Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Florian Pöll"'
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e39458 (2012)
The newly developed multireceptor somatostatin analogs pasireotide (SOM230), octreotide and somatoprim (DG3173) have primarily been characterized according to their binding profiles. However, their ability to activate individual somatostatin receptor
Externí odkaz:
https://doaj.org/article/72b018b5770648bb9ef6b75bb471d9b2
Publikováno v:
British Journal of Pharmacology. 167:1259-1270
BACKGROUND AND PURPOSE The molecular basis of agonist-selective signalling at the µ-opioid receptor is poorly understood. We have recently shown that full agonists such as [D-Ala2-MePhe4-Gly-ol]enkephalin (DAMGO) stimulate the phosphorylation of a n
Publikováno v:
British Journal of Pharmacology. 164:298-307
BACKGROUND AND PURPOSE Morphine activates the µ-opioid receptor without causing its rapid endocytosis. In contrast, full agonists such as [d-Ala2-MePhe4-Gly-ol]enkephalin (DAMGO) or etonitazene stimulate a rapid and profound internalization. However
Autor:
Florian Pöll, Andrea Kliewer, Jan Carlo Märtens, Anika Mann, Aline Petrich, Anne Strigli, Falko Nagel, Stefan Schulz
Publikováno v:
Molecular endocrinology (Baltimore, Md.). 27(4)
The frequent overexpression of the somatostatin receptors sst2 and sst5 in neuroendocrine tumors provides the molecular basis for therapeutic application of novel multireceptor somatostatin analogs. Although the phosphorylation of the carboxyl-termin
Autor:
Christian, Doll, Florian, Pöll, Kenneth, Peuker, Anastasia, Loktev, Laura, Glück, Stefan, Schulz
Publikováno v:
British journal of pharmacology. 167(6)
The molecular basis of agonist-selective signalling at the µ-opioid receptor is poorly understood. We have recently shown that full agonists such as [D-Ala(2)-MePhe(4)-Gly-ol]enkephalin (DAMGO) stimulate the phosphorylation of a number of carboxyl-t
Publikováno v:
PLoS ONE
PLoS ONE, Vol 7, Iss 6, p e39458 (2012)
PLoS ONE, Vol 7, Iss 6, p e39458 (2012)
The newly developed multireceptor somatostatin analogs pasireotide (SOM230), octreotide and somatoprim (DG3173) have primarily been characterized according to their binding profiles. However, their ability to activate individual somatostatin receptor
Publikováno v:
The Journal of biological chemistry. 286(38)
Termination of signaling of activated G protein-coupled receptors (GPCRs) is essential for maintenance of cellular homeostasis. It is well established that β-arrestin redistributes to phosphorylated GPCRs and thereby facilitates desensitization of c
Publikováno v:
British journal of pharmacology. 164(2)
Morphine activates the µ-opioid receptor without causing its rapid endocytosis. In contrast, full agonists such as [d-Ala(2) -MePhe(4) -Gly-ol]enkephalin (DAMGO) or etonitazene stimulate a rapid and profound internalization. However, the detailed mo
Publikováno v:
Molecular endocrinology (Baltimore, Md.). 25(5)
The clinically used somatostatin (SS-14) analogs octreotide and pasireotide (SOM230) stimulate distinct species-specific patterns of sst(2A) somatostatin receptor phosphorylation and internalization. Like SS-14, octreotide promotes the phosphorylatio
Autor:
Amelie Lupp, Diana Lehmann, Mihaela Ginj, Ralf Stumm, Susann Illing, Stefan Schulz, Florian Pöll, Stefan Jacobs
Publikováno v:
Molecular endocrinology (Baltimore, Md.). 24(2)
Pasireotide (SOM230) is currently under clinical evaluation as a successor compound to octreotide for the treatment of acromegaly, Cushing's disease, and carcinoid tumors. Whereas octreotide acts primarily via the sst(2A) somatostatin receptor, pasir