Zobrazeno 1 - 10 of 56 pro vyhledávání: '"H. A. Dailey"'
1
Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters
Autor: H A, Dailey, T A, Dailey, C K, Wu, A E, Medlock, K F, Wang, J P, Rose, B C, Wang
Publikováno v: Cellular and Molecular Life Sciences. 57:1909-1926
Ferrochelatase (E.C. 4.99.1.1, protoheme ferrolyase) catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme (heme). In the past 2 years, the crystal structures of ferrochelatases from the bacterium Bacillus subtilis and huma
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1160aa7b274620bab9de8cb8bbc276dd
https://doi.org/10.1007/pl00000672
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3
Biphasic Ordered Induction of Heme Synthesis in Differentiating Murine Erythroleukemia Cells: Role of Erythroid 5-Aminolevulinate Synthase
Autor: H Lake-Bullock, H A Dailey
Publikováno v: Molecular and Cellular Biology. 13:7122-7132
During dimethyl sulfoxide (DMSO)-stimulated differentiation of murine erythroleukemia (MEL) cells, one of the early events is the induction of the heme biosynthetic pathway. While recent reports have clearly demonstrated that GATA-1 is involved in th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::481423c75d3d24bd01a0563030fd0c34
https://doi.org/10.1128/mcb.13.11.7122-7132.1993
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4
Expression of mammalian 5-aminolevulinate synthase in Escherichia coli. Overproduction, purification, and characterization
Autor: H A Dailey, Gloria C. Ferreira
Publikováno v: Journal of Biological Chemistry. 268:584-590
5-Aminolevulinate synthase catalyzes the first step of the heme biosynthetic pathway in nonplant higher eukaryotes. A cDNA encoding for the mouse erythroid 5-aminolevulinate synthase (Schoenhaut, D. S., and Curtis, P.J. (1986) Gene (Amst.) 48, 55-63)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0d02cc7b5aa827005b03a3bcc668369d
https://doi.org/10.1016/s0021-9258(18)54191-0
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5
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis
Autor: C K, Wu, H A, Dailey, J P, Rose, A, Burden, V M, Sellers, B C, Wang
Publikováno v: Nature structural biology. 8(2)
Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 A structure from the single wavelength i
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7097c4a0917db500ac11f18a26fdddfc
https://pubmed.ncbi.nlm.nih.gov/11175906
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6
Use of recombinant human ferrochelatase as a sensitive bioassay for N-alkylprotoporphyrin IX formed after interaction of porphyrinogenic xenobiotics with rat liver microsomes
Autor: J T, Gamble, S G, Wong, H A, Dailey, G S, Marks
Publikováno v: Canadian journal of physiology and pharmacology. 78(7)
Several porphyrinogenic xenobiotics elicit mechanism-based inactivation of cytochrome P450 (CYP) isozymes, leading to the formation of N-alkylprotoporphyrin IX (N-alkylPP), a potent inhibitor of ferrochelatase, the terminal enzyme in heme biosynthesi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc542ecf74ab61be8845aec5a0711f52
https://pubmed.ncbi.nlm.nih.gov/10926165
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7
Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster
Autor: V M, Sellers, K F, Wang, M K, Johnson, H A, Dailey
Publikováno v: The Journal of biological chemistry. 273(35)
In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::70457bcc9e3f5428003cbaeb95eb5060
https://pubmed.ncbi.nlm.nih.gov/9712849
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8
Examination of ferrochelatase mutations that cause erythropoietic protoporphyria
Autor: V M, Sellers, T A, Dailey, H A, Dailey
Publikováno v: Blood. 91(10)
Ferrochelatase (E.C. 4.99.1.1), the enzyme that catalyzes the terminal step in the heme biosynthetic pathway, is the site of defect in the human inherited disease erythropoietic protoporphyria (EPP). Previously it has been demonstrated that patients
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5bd23e5f66fe369df74d4290922a75ab
https://pubmed.ncbi.nlm.nih.gov/9573038
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9
Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus
Autor: T A, Dailey, H A, Dailey
Publikováno v: The Journal of biological chemistry. 273(22)
A large number of FAD-containing proteins have previously been shown to contain a signature sequence that is referred to as the dinucleotide binding motif. Protoporphyrinogen oxidase (PPO), the penultimate enzyme of the heme biosynthetic pathway, is
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::547e6f9fa0730e39ee21dc5ef7befd36
https://pubmed.ncbi.nlm.nih.gov/9593705
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10
Variegate porphyria in South Africa, 1688-1996--new developments in an old disease
Autor: R J, Hift, P N, Meissner, A V, Corrigall, M R, Ziman, L A, Petersen, D M, Meissner, B P, Davidson, J, Sutherland, H A, Dailey, R E, Kirsch
Publikováno v: South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde. 87(6)
Variegate porphyria, an autosomal dominant inherited trait resulting in decreased activity of protoporphyrinogen oxidase, the penultimate haem biosynthetic enzyme, is characterised clinically by photosensitive skin disease and a propensity to acute n
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::10853a26291ff084ae1b54f1bb61be84
https://pubmed.ncbi.nlm.nih.gov/9254745
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