Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Jens C Fuhrmann"'
Autor:
David M Mutch, Jens C Fuhrmann, Dietrich Rein, Jan C Wiemer, Jean-Luc Bouillot, Christine Poitou, Karine Clément
Publikováno v:
PLoS ONE, Vol 4, Iss 11, p e7905 (2009)
BACKGROUND: Roux-en-Y gastric bypass (RYGB) surgery is associated with weight loss, improved insulin sensitivity and glucose homeostasis, and a reduction in co-morbidities such as diabetes and coronary heart disease. To generate further insight into
Externí odkaz:
https://doaj.org/article/1c3c4cca99954c39a08603ea8c2c3c1f
Autor:
M.C. de Vernejoul, Jens C. Fuhrmann, Thomas J. Jentsch, Uwe Kornak, C. Schlack, Chayarop Supanchart, Lena Wartosch, Dieter Felsenberg, Jirko Kühnisch
Publikováno v:
Bone. 58:92-102
Mutations in the 2Cl(-)/1H(+)-exchanger ClC-7 impair osteoclast function and cause different types of osteoclast-rich osteopetrosis. However, it is unknown to what extent ClC-7 function has to be reduced to become rate-limiting for bone resorption. I
Autor:
Thomas J. Jentsch, Jonathan D. Cooper, Tobias Stauber, Jens C. Fuhrmann, Sarah N.R. Pressey, Kieran J. O’Donnell, Jaana Tyynelä
Publikováno v:
Journal of Neuropathology & Experimental Neurology. 69:1228-1246
The proteins ClC-6 and ClC-7 are expressed in the endosomal-lysosomal system. Because Clcn6-deficient mice display some features of neuronal ceroid lipofuscinosis (NCL), CLCN6 may be a candidate gene for novel forms of NCL. Using landmarks of disease
Publikováno v:
The FASEB Journal. 23:4056-4068
Mutations in either ClC-7, a late endosomal/lysosomal member of the CLC family of chloride channels and transporters, or in its beta-subunit Ostm1 cause osteopetrosis and lysosomal storage disease in mice and humans. The severe phenotype of mice glob
Publikováno v:
Journal of Histochemistry & Cytochemistry. 54:991-996
Tripeptidyl peptidase I (TPP-I) is a lysosomal peptidase with unclear physiological function. TPP-I deficiency is associated with late-infantile neuronal ceroid lipofuscinosis (NCL), a fatal neurodegenerative disease of childhood that is characterize
Publikováno v:
Annual Review of Physiology
Annual Review of Physiology, Annual Reviews, 2005, 67 (1), pp.779-807. ⟨10.1146/annurev.physiol.67.032003.153245⟩
Annual Review of Physiology, Annual Reviews, 2005, 67 (1), pp.779-807. ⟨10.1146/annurev.physiol.67.032003.153245⟩
▪ Abstract The CLC gene family encodes nine different Cl− channels in mammals. These channels perform their functions in the plasma membrane or in intracellular organelles such as vesicles of the endosomal/lysosomal pathway or in synaptic vesicle
Autor:
Stefan Kins, Jens C. Fuhrmann, Y. Grosskreutz, Heinrich Betz, Achim Hermann, Matthias Kneussel
Publikováno v:
Biological Chemistry. 382:1455-1462
The brainspecific GDP/GTP exchange factor collybistin interacts with the receptoranchoring protein gephyrin and activates the Rholike GTPase Cdc42, which is known to regulate actin cytoskeleton dynamics. Alternative splicing creates two collybistin v
Publikováno v:
GBM Annual Spring meeting Mosbach 2007. 2007
Publikováno v:
GBM Annual Spring meeting Mosbach 2007. 2007
Autor:
Sara E. Mole, Uwe Kornak, Jens C. Fuhrmann, Thomas J. Jentsch, Anja Schmitt, Christian A. Hübner, Mallorie Poët, Michaela Schweizer, Rosa Planells-Cases, Anselm A. Zdebik, Sabine Hoelter, Olaf Scheel, Wolfgang Wurst
Mammalian CLC proteins function as Cl − channels or as electrogenic Cl − /H + exchangers and are present in the plasma membrane and intracellular vesicles. We now show that the ClC-6 protein is almost exclusively expressed in neurons of the centr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f62fb683239b5eb0b35fe82ff5d9f8ab
https://europepmc.org/articles/PMC1564226/
https://europepmc.org/articles/PMC1564226/