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Titlebook: Enzymology and Molecular Biology of Carbonyl Metabolism 6; Henry Weiner,Ronald Lindahl,T. Geoffrey Flynn Book 1997 The Editor(s) (if appli

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书目名称Enzymology and Molecular Biology of Carbonyl Metabolism 6
编辑Henry Weiner,Ronald Lindahl,T. Geoffrey Flynn
视频videohttp://file.papertrans.cn/314/313128/313128.mp4
丛书名称Advances in Experimental Medicine and Biology
图书封面Titlebook: Enzymology and Molecular Biology of Carbonyl Metabolism 6;  Henry Weiner,Ronald Lindahl,T. Geoffrey Flynn Book 1997 The Editor(s) (if appli
描述Since 1982, our ever-expanding group of investigators has been meeting in exotic parts of the world to discuss aspects of three enzyme systems. The 1996 meeting was no exception. Nearly 90 scientists from 15 countries met in the small city of Deadwood, South Dakota, for four days of stimulating talks and posters and incredible scenery. Once more this meeting reflected the changing trends in biochemical research. At the 1982 meeting most of the speakers discussed isolating new enzymes and trying to characterize them. At this meeting many speakers discussed interpretations of three-dimensional struc­ ture or regulatory elements of the genes controlling for the tissue-specific expression of the enzyme. Hopefully, readers will find the proceedings of the meeting to be of interest. Though they reflects the scientific information that was presented at the meeting, they do not indicate the level of personal interactions that went on during the meeting. Once again, the willingness of the participants to discuss unpublished data and to share thoughts about the future directions of their research helped make this, like our previous seven meetings, a special scientific experience for those wh
出版日期Book 1997
关键词Drogen; biology; enzyme; enzymes; enzymology; genes; metabolism; molecular biology; protein; research; steroid
版次1
doihttps://doi.org/10.1007/978-1-4615-5871-2
isbn_softcover978-1-4613-7692-7
isbn_ebook978-1-4615-5871-2Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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Conserved Residues in the Aldehyde Dehydrogenase Family,d in binding NAD, its role is completely different from that observed for the first glycine residue of the GXGXXG motif in other dehydrogenases with traditional Rossmann folds. It was thus of interest, once the sequence was fit into the electron density, to examine the locations of strictly conserve
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Human Corneal and Lens Aldehyde Dehydrogenases,n human ALDHs have been reported, of which ALDH1, 2, 3, 5, 6, and 7 (Hsu et al, 1994), and a related enzyme, γ-amino butyraldehyde dehydrogenase (GABADH) (Kurys et al, 1993), have been thus far cloned and sequenced (Hsu et al., 1994). Sequence analysis verifies that these are closely related enzymes
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Changes in Aldehyde Dehydrogenase Isozymes Expression in Long-Term Cultures of Human Hematopoietic us bone marrow samples before reinfusion (Beran et al., 1987; Yeager et al., 1990; Carlo-Stella et al., 1994). Recently published studies from many laboratories including our own have unequivocally established that there is an associative as well as causative inverse relationship between cellular co
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Expression of ALDH3 and NMO1 in Human Corneal Epithelial and Breast Adenocarcinoma Cells,989). The hazards of UV light exposure to the eye have been recognized since the early 1900’s (van der Hoeve, 1920). Exposure to UV radiation has been linked to acute keratitis and other disorders of the ocular surface (Schein, 1992). Protein modification, extensive DNA damage and generation of reac
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A Preliminary Report on the Cloning of a Constitutively Expressed Rat Liver Cytosolic ALDH cDNA by . ALDH is located in virtually all mammalian tissues and found in all major subcellular organelles. The hepatic cDNAs for phenobarbital(PB)-inducible cytosolic ALDH, mitochondrial ALDH, microsomal ALDH, and tumor specific cytosolic ALDH have been cloned in the rat (Dunn, ., 1989; Farres, ., 1989; Mi
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