Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Theodore R. Holman"'
Autor:
Theodore R. Holman, Jennyfer Tena, Benjamin Liu, Benjamin E. Tourdot, Cody J. Freedman, Michael Holinstat, Abigail R. Green
Publikováno v:
Biochemistry
The reaction of 5 S,15 S-dihydroperoxyeicosatetraenoic acid (5,15-diHpETE) with human 5-lipoxygenase (LOX), human platelet 12-LOX, and human reticulocyte 15-LOX-1 was investigated to determine the reactivity and relative rates of producing lipoxins (
Autor:
Theodore R. Holman, Chakrapani Kalyanaraman, Jennyfer Tena, Matthew P. Jacobson, Gabriella Alvarez, Wan-Chen Tsai, Ansari Mukhtar Aleem, Joshua D. Deschamps
Publikováno v:
Biochemistry
Biochemistry, vol 58, iss 6
Biochemistry, vol 58, iss 6
Human platelet ALOX12 (hALOX12 or h12-LOX) has been implicated in a variety of human diseases. The present study investigates the active site of hALOX12 to more thoroughly understand how it positions the substrate and achieves nearly perfect regio- a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52f546fac581c1f96f8ac1a03aa67ffd
https://europepmc.org/articles/PMC7270147/
https://europepmc.org/articles/PMC7270147/
Autor:
Thomas Horn, Theodore R. Holman, Abigail R. Green, Jose Carlos, Jevgenij A. Raskatov, Shannon R. Barbour
Publikováno v:
Biochemistry, vol 55, iss 20
Lipoxins are an important class of lipid mediators that induce the resolution of inflammation and arise from transcellular exchange of arachidonic acid (AA)-derived lipoxygenase products. Human epithelial 15-lipoxygenase-2 (h15-LOX-2), the major lipo
Publikováno v:
Bioorganic & Medicinal Chemistry. 17:6534-6539
Recently, it has been shown that lipoxygenase (LO) products affect the substrate specificity of human 15-LO. In the current paper, we demonstrate that soybean LO-1 (sLO-1) is not affected by its own products, however, inhibitors which bind the allost
Publikováno v:
Biochemistry. 47:7364-7375
Human lipoxygenases (hLO) are a family of structurally related enzymes that catalyze the hydroperoxidation of polyunsaturated fatty acids using molecular oxygen (Scheme 1) (1). There are three main isozymes of pharmacological interest: 5-hLO, 12-hLO
Publikováno v:
Journal of the American Chemical Society. 129:7531-7537
Lipoxygenases (LOs) comprise a class of substrate activating mononuclear nonheme iron enzymes which catalyze the hydroperoxidation of unsaturated fatty acids. A commonly proposed mechanism for LO catalysis involves H-atom abstraction by an FeIII-OH-
Lipoxygenases (LOXs) regulate inflammation through the production of a variety of molecules whose specific downstream effects are not entirely understood due to the complexity of the inflammation pathway. The generation of these biomolecules can pote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d448e1da1d82ae88ef4fcac35626dbd
https://escholarship.org/uc/item/9qp948df
https://escholarship.org/uc/item/9qp948df
Autor:
Erika N. Segraves, Theodore R. Holman
Publikováno v:
Biochemistry. 42:5236-5243
Mammalian lipoxygenases have been implicated in several inflammatory disorders; however, the details of the kinetic mechanism are still not well understood. In this paper, human platelet 12-lipoxygenase (12-hLO) and human reticulocyte 15-lipoxygenase
Publikováno v:
Biochemistry. 40:7509-7517
Lipoxygenases are an important class of non-heme iron enzymes that catalyze the hydroperoxidation of unsaturated fatty acids. The details of the enzymatic mechanism of lipoxygenases are still not well understood. This study utilizes a combination of
Autor:
Rakesh Mogul, Theodore R. Holman
Publikováno v:
Biochemistry. 40:4391-4397
Lipoxygenases are currently potential targets for therapies against asthma, artherosceloris, and cancer. Recently, inhibition studies on both soybean (SLO) and human lipoxygenase (15-HLO) revealed the presence of an allosteric site that binds both su