Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Ronald M. Shymko"'
Autor:
Birgitte Ursø, Frédéric P. Lemaigre, Hans Tornqvist, Ronald M. Shymko, Pierre De Meyts, Claus T. Christoffersen, Guy G. Rousseau, Christophe E. Pierreux
Publikováno v:
Experimental and Clinical Endocrinology & Diabetes. 104:68-70
Publikováno v:
Biochemical Journal. 339:675-683
Mitogenic signalling through the insulin receptor is enhanced compared with metabolic signalling for insulin analogues having slower dissociation kinetics than insulin itself. A plausible explanation in molecular terms of this timing-dependent specif
Autor:
Hans Hauner, W Teller, Martin Wabitsch, Pierre De Meyts, E Heinze, Ronald M. Shymko, Mapoko M. Ilondo
Publikováno v:
Metabolism. 45:34-42
The effects of human growth hormone (hGH) on proliferation and differentiation of primary adipocyte precursor cells isolated from rat epididymal fat pads were studied under serum-free culture conditions. hGH markedly reduced the formation of new fat
Autor:
Brenda Wallach, Karen Grønskov, Birgitte Ursø, Ronald M. Shymko, Claus T. Christoffersen, Fumiatsu Yakushiji, Pierre De Meyts
Publikováno v:
Metabolism. 44:2-11
The signal transduction pathways activated by hormones, growth factors, and cytokines show an extraordinary degree of cross-talk and redundancy. This review addresses the question of how the specificity conferred at the binding step is maintained thr
Publikováno v:
Annals of the New York Academy of Sciences. 766:388-401
Autor:
P De Meyts, J ten Hoeve, Henrik Vissing, Claus T. Christoffersen, Noe Gonzales, John Groffen, Karin E. Bornfeldt, Nora Heisterkamp, Ronald M. Shymko, C M Rotella
Publikováno v:
Endocrinology. 135:472-475
Insulin and insulin-like growth factor-I (IGF-I) share a spectrum of metabolic and growth-promoting effects, mediated through homologous receptors that belong to the tyrosine kinase family. The dissociation rate of insulin from its receptor is affect
Publikováno v:
Endocrinology. 134:2397-2403
Binding of GH to its cell surface receptors is thought to result in the formation of a complex comprised of one molecule of hormone per two molecules of receptor. It has been proposed that this hormone-induced receptor dimerization is important for t
Autor:
Ronald M. Shymko, M. Mapoko Ilondo, Lori-Jo Latus, Fumiatsu Yakushiji, Birgitte Ursø, Brenda Wallach, Pierre De Meyts, Karen Grønskov, Claus T. Christoffersen
Publikováno v:
Hormone Research. 42:152-169
The nonclassical binding kinetics of IGF-I and insulin to their respective receptors, suggestive of negative cooperativity, can be readily explained by our recently proposed novel binding mechanism wh
Publikováno v:
Bulletin of Mathematical Biology. 56:161-170
Autor:
Jia Li Gu, Jonathan Whittaker, Pierre De Meyts, Bruce E. Kaplan, Graeme I. Bell, Ronald M. Shymko
Publikováno v:
Molecular Endocrinology. 4:409-416
Structure-function studies of the insulin molecule indicate that an insulin B chain domain comprising residues 22-26 is involved both in binding to the insulin receptor (INSR) and in insulin dimer formation, suggesting that this domain might also int