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pro vyhledávání: '"Gerrit Vortmeier"'
Autor:
Gerrit Vortmeier, Stephanie H DeLuca, Sylvia Els-Heindl, Constance Chollet, Holger A Scheidt, Annette G Beck-Sickinger, Jens Meiler, Daniel Huster
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0122444 (2015)
The peptide hormone ghrelin activates the growth hormone secretagogue receptor 1a, also known as the ghrelin receptor. This 28-residue peptide is acylated at Ser3 and is the only peptide hormone in the human body that is lipid-modified by an octanoyl
Externí odkaz:
https://doaj.org/article/19d0b2b4c83e415fb09d733911cacbee
Autor:
Sylvia Els-Heindl, Jens Meiler, Gerrit Vortmeier, Anette Kaiser, Annette G. Beck-Sickinger, Ulrike Krug, Mathias Bosse, Brian J. Bender, Stefan Ernicke, Daniel Huster
Publikováno v:
Structure
The peptide ghrelin targets the growth hormone secretagogue receptor 1a (GHSR) to signal changes in cell metabolism and is a sought-after therapeutic target, although no structure is known to date. To investigate the structural basis of ghrelin bindi
Autor:
Annette G. Beck-Sickinger, Daniel Huster, Gerrit Vortmeier, Holger A. Scheidt, Peter Schmidt, Dennis J. Worm, Stefanie Schrottke, Mathias Bosse, Anette Kaiser, Sylvia Els-Heindl
Publikováno v:
Scientific Reports
The expression, functional reconstitution and first NMR characterization of the human growth hormone secretagogue (GHS) receptor reconstituted into either DMPC or POPC membranes is described. The receptor was expressed in E. coli. refolded, and recon
Autor:
Gerrit Vortmeier, Annette G. Beck-Sickinger, Stephanie H. DeLuca, Jens Meiler, Stefanie Schrottke, Brian J. Bender, Daniel Huster, Sylvia Els-Heindl
Publikováno v:
Biophysical Journal. 114:22a
Autor:
Jens Meiler, Daniel Huster, Constance Chollet, Stephanie H. DeLuca, Gerrit Vortmeier, Annette G. Beck-Sickinger, Sylvia Els-Heindl, Holger A. Scheidt
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0122444 (2015)
PLoS ONE
PLoS ONE
The peptide hormone ghrelin activates the growth hormone secretagogue receptor 1a, also known as the ghrelin receptor. This 28-residue peptide is acylated at Ser3 and is the only peptide hormone in the human body that is lipid-modified by an octanoyl
Publikováno v:
Chemistry and physics of lipids. 183
The PC/LPC ratio of blood serum is increasingly considered to represent an important clinical parameter that reflects various kinds of diseases. Here, a simple and fast method of lipid analyses of “intact” blood serum (i.e. without extraction) by
Autor:
Daniel Huster, Annette G. Beck-Sickinger, Constance Chollet, Lars Thomas, Holger A. Scheidt, Gerrit Vortmeier
Publikováno v:
Biophysical Journal. 102(3)
Ghrelin is a 28-amino acid peptide, which is known to play a key role in the regulation of food intake and body weight. Ghrelin is the only known hormone that carries an octanoyl lipid modification at residue Ser 3. Here, we have studied the structur