N8403
6-Nitroso-1,2-benzopyrone
ADP-ribosyltransferase inhibitor
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About This Item
form
solid
storage temp.
−20°C
SMILES string
O=Nc1ccc2OC(=O)C=Cc2c1
InChI
1S/C9H5NO3/c11-9-4-1-6-5-7(10-12)2-3-8(6)13-9/h1-5H
InChI key
HXTDAUGEZTYMGP-UHFFFAOYSA-N
Application
Binds to the DNA-recognizing domain of ADP-ribosyltransferase and preferentially destabilizes one of the two zinc finger polypeptide complexes. The affected enzyme loses almost all activity, but still binds to DNA.
Binds to the DNA-recognizing domain of ADP-ribosyltransferase and preferentially destabilizes one of the two zinc finger polypeptide complexes. The affected enzyme loses almost all activity, but still binds to DNA.>
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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The Biochemical journal, 436(3), 709-717 (2011-04-07)
PPTases (phosphopantetheinyl transferases) are of great interest owing to their essential roles in activating fatty acid, polyketide and non-ribosomal peptide synthetase enzymes for both primary and secondary metabolism, as well as an increasing number of biotechnological applications. However, existing techniques
Proceedings of the National Academy of Sciences of the United States of America, 105(42), 16242-16247 (2008-10-15)
Invasive insulitis is a destructive T cell-dependent autoimmune process directed against insulin-producing beta cells that is central to the pathogenesis of type 1 diabetes mellitus (T1DM) in humans and the clinically relevant nonobese diabetic (NOD) mouse model. Few therapies have
FEBS letters, 290(1-2), 181-185 (1991-09-23)
6-Nitroso-1,2-benzopyrone, an oxidation product of 6-amino-1,2-benzopyrone, binds to the DNA-recognizing domain of the ADP-ribose transferase protein and preferentially destabilizes Zn2+ from one of the two zinc finger polypeptide complexes present in the intact enzyme, as determined by the loss of
Proceedings of the National Academy of Sciences of the United States of America, 89(16), 7703-7707 (1992-08-15)
6-Nitroso-1,2-benzopyrone and 3-nitrosobenzamide, two C-nitroso compounds that inactivate the eukaryotic nuclear protein poly(ADP-ribose) polymerase [NAD+:poly(adenosine diphosphate D-ribose) ADP-D-ribosyltransferase, ADPRT, EC 2.4.2.30] at one zinc-finger site, completely suppressed the proliferation of leukemic and other malignant human cells and subsequently produced cell
Nature, 361(6411), 473-475 (1993-02-04)
Retroviral nucleocapsid and gag-precursor proteins from all known strains of retroviruses contain one or two copies of an invariant sequence, Cys-X2-Cys-X4-His-X4-Cys, that is populated with zinc in mature particles. Modification of cysteine or histidine residues results in defective packaging of
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