Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Alexandra Kikonyogo"'
Autor:
Marcy L. Vana, Yan Xiang, Jonathan Leis, Ashok Aiyar, Fadila Bouamr, Carol A. Carter, Alexandra Kikonyogo
Publikováno v:
Proceedings of the National Academy of Sciences. 98:11199-11204
The late assembly (L) domain of retrovirus Gag, required in the final steps of budding for efficient exit from the host cell, is thought to mediate its function through interaction with unknown cellular factors. Here, we report the identification of
Publikováno v:
European Journal of Biochemistry. 262:704-712
Low concentrations of citral (3,7-dimethyl-2,6-octadienal), an inhibitor of retinoic acid biosynthesis, inhibited E1, E2 and E3 isozymes of human aldehyde dehydrogenase (EC1.2.1.3). The inhibition was reversible on dilution and upon long incubation i
Autor:
Jonathan Leis, Carol A. Carter, Alexandra Kikonyogo, Beth E. Agresta, Lynn VerPlank, Fadila Bouamr, Tracy J. LaGrassa
Ubiquitination appears to be involved in virus particle release from infected cells. Free ubiquitin (Ub), as well as Ub covalently bound to a small fraction of p6 Gag, is detected in mature HIV particles. Here we report that the p6 region in the Pr55
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e140533042fb73097a7980177dab964
https://europepmc.org/articles/PMC35409/
https://europepmc.org/articles/PMC35409/
Autor:
Gonzalo Izaguirre, Wojciech Ambroziak, Alexandra Kikonyogo, Darryl P. Abriola, Marek Dryjanski, Regina Pietruszko
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461371465
Aldehyde dehydrogenases catalyze aldehyde dehydrogenation as well as ester hydrolysis. Nitrate esters e.g. isosorbide nitrates and nitroglycerin inhibit the enzyme. Mechanism of inhibition which involves aldehyde dehydrogenase catalyzed formation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eda6148649a08e6aae8167b1c7e7d205
https://doi.org/10.1007/978-1-4615-4735-8_10
https://doi.org/10.1007/978-1-4615-4735-8_10
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 119(4)
Methylglyoxal was demonstrated to be a substrate for the isozymes E1, E2 and E3 of human aldehyde dehydrogenase. Pyruvate was the product from the oxidation of methylglyoxal by the three isozymes. At pH 7.4 and 25 degrees C, the major and minor compo
Autor:
Jonathan Leis, Todd W. Ridky, Alexandra Kikonyogo, Alexander Wlodawer, John W. Erickson, S V Gulnik, Igor Kurinov, Terry D. Copeland, Robert W. Harrison, Irene T. Weber
Publikováno v:
Biochemistry. 37(39)
A series of mutations, first identified in protease inhibitor-resistant HIV-1 viral isolates, were introduced into HIV-1 PR as individual substitutions. Mutants containing R8K, V32I, V82T, I84V, G48V/L90M, or V82T/I84V substitutions were analyzed for
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 118(1)
The tissue distribution of the E3 isozyme of human aldehyde dehydrogenase has been investigated by three methods: enzyme activity assay employing betaine aldehyde as substrate, Western blotting employing E3 isozyme-specific antibodies, and Northern b
Autor:
Regina Pietruszko, Alexandra Kikonyogo
Publikováno v:
Molecular pharmacology. 52(2)
The histamine H2-receptor antagonists have been identified as inhibitors of human liver aldehyde dehydrogenase (EC 1.2.1.3) isozymes, E1, E2, and E3. Inhibition was strongest with the E3 isozyme, whose substrates include gamma-aminobutyraldehyde, the
Autor:
Regina Pietruszko, Alexandra Kikonyogo
Publikováno v:
The Biochemical journal. 316
Enzyme purification and characterization, cDNA cloning and Northern blot analysis were the techniques utilized during this investigation to determine the identity and occurrence of the aldehyde dehydrogenase that metabolizes γ-aminobutyraldehyde in
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461376927
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60e4c2fd5a4fbcbb76ddf8df061a37ed
https://doi.org/10.1007/978-1-4615-5871-2_28
https://doi.org/10.1007/978-1-4615-5871-2_28