Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Torben Lübke"'
Autor:
Miao Sun, Cornelia K. Kaminsky, Philip Deppe, Mai-Britt Ilse, Frédéric M. Vaz, Barbara Plecko, Torben Lübke, Linda M. Randolph
Publikováno v:
Genes and Diseases, Vol 11, Iss 3, Pp 101025- (2024)
Externí odkaz:
https://doaj.org/article/360deb19642148408ae569c301ad2850
Autor:
Arne Linhorst, Torben Lübke
Publikováno v:
Cells, Vol 11, Iss 10, p 1592 (2022)
N-terminal nucleophile (Ntn)-hydrolases catalyze the cleavage of amide bonds in a variety of macromolecules, including the peptide bond in proteins, the amide bond in N-linked protein glycosylation, and the amide bond linking a fatty acid to sphingos
Externí odkaz:
https://doaj.org/article/332f43d0975c4394ae3df5f62cd5ddfd
Autor:
Heike Wolf, Markus Damme, Stijn Stroobants, Rudi D'Hooge, Hans Christian Beck, Irm Hermans-Borgmeyer, Renate Lüllmann-Rauch, Thomas Dierks, Torben Lübke
Publikováno v:
Disease Models & Mechanisms, Vol 9, Iss 9, Pp 1015-1028 (2016)
Fucosidosis is a rare lysosomal storage disorder caused by the inherited deficiency of the lysosomal hydrolase α-L-fucosidase, which leads to an impaired degradation of fucosylated glycoconjugates. Here, we report the generation of a fucosidosis mou
Externí odkaz:
https://doaj.org/article/138a1d71f754489d931af1f83c6469a3
Autor:
Stijn Stroobants, Heike Wolf, Zsuzsanna Callaerts-Vegh, Thomas Dierks, Torben Lübke, Rudi D’Hooge
Publikováno v:
Frontiers in Behavioral Neuroscience, Vol 12 (2018)
Fucosidosis is a lysosomal storage disorder (LSD) caused by lysosomal α-L-fucosidase deficiency. Insufficient α-L-fucosidase activity triggers accumulation of undegraded, fucosylated glycoproteins and glycolipids in various tissues. The human pheno
Externí odkaz:
https://doaj.org/article/7615384748734c13818a8b2b09b41729
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0172854 (2017)
Vasoactive and mitogenic peptide, endothelin-1 (ET-1) plays an important role in physiology of the ocular tissues by regulating the growth of corneal epithelial cells and maintaining the hemodynamics of intraocular fluids. We have previously establis
Externí odkaz:
https://doaj.org/article/8ad01cae92694c4ab4cf66615eada381
Autor:
Xiang Y. Kong, Cecilie Kasi Nesset, Markus Damme, Else-Marit Løberg, Torben Lübke, Jan Mæhlen, Kristin B. Andersson, Petra I. Lorenzo, Norbert Roos, G. Hege Thoresen, Arild C. Rustan, Eili T. Kase, Winnie Eskild
Publikováno v:
Disease Models & Mechanisms, Vol 7, Iss 3, Pp 351-362 (2014)
Human kidney predominant protein, NCU-G1, is a highly conserved protein with an unknown biological function. Initially described as a nuclear protein, it was later shown to be a bona fide lysosomal integral membrane protein. To gain insight into the
Externí odkaz:
https://doaj.org/article/118cd37476824946b0852ead9ad9bb7b
Autor:
Xuefang Pan, Lubov Grigoryeva, Volkan Seyrantepe, Junzheng Peng, Katrin Kollmann, Johanne Tremblay, Julie L Lavoie, Aleksander Hinek, Torben Lübke, Alexey V Pshezhetsky
Publikováno v:
PLoS Genetics, Vol 10, Iss 2, p e1004146 (2014)
The potent vasoconstrictor peptides, endothelin 1 (ET-1) and angiotensin II control adaptation of blood vessels to fluctuations of blood pressure. Previously we have shown that the circulating level of ET-1 is regulated through its proteolytic cleava
Externí odkaz:
https://doaj.org/article/a52a5f441dab48ebbd8044eab43b9068
Publikováno v:
Glycobiology. 31:1670-1776
Autor:
Markus Damme, Torben Lübke
Publikováno v:
Biochemical Journal. 477:3963-3983
Sulfatases constitute a family of enzymes that specifically act in the hydrolytic degradation of sulfated metabolites by removing sulfate monoesters from various substrates, particularly glycolipids and glycosaminoglycans. A common essential feature
Publikováno v:
The Biochemical journal. 478(17)
The lysosomal degradation of heparan sulfate is mediated by the concerted action of nine different enzymes. Within this degradation pathway, Arylsulfatase G (ARSG) is critical for removing 3-O-sulfate from glucosamine, and mutations in ARSG are causa