adelman, John M. Maraganore, Rosa Maria Lidon, Pierre Théroux, Supoat Charenkavanich, Edward Young, Christopher P. Cannon
Publikováno v:
Journal of Thrombosis and Thrombolysis. 23:93-100
Maintaining a therapeutic level of anticoagulation with unfractionated heparin remains a major challenge for clinicians because of the wide variability of patient responses, which may be explained by variable binding of heparin to plasma proteins. Di
Autor:
Catherine Hession, Konrad Miatkowski, D A Griffiths, Jeffrey L. Browning, Bourdon Paul R, Werner Meier, Christine Ambrose
Publikováno v:
Journal of Biological Chemistry. 271:8618-8626
The lymphotoxin (LT) protein complex is a heteromer of alpha (LT-alpha, also called tumor necrosis factor (TNF)-beta) and beta (LT-beta) chains anchored to the membrane surface by the transmembrane domain of the LT-beta portion. Both proteins belong
Publikováno v:
Proceedings of the National Academy of Sciences. 89:6040-6044
To determine in vivo functional roles for thrombin's structural domains, we have compared the relative antithrombotic and antihemostatic effects of (i) catalytic-site antithrombin peptide, D-Phe-Pro-Arg; (ii) exosite antithrombin peptide, the C-termi
Publikováno v:
Biochemistry. 29:7095-7101
A novel class of synthetic peptides has been designed that inhibit the thrombin catalytic site and exhibit specificity for the anion-binding exosite (ABE) of {alpha}-thrombin. These peptides, called hirulogs, consist of (i) an active-site specificity
Autor:
Bourdon Paul R, Yves Chicheportiche, Yen-Ming Hsu, Jeffrey L. Browning, Hamish S. Scott, Catherine Hession, Irène Garcia, Haoda Xu
Publikováno v:
Journal of Biological Chemistry, Vol. 272, No 51 (1997) pp. 32401-32410
The members of the tumor necrosis factor (TNF) family play pivotal roles in the regulation of the immune system. Here we describe a new ligand in this family, designated TWEAK. The mouse and human versions of this protein are unusually conserved with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0b8db9efb8481f6e93206e60550ff26
https://archive-ouverte.unige.ch/unige:11193
https://archive-ouverte.unige.ch/unige:11193
Publikováno v:
FEBS letters. 294(3)
Using hirudin as a model, a novel class of bivalent thrombin inhibitors has been designed and characterized (Maraganore et al. (1990) Biochemistry 29, 7095–7101). These peptides, designated ‘hirulogs’, interact with both thrombin's catalytic ce
Publikováno v:
Biochemical and biophysical research communications. 177(3)
Using the natural protein hirudin as a model, a novel class of synthetic peptide inhibitors were recently designed. These inhibitors, ‘hirulogs’, retain the carboxy terminal Hir53–64 domain that interacts with the anion binding exosite of throm
Publikováno v:
Biochemistry. 29(27)
In order to define structural regions in thrombin that interact with hirudin, the N alpha-dinitrofluorobenzyl analogue of an undecapeptide was synthesized corresponding to residues 54-64 of hirudin [GDFEEIPEEY(O35SO3)L (DNFB-[35S]Hir54-64)]. DNFB-[35
Autor:
Chicheportiche, Yves, Bourdon, Paul R., Xu, Haoda, Hsu, Yen-Ming, Scott, Hamish, Hession, Catherine, Garcia, Irene, Browning, Jeffrey L.
Publikováno v:
Journal of Biological Chemistry; December 1997, Vol. 272 Issue: 51 p32401-32410, 10p
Autor:
Browning, Jeffrey L., Miatkowski, Konrad, Griffiths, David A., Bourdon, Paul R., Hession, Catherine, Ambrose, Christine M., Meier, Werner
Publikováno v:
Journal of Biological Chemistry; April 1996, Vol. 271 Issue: 15 p8618-8626, 9p