Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kathrin Pohl"'
Autor:
Erwin Schleicher, Anita M. Hennige, Cora Weigert, Rainer Lehmann, Miriam Hoene, Ann Kathrin Pohl, Hans U. Häring
Publikováno v:
The Journal of Physiology. 587:241-252
Acute exercise performance represents a major metabolic challenge for the skeletal muscle, but also for the liver as the most important source of energy. However the molecular adaptation of the liver to one single bout of exercise is largely unknown.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::acff34ccf44ba6dc58ba1c00040f07cc
https://doi.org/10.1113/jphysiol.2008.160275
https://doi.org/10.1113/jphysiol.2008.160275
Publikováno v:
Liebigs Annalen. 1996:1905-1916
Dyotropic Hydrogen Transfer in Dihydrosesqui- and in Dihydro-syn-sesterbicyclo[2.2.2]octenes The intramolecular dyotropic hydrogen transfer is studied in dihydrosesquibicyclo[2.2.2]octenes. In the parent system 4-d2 the process transfers two hydrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d41b8ed7ee0e49b13c099afa5e6e522
https://doi.org/10.1002/jlac.199619961127
https://doi.org/10.1002/jlac.199619961127
Autor:
Miriam, Hoene, Rainer, Lehmann, Anita M, Hennige, Ann Kathrin, Pohl, Hans U, Häring, Erwin D, Schleicher, Cora, Weigert
Publikováno v:
The Journal of physiology. 587(1)
Acute exercise performance represents a major metabolic challenge for the skeletal muscle, but also for the liver as the most important source of energy. However the molecular adaptation of the liver to one single bout of exercise is largely unknown.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2fc3ce5197b9263443f364688c1afa71
https://pubmed.ncbi.nlm.nih.gov/19001047
https://pubmed.ncbi.nlm.nih.gov/19001047
Autor:
Cora Weigert, Ann Kathrin Pohl, Hubert Kalbacher, Hans-Ulrich Häring, Matthias Kron, Rainer Lehmann, Erwin Schleicher, Heike Runge
Publikováno v:
Molecular endocrinology (Baltimore, Md.). 22(12)
Transduction of the insulin signal is mediated by multisite Tyr and Ser/Thr phosphorylation of the insulin receptor substrates (IRSs). Previous studies on the function of single-site phosphorylation, particularly phosphorylation of Ser-302, -307, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65b5fa159bc6573f4c58ed2cf00cc4c3
https://pubmed.ncbi.nlm.nih.gov/18927238
https://pubmed.ncbi.nlm.nih.gov/18927238