Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Tine N. Vinther"'
Autor:
Tine N Vinther, Mathias Norrman, Holger M Strauss, Kasper Huus, Morten Schlein, Thomas Å Pedersen, Thomas Kjeldsen, Knud J Jensen, František Hubálek
Publikováno v:
PLoS ONE, Vol 7, Iss 2, p e30882 (2012)
An ingenious system evolved to facilitate insulin binding to the insulin receptor as a monomer and at the same time ensure sufficient stability of insulin during storage. Insulin dimer is the cornerstone of this system. Insulin dimer is relatively we
Externí odkaz:
https://doaj.org/article/56be5fcb4f9d42f782c421c1d91bc207
Autor:
Trine R. Clausen, Marika Ejby Reinau, Ulrich Sensfuss, Kasper Huus, Henriette Kold Uldam, Tine N. Vinther, Susanne Schéele, Rikke Bjerring Skyggebjerg, Thomas Kruse, Bill Vestergaard
Publikováno v:
Journal of medicinal chemistry. 62(3)
A group of peptide-based, long-acting, stable, highly selective cholecystokinin 1 receptor (CCK-1R) agonists with the potential to treat obesity has been identified and characterized, based on systematic investigation of synthetic CCK-8 analogues wit
Publikováno v:
Journal of Peptide Science. 21:797-806
Insulin, a small peptide hormone, is crucial in maintaining blood glucose homeostasis. The stability and activity of the protein is directed by an intricate system involving disulfide bonds to stabilize the active monomeric species and by their non-c
Autor:
Knud J. Jensen, Morten Schlein, Anders S. Sørensen, Ingrid Pettersson, Kasper Huus, Tine N. Vinther, Thomas Kjeldsen, Frantisek Hubalek, Dorte Bjerre Steensgaard
Publikováno v:
Protein Science. 24:779-788
The structure of insulin, a glucose homeostasis-controlling hormone, is highly conserved in all vertebrates and stabilized by three disulfide bonds. Recently, we designed a novel insulin analogue containing a fourth disulfide bond located between pos
Autor:
Knud J. Jensen, Ulla Ribel, Morten Schlein, Thomas Åskov Pedersen, Ingrid Pettersson, Svend Ludvigsen, Kasper Huus, Mathias Norrman, Tine N. Vinther, Thomas Kjeldsen, Frantisek Hubalek, Dorte Bjerre Steensgaard
Publikováno v:
Protein Science. 22:296-305
Insulin is a key hormone controlling glucose homeostasis. All known vertebrate insulin analogs have a classical structure with three 100% conserved disulfide bonds that are essential for structural stability and thus the function of insulin. It might
Autor:
Tine N. Vinther, Thomas Kjeldsen, Thomas Åskov Pedersen, Ulla Ribel, Knud J. Jensen, Frantisek Hubalek
Publikováno v:
ChemBioChem. 12:2448-2455
Chemical modifications of proteins are increasingly important in the development of protein drugs with fine-tuned properties. Regioselective modification, such as the chemoselective alkylation of an unpaired cysteine residue, is a prerequisite for ob
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 21(11)
Insulin, a small peptide hormone, is crucial in maintaining blood glucose homeostasis. The stability and activity of the protein is directed by an intricate system involving disulfide bonds to stabilize the active monomeric species and by their non-c
Autor:
Tine N, Vinther, Mathias, Norrman, Ulla, Ribel, Kasper, Huus, Morten, Schlein, Dorte B, Steensgaard, Thomas Å, Pedersen, Ingrid, Pettersson, Svend, Ludvigsen, Thomas, Kjeldsen, Knud J, Jensen, František, Hubálek
Publikováno v:
Protein science : a publication of the Protein Society. 22(3)
Insulin is a key hormone controlling glucose homeostasis. All known vertebrate insulin analogs have a classical structure with three 100% conserved disulfide bonds that are essential for structural stability and thus the function of insulin. It might
Autor:
Ulla Ribel, Frantisek Hubalek, Tine N. Vinther, Knud J. Jensen, Thomas Kjeldsen, Thomas Åskov Pedersen
Publikováno v:
ChemBioChem. 12:2378-2378