Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Doug Bittel"'
Autor:
Karen Kover, Pei Ying Tong, Dara Watkins, Mark Clements, Lisa Stehno-Bittel, Lesya Novikova, Doug Bittel, Nataliya Kibiryeva, Jacob Stuhlsatz, Yun Yan, Shui Qing Ye, Wayne V Moore
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e58767 (2013)
Nicotinamide phosphoribosyltransferase (Nampt) is a rate-limiting enzyme in the mammalian NAD+ biosynthesis of a salvage pathway and exists in 2 known forms, intracellular Nampt (iNampt) and a secreted form, extracellular Nampt (eNampt). eNampt can g
Externí odkaz:
https://doaj.org/article/2006e7d80dbe417f9ffda263ff5b29f5
Publikováno v:
American Journal of Medical Genetics. :168-171
Coenzyme Q10 (CoQ10) is an essential component of the mitochondrial respiratory chain and an important scavenger of reactive oxygen species. Low levels are found in individuals with reduced energy expenditure, cardiac and skeletal muscle dysfunction,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da39c94fb859442197c5f765abf6931d
https://doi.org/10.1002/ajmg.a.10055
https://doi.org/10.1002/ajmg.a.10055
Publikováno v:
Nucleic Acids Research. 30:3130-3140
The zinc finger protein, metal response element-binding transcription factor-1 (MTF-1) regulates the expression of genes in response to metal ions and oxidative stress. The precise mechanisms by which this occurs are not understood. To further examin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38c3d9f00b17f8fd400b233443874d36
https://doi.org/10.1093/nar/gkf432
https://doi.org/10.1093/nar/gkf432
Publikováno v:
Biochemical Pharmacology. 57:1031-1035
Many iron(III)-selective chelators possess an appreciable affinity for zinc(II) and this can prove to be undesirable when such chelators are being assessed for clinical application. At present, there is no useful test available which can reliably acc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aefd1ab21b0059ab4607a02aebee419b
https://doi.org/10.1016/s0006-2952(99)00014-3
https://doi.org/10.1016/s0006-2952(99)00014-3
Autor:
Ningmei Hu, Qingwen Li, Glen K. Andrews, Melissa A. F. Daggett, Jeffrey A. Johnson, Waihei A. Chu, Doug Bittel
Publikováno v:
Nucleic Acids Research. 26:5182-5189
The roles of the bHLH-Zip protein, upstream stimulatory factor (USF), in mouse metallothionein-I (MT-I) gene expression were examined. The promoter contains a putative USF binding site which overlaps an antioxidant response element (ARE) located at -
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9ad86420e4bb09124770f89d2acdbf4
https://doi.org/10.1093/nar/26.22.5182
https://doi.org/10.1093/nar/26.22.5182
Publikováno v:
Molecular and Cellular Biology. 17:2781-2789
The DNA-binding activity of the Zn finger protein metal response element-binding transcription factor 1 (MTF-1) was rapidly induced both in vivo in mouse Hepa cells, canine MDCK, and human HeLa cells after incubation in medium containing zinc and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d04b4b8c6298443292541df698be832
https://doi.org/10.1128/mcb.17.5.2781
https://doi.org/10.1128/mcb.17.5.2781
Autor:
Dara J. Watkins, Shui Qing Ye, Yun Yan, Karen Kover, Nataliya Kibiryeva, Doug Bittel, Wayne V. Moore, Pei Ying Tong, Lesya Novikova, Jacob Stuhlsatz, Mark A. Clements, Lisa Stehno-Bittel
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 3, p e58767 (2013)
PLoS ONE, Vol 8, Iss 3, p e58767 (2013)
Nicotinamide phosphoribosyltransferase (Nampt) is a rate-limiting enzyme in the mammalian NAD+ biosynthesis of a salvage pathway and exists in 2 known forms, intracellular Nampt (iNampt) and a secreted form, extracellular Nampt (eNampt). eNampt can g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04a6c28f82be8948f7db49e4337cc9e2
http://europepmc.org/articles/PMC3594147
http://europepmc.org/articles/PMC3594147
Publikováno v:
Journal of Biological Chemistry. 271:26233-26241
Oxidative stress (tert-butylhydroquinone) rapidly induced metallothionein-I gene expression in mouse Hepa cells, and this effect was mediated predominantly through metal response promoter elements in transient transfection assays. In vivo genomic foo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f950fcf3001bdfa7cec641ce899796c
https://doi.org/10.1074/jbc.271.42.26233
https://doi.org/10.1074/jbc.271.42.26233
Publikováno v:
The Journal of biological chemistry. 274(9)
Metal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d05eff5a8f45dafadd5a5dd5ff54f8
https://pubmed.ncbi.nlm.nih.gov/10026134
https://pubmed.ncbi.nlm.nih.gov/10026134
Autor:
M. Daggett, Doug Bittel, Waihei A. Chu, Glen K. Andrews, Tim Dalton, Jeffrey A. Johnson, Qingwen Li, N. Hu
Publikováno v:
Metallothionein IV ISBN: 9783034897990
Mouse MT-I and MT-II gene transcription is induced rapidly by heavy metals (especially Zn & Cd) [1]. Metal response elements (MRE) are essential for this induction, and these elements are present in multiple copies in the proximal promoters of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a742c37498215ad877dc7093e4c32de4
https://doi.org/10.1007/978-3-0348-8847-9_30
https://doi.org/10.1007/978-3-0348-8847-9_30
