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A28651

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关键词:'A28651'
显示 31-37 共 37 条结果 关于 "A28651" 范围 论文
Naris Thengchaisri et al.
Microvascular research, 77(3), 356-363 (2009-03-28)
We previously demonstrated a vascular network response initiated by elevated tissue concentrations of adenosine that is distinct from the dilation caused when adenosine is applied directly to the arteriole. The purpose of this study was to elucidate the potential mechanism(s)
Shuxia Chen et al.
PloS one, 8(11), e79730-e79730 (2013-11-16)
Two phenolic compound parameters (total phenolic and flavonoid contents) and 5 antioxidant parameters (DPPH [2, 2-diphenyl-1-picrylhydrazyl] radical scavenging activity, HRSC (hydroxyl radical scavenging capacity), FRAP (ferric ion reducing antioxidant power), CUPRAC (cupric ion reducing antioxidant capacity), and MCA (metal chelating
Alexander Barthel et al.
Archiv der Pharmazie, 342(8), 445-452 (2009-07-01)
The synthesis of dimeric compounds derived from quinazolin-2-one and 1,4-benzodiazepin-2-one possessing a piperazine or homopiperazine spacer was investigated. In addition, a piperazine spacered bis-isoalloxazine and a bis-riboflavin compound were prepared and their ability to interrupt the association of prion proteins
Katalin Módis et al.
International journal of molecular medicine, 31(2), 437-446 (2012-12-13)
Liver ischemia represents a common clinical problem. In the present study, using an in vitro model of hepatic ischemia-reperfusion injury, we evaluated the potential cytoprotective effect of the purine metabolites, such as adenosine and inosine, and studied the mode of
Stefan Weber et al.
Photochemistry and photobiology, 87(3), 574-583 (2011-01-05)
Blue-light sensitive photoreceptory BLUF domains are flavoproteins, which regulate various, mostly stress-related processes in bacteria and eukaryotes. The photoreactivity of the flavin adenine dinucleotide (FAD) cofactor in three BLUF domains from Rhodobacter sphaeroides, Synechocystis sp. PCC 6803 and Escherichia coli
Olayinka O Ogunro et al.
Nano letters, 9(3), 1034-1038 (2009-02-25)
We have studied the structural and electronic stability of a helical ribbon of flavin mononucleotide wrapping around single-walled carbon nanotubes using first-principles density-functional calculations. The helical ribbon is formed through hydrogen bonding between adjacent uracil moieties of the isoalloxazine ring
Sarah Raffelberg et al.
Biological chemistry, 394(11), 1517-1528 (2013-07-06)
Flavin-binding light, oxygen, and voltage (LOV) domains are UVA/blue-light-sensing protein units that form a reversible flavin mononucleotide-cysteine adduct upon light induction. In their dark-adapted state, LOV domains exhibit the typical spectral features of fully oxidized riboflavin derivatives. A survey on
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