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Quality Level
assay
97%
mp
132.5-135.5 °C (lit.)
SMILES string
COc1cccc(c1)C(N)=O
InChI
1S/C8H9NO2/c1-11-7-4-2-3-6(5-7)8(9)10/h2-5H,1H3,(H2,9,10)
InChI key
VKPLPDIMEREJJF-UHFFFAOYSA-N
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Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Advances in experimental medicine and biology, 419, 249-252 (1997-01-01)
Stimulating monocytes/macrophages with bacterial lipopolysaccharide (LPS) results in TNF-alpha, IL-1, IL-6 and nitrite (NO2-) formation. Inhibitors of poly(ADP-ribose)polymerase inhibit release of these mediators by preventing mRNA expression indicating that ADP-ribosylation plays a crucial role in the synthesis of these mediators.
Journal of bacteriology, 181(4), 1348-1351 (1999-02-11)
3-Methoxybenzamide (3-MBA), which is known to be an inhibitor of ADP-ribosyltransferase, inhibits cell division in Bacillus subtilis, leading to filamentation and eventually lysis of cells. Our genetic analysis of 3-MBA-resistant mutants indicated that the primary target of the drug is
The Biochemical journal, 277 ( Pt 3), 607-610 (1991-08-01)
ADP-ribosylation of core histones was investigated in isolated nuclei of Physarum polycephalum. Core histone species differed in the mode of modification. Whereas ADP-ribosylation of H2A and H2B is sensitive to inhibition by 3-methoxybenzamide, as with most other nuclear acceptor proteins
Carcinogenesis, 12(4), 623-629 (1991-04-01)
Regulation of P(1)450 gene expression in mouse hepatocytes from responsive (C57BL/6) and non-responsive (DBA/2) strains in primary culture was investigated with respect to aryl hydrocarbon hydroxylase (AHH) activity and P450 transcript levels. Although significant induction of AHH activity in C57BL/6
Acta biologica Hungarica, 41(1-3), 19-34 (1990-01-01)
Poly(ADP-ribose)-polymerase is an important cellular regulatory enzyme which can change chromatin structure and function. Action mechanisms and activation of the enzyme are described. The synthesis of poly(ADP-ribose) can be modulated by interaction of substances with the DNA binding site of
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