InChI
1S/C4H6O4/c5-3(6)1-2-4(7)8/h1-2H2,(H,5,6)(H,7,8)
InChI key
KDYFGRWQOYBRFD-UHFFFAOYSA-N
SMILES string
OC(=O)CCC(O)=O
assay
≥99%
bp
235 °C (lit.)
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Application
用作亲和层析中的间隔臂。
法规信息
新产品
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Sachiko Tsukamoto et al.
Bioorganic & medicinal chemistry letters, 16(1), 69-71 (2005-10-26)
A new inhibitor of p53-HDM2 interaction was isolated from a culture of marine-derived fungus, Arthrinium sp. The structure was identified to be (-)-hexylitaconic acid (1) by spectroscopic analysis. The inhibition of p53-HDM2 binding was tested by the ELISA method, and
Ivanhoe K H Leung et al.
Journal of medicinal chemistry, 53(2), 867-875 (2009-12-23)
This report demonstrates that solvent water relaxation measurements can be used for quantitative screening of ligand binding and for mechanistic investigations of enzymes containing paramagnetic metal centers by using conventional NMR instrumentation at high field. The method was exemplified using
Christopher J Stubbs et al.
Journal of medicinal chemistry, 52(9), 2799-2805 (2009-04-15)
Limited proteolysis coupled to matrix-assisted laser desorption/ionization (MALDI) mass spectrometric analyses can be used to screen for compounds that alter protein structure by monitoring stabilizing/destabilizing effects with respect to the rate and nature of proteolysis. When applied to prolyl hydroxylase
Kuo-Liang Su et al.
Bioorganic & medicinal chemistry, 17(15), 5414-5419 (2009-07-15)
Fumarate, a four-carbon trans dicarboxylic acid, is the allosteric activator of the human mitochondrial NAD(P)(+)-dependent malic enzyme (m-NAD(P)-ME). In this paper, we discuss the effects of the structural analogues of fumarate on human m-NAD(P)-ME. Succinate, a dicarboxylic acid with a
Nathan R Rose et al.
Journal of medicinal chemistry, 51(22), 7053-7056 (2008-10-24)
The dynamic methylation of histone lysyl residues plays an important role in biology by regulating transcription, maintaining genomic integrity, and by contributing to epigenetic effects. Here we describe a variety of inhibitor scaffolds that inhibit the human 2-oxoglutarate-dependent JMJD2 subfamily
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