Zobrazeno 1 - 10
of 37
pro vyhledávání: '"J. Gottowik"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1352:129-132
We have identified the human counterpart of the corticotropin-releasing factor receptor subtype 2beta. Its functional response to human urocortin was demonstrated after stable expression in HEK-293 cells. The receptor was also shown to bind sauvagine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e4bdea0632f62c02b9cb84ff3dda39
https://doi.org/10.1016/s0167-4781(97)00047-x
https://doi.org/10.1016/s0167-4781(97)00047-x
Autor:
Z. Bleuel, J. Gottowik, J. Gray, Cesura Andrea, Edilio Borroni, J. Saura, J. G. Richards, P. Malherbe
Publikováno v:
European Neuropsychopharmacology. 6:S4-11
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcba8f1a49560ac53eee3d77e78c67c6
https://doi.org/10.1016/0924-977x(96)83223-8
https://doi.org/10.1016/0924-977x(96)83223-8
Autor:
Cesura Andrea, Mosé Da Prada, Urs Röthlisberger, Hans-Werner Lahm, Rene Imhof, J. Gottowik, Gabrielle Lang, Pari Malherbe
Publikováno v:
European Journal of Biochemistry. 236:996-1002
The structural features of the active site of human monoamine oxidase B (MAO-B) were investigated by affinity labeling and site-directed mutagenesis. The pseudosubstrate inhibitor N-[2-aminoethyl]-5-chloro-2-pyridine carboxamide HCl (lazabemide) can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e4e2196353125ea5cb6513b0ac40e9b
https://doi.org/10.1111/j.1432-1033.1996.00996.x
https://doi.org/10.1111/j.1432-1033.1996.00996.x
Publikováno v:
European Journal of Biochemistry. 230:934-942
Monoamine oxidases (MAO) A and B show a high degree of amino acid similarity. Apart from the NH2-terminus, which contains an ADP-binding consensus sequence, little is known about their structural features or the sequences involved in the binding of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d2f8baa32bfc53e1a66a7f1c37863b0
https://doi.org/10.1111/j.1432-1033.1995.tb20639.x
https://doi.org/10.1111/j.1432-1033.1995.tb20639.x
Akademický článek
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Publikováno v:
Advances in neurology. 80
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::294460a2ec4de02661cc097a42726688
https://pubmed.ncbi.nlm.nih.gov/10410766
https://pubmed.ncbi.nlm.nih.gov/10410766
Publikováno v:
Journal of neural transmission. Supplementum. 52
To gain insight into the structure of monoamine oxidases (MAO) A and B, we investigated the properties of various chimaeric enzymes, engineered by moving progressively the junction between the NH2- and the COOH-termini of each MAO form. Whereas excha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8c875b3c32bf65d9c00fc3a68f24415e
https://pubmed.ncbi.nlm.nih.gov/9564619
https://pubmed.ncbi.nlm.nih.gov/9564619
Publikováno v:
MAO — The Mother of all Amine Oxidases ISBN: 9783211830376
To gain insight into the structure of monoamine oxidases (MAO) A and B, we investigated the properties of various chimaeric enzymes, engineered by moving progressively the junction between the NH2- and the COOH-termini of each MAO form. Whereas excha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60ed57a77a3dc28de09fd5aef27ede82
https://doi.org/10.1007/978-3-7091-6499-0_18
https://doi.org/10.1007/978-3-7091-6499-0_18
Autor:
J.M. Luque, Josep Saura, J. G. Richards, Cesura Andrea, Edilio Borroni, P. Malherbe, J. Gottowik, J. Gray
Publikováno v:
MAO — The Mother of all Amine Oxidases ISBN: 9783211830376
The present report reviews recent advances in mapping the cellular sites of synthesis and catalytic activity, as well as age- and disease-related changes of monoamine oxidases A and B in the brain. A transgenic model of oxidative stress is also descr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1872c933bb88302d074f250b1c99ba1d
https://doi.org/10.1007/978-3-7091-6499-0_17
https://doi.org/10.1007/978-3-7091-6499-0_17
Publikováno v:
FEBS letters. 317(1-2)
Monoamine oxidase (MAO)-A and MAO-B are FAD-containing mitochondrial enzymes which catabolize biogenic and xenobiotic amines. The N-terminal regions of both forms of MAO contain an ADP-binding consensus sequence found in several dinucleotide-dependen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6450de8a7d0168f760f2aa61a4373652
https://pubmed.ncbi.nlm.nih.gov/8428624
https://pubmed.ncbi.nlm.nih.gov/8428624