Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Madlen Dorn"'
Autor:
Eva Bosse-Doenecke, Matthias Brandsch, Fritz Markwardt, Michael Jaehme, Matthias Weiwad, Rainer Rudolph, Madlen Dorn
Publikováno v:
FEBS Letters. 583:1631-1636
In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470. To determine the functional role of N-glycosylation, gly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eef8624713b8a302e6058c725a213b6
https://doi.org/10.1016/j.febslet.2009.04.037
https://doi.org/10.1016/j.febslet.2009.04.037
Publikováno v:
Molecular Pharmaceutics. 6:1006-1011
The orally administered creatine analogue beta-guanidinopropionic acid (beta-GPA) decreases plasma glucose levels by increasing the sensitivity to insulin. This effect is based on a beta-GPA induced expression of mRNA and total protein content of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38031321c203ff6095b7f9a9602c3a60
https://doi.org/10.1021/mp9000684
https://doi.org/10.1021/mp9000684
Autor:
Fritz Markwardt, Matthias Brandsch, Linda Laug, Matthias Weiwad, Rainer Rudolph, Eva Bosse-Doenecke, Madlen Dorn
Publikováno v:
The Journal of biological chemistry. 284(33)
The proton-coupled amino acid transporter 1 (PAT1, SLC36A1) mediates the uptake of small neutral amino acids at the apical membrane of intestinal epithelial cells after protein digestion. The transporter is currently under intense investigation, beca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9e94c85d84a4a2a351a1b6d6877bf4b
https://pubmed.ncbi.nlm.nih.gov/19549785
https://pubmed.ncbi.nlm.nih.gov/19549785
Autor:
Vadivel Ganapathy, Kristin Natho, Matthias Brandsch, Madlen Dorn, Katja Zebisch, Linda Metzner, Eva Bosse-Doenecke
Publikováno v:
Biochimica et biophysica acta. 1778(4)
The proton-coupled amino acid transporter 1 (PAT1) represents a major route by which small neutral amino acids are absorbed after intestinal protein digestion. The system also serves as a novel route for oral drug delivery. Having shown that H+ affec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a041d3b13478af3c6631b303008e3ac
https://pubmed.ncbi.nlm.nih.gov/18230330
https://pubmed.ncbi.nlm.nih.gov/18230330
Autor:
Marie-Christine Moutty, Gunter Fischer, Matthias Weiwad, Susann Kilka, Franziska Jarczowski, Frank Erdmann, Frank Edlich, Madlen Dorn
Publikováno v:
Biochemistry. 45(51)
Multiple intracellular receptors of the FK506 binding protein (FKBP) family of peptidylprolyl cis/trans-isomerases are potential targets for the immunosuppressive drug FK506. Inhibition of the protein phosphatase calcineurin (CaN), which has been imp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4e504121aad1d5e0f78694dc1c533e5
https://pubmed.ncbi.nlm.nih.gov/17176100
https://pubmed.ncbi.nlm.nih.gov/17176100
Autor:
Arndt Pechstein, Franziska Jarczowski, Frank Erdmann, Susann Kilka, Gunter Fischer, Matthias Weiwad, Frank Edlich, Madlen Dorn
Publikováno v:
FEBS letters. 579(7)
The microbial peptidomacrolide FK506 affects many eukaryotic developmental and cell signaling programs via calcineurin inhibition. Prior formation of a complex between FK506 and intracellular FK506-binding proteins (FKBPs) is the precondition for the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5c2333a5178bed21c542e0fde674659
https://pubmed.ncbi.nlm.nih.gov/15757646
https://pubmed.ncbi.nlm.nih.gov/15757646