Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Markus R. Probst"'
Autor:
Frances M. Platt, Marc Iglarz, Eric A. Ertel, Daniela Baldoni, Richard W. D. Welford, Caroline Deymier, Markus R. Probst, David A. Priestman, Andreas Mühlemann, Marco Garzotti
Publikováno v:
Molecular Genetics and Metabolism. 120:S139-S140
Fabry disease (FD) is a lysosomal disorder caused by mutations in the GLA gene coding for α‑galactosidase A (α‑GalA). These mutations lead to the accumulation of α‑GalA substrates, including globotriaosylceramide (Gb3). As a consequence of l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ce03a0f6c08adc66569b7dcaee14962
https://doi.org/10.1016/j.ymgme.2016.11.369
https://doi.org/10.1016/j.ymgme.2016.11.369
Publikováno v:
Molecular and Cellular Biology. 14:6075-6086
The activated aryl hydrocarbon receptor (AHR) and the AHR nuclear translocator (ARNT) bind DNA as a heterodimer. Both proteins represent a novel class of basic helix-loop-helix (bHLH)-containing transcription factors in that (i) activation of AHR req
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::012a599f28b3fc3c4310bd2bc3a29dac
https://doi.org/10.1128/mcb.14.9.6075
https://doi.org/10.1128/mcb.14.9.6075
Publikováno v:
Carcinogenesis. 13:1713-1717
The metabolic activation of the heterocyclic food carcinogen 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) by two human cytochrome P450 monoxygenases (P4501A1 and P4501A2) and two human N-acetyltransferases (NAT1 and NAT2) was investigated. Various co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a7b78148966e6a8aadc4a490aa02c0f
https://doi.org/10.1093/carcin/13.10.1713
https://doi.org/10.1093/carcin/13.10.1713
Autor:
Michael G. Rosenfeld, Suzanne Reisz-Porszasz, Oliver Hankinson, Khurshid Muhammad, Walter E. Nelson, Song Wang, David W. Rose, Joseph Torchia, Markus R. Probst, Timothy V. Beischlag
Publikováno v:
Molecular and cellular biology. 22(12)
The aryl hydrocarbon receptor complex heterodimeric transcription factor, comprising the basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain aryl hydrocarbon receptor (AHR) and aryl hydrocarbon receptor nuclear translocator (ARNT) proteins, mediate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fbd99d73eeb32ad28a82a20d46d2dcd
https://pubmed.ncbi.nlm.nih.gov/12024042
https://pubmed.ncbi.nlm.nih.gov/12024042
Publikováno v:
Biochemical pharmacology. 55(4)
Previous experiments have shown that the total cellular content of the AH receptor (AHR) drops rapidly after exposure of mouse hepatoma cells (Hepa-1) to the potent AHR ligand 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD); within 6 hr after treatment, l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e28a95f7ad353ba812668bec4d2205dd
https://pubmed.ncbi.nlm.nih.gov/9514084
https://pubmed.ncbi.nlm.nih.gov/9514084
Publikováno v:
The Journal of biological chemistry. 272(7)
Drosophila single-minded, which acts as a positive master gene regulator in central nervous system midline formation in Drosophila, its two mouse homologs SIM1 and SIM2, and the mammalian aryl hydrocarbon receptor (AHR) and aryl hydrocarbon receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99cb55991e920b5d71bf9bcab1941c86
https://pubmed.ncbi.nlm.nih.gov/9020169
https://pubmed.ncbi.nlm.nih.gov/9020169
Publikováno v:
The Journal of biological chemistry. 270(49)
Functional domains of the mouse aryl hydrocarbon receptor (Ahr) were investigated by deletion analysis. Ligand binding was localized to a region encompassing the PAS B repeat. The ligand-mediated dissociation of Ahr from the 90-kDa heat shock protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3316e38cc6717ed80745cd9ef41f00f4
https://pubmed.ncbi.nlm.nih.gov/7493958
https://pubmed.ncbi.nlm.nih.gov/7493958
Publikováno v:
Biochemical and biophysical research communications. 177(1)
Arylacetamide deacetylation is an important enzyme activity in the metabolic activation of arylamine substrates to ultimate carcinogens, best described as a carboxylesterase/amidase type of reaction. A 7-fold variation in the Vmax of 2-acetylaminoflu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceb1a07a8d7138dab8c22d1d1b2b10a7
https://pubmed.ncbi.nlm.nih.gov/2043131
https://pubmed.ncbi.nlm.nih.gov/2043131