The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

PubChem8163     4-nitrobenzaldehyde

Synonyms: CPD-703, AGN-PC-007OFU, CHEMBL164236, NSC-6103, ACMC-1B0H8, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of p-Nitrobenzaldehyde

 

High impact information on p-Nitrobenzaldehyde

 

Biological context of p-Nitrobenzaldehyde

 

Anatomical context of p-Nitrobenzaldehyde

 

Associations of p-Nitrobenzaldehyde with other chemical compounds

 

Gene context of p-Nitrobenzaldehyde

  • AHR-A2 exhibited a defined specificity toward p-nitrobenzaldehyde as substrate, whereas the other enzymes exhibited broad specificities toward various aliphatic, aromatic, and monosaccharide aldehydes [20].
  • This indicated that M79175 was the most effective inhibitor tested of aldose reductase with 4NB in vitro [21].
  • In untreated mice, carbonyl reductase activity towards 15KD-PGF2 alpha was not detected, whereas the activities towards PNAP and PNBA were detected, which activities were lower than those in rats and hamsters [22].
  • This radiotracer has been synthesized using nucleophilic displacement of the activated nitro group of p-nitrobenzaldehyde by NCA 18F- obtained from the 18O (p, n) reaction on enriched water [23].
  • The activity of the reductase with p-nitrobenzaldehyde and 3-indolacetaldehyde and the similarity of its physical properties with the 'low Km' aldehyde reductase of porcine brain previously reported indicates that these enzymes may be identical [24].

References

  1. Androgen-regulated expression of a novel member of the aldo-keto reductase superfamily in regrowing rat prostate. Nishi, N., Shoji, H., Miyanaka, H., Nakamura, T. Endocrinology (2000) [Pubmed]
  2. Influence of hydroxypropylcyclodextrins on the toxicity of mixtures. Lin, Z., Kong, D., Zhong, P., Yin, K., Dong, L. Chemosphere (2005) [Pubmed]
  3. Purification and characterization of rho-crystallin from Japanese common bullfrog lens. Fujii, Y., Watanabe, K., Hayashi, H., Urade, Y., Kuramitsu, S., Kagamiyama, H., Hayaishi, O. J. Biol. Chem. (1990) [Pubmed]
  4. Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. O'connor, T., Ireland, L.S., Harrison, D.J., Hayes, J.D. Biochem. J. (1999) [Pubmed]
  5. Role of cysteines in the activation and inactivation of brewers' yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein. Zeng, X., Farrenkopf, B., Hohmann, S., Dyda, F., Furey, W., Jordan, F. Biochemistry (1993) [Pubmed]
  6. Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase. Kitson, T.M. Biochem. J. (1989) [Pubmed]
  7. Active-site cobalt(II)-substituted horse liver alcohol dehydrogenase: characterization of intermediates in the oxidation and reduction processes as a function of pH. Sartorius, C., Gerber, M., Zeppezauer, M., Dunn, M.F. Biochemistry (1987) [Pubmed]
  8. Bovine lens aldehyde dehydrogenase. Kinetics and mechanism. Ting, H.H., Crabbe, M.J. Biochem. J. (1983) [Pubmed]
  9. Active site cobalt(II)-substituted liver alcohol dehydrogenase: characterization of intermediates in the reduction of p-nitrobenzaldehyde by rapid-scanning ultraviolet-visible spectroscopy. Koerber, S.C., MacGibbon, A.K., Dietrich, H., Zeppezauer, M., Dunn, M.F. Biochemistry (1983) [Pubmed]
  10. Comparison of aldose reductase inhibitors in vitro. Effects of enzyme purification and substrate type. Poulsom, R. Biochem. Pharmacol. (1987) [Pubmed]
  11. Chemical-chemical interaction between cyanogenic toxicants and aldehydes: a mechanism-based QSAR approach to assess toxicological joint effects. Lin, Z., Wei, D., Wang, X., Yin, K., Zhao, D. SAR and QSAR in environmental research. (2004) [Pubmed]
  12. Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Maser, E., Möbus, E., Xiong, G. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  13. Age-related changes in aldehyde reductase activity of rat brain, liver and heart. Cao Danh, H., Strolin Benedetti, M., Dostert, P. Gerontology. (1984) [Pubmed]
  14. Further investigation on aldehyde reductase activity in ageing rat tissues. Cao Danh, H., Pasquier-Béchet, P., Strolin Benedetti, M., Dostert, P. J. Pharm. Pharmacol. (1985) [Pubmed]
  15. Interindividual variability of carbonyl reductase levels in human livers. Iwata, N., Inazu, N., Hara, S., Yanase, T., Kano, S., Endo, T., Kuriiwa, F., Sato, Y., Satoh, T. Biochem. Pharmacol. (1993) [Pubmed]
  16. Cloning and expression of ntnD, encoding a novel NAD(P)(+)-independent 4-nitrobenzyl alcohol dehydrogenase from Pseudomonas sp. Strain TW3. James, K.D., Hughes, M.A., Williams, P.A. J. Bacteriol. (2000) [Pubmed]
  17. Photoreactivity of chloramphenicol in vitro and in vivo. de Vries, H., Hemelaar, P.J., Gevers, A.C., Beyersbergen van Henegouwen, G.M. Photochem. Photobiol. (1994) [Pubmed]
  18. Characterization of Ypr1p from Saccharomyces cerevisiae as a 2-methylbutyraldehyde reductase. Ford, G., Ellis, E.M. Yeast (2002) [Pubmed]
  19. Characterization of multiple Chinese hamster carbonyl reductases. Terada, T., Sugihara, Y., Nakamura, K., Sato, R., Sakuma, S., Fujimoto, Y., Fujita, T., Inazu, N., Maeda, M. Chem. Biol. Interact. (2001) [Pubmed]
  20. Biochemical genetics of aldehyde reductase in the mouse: Ahr-1--a new locus linked to the alcohol dehydrogenase gene complex on chromosome 3. Duley, J.A., Holmes, R.S. Biochem. Genet. (1982) [Pubmed]
  21. Inhibition of aldose reductase from human retina. Poulsom, R. Curr. Eye Res. (1987) [Pubmed]
  22. Gonadotropin-induced ovarian carbonyl reductase in mice and hamsters: comparison with carbonyl reductase in rats. Iwata, N., Inazu, N., Endo, T., Satoh, T. Life Sci. (1993) [Pubmed]
  23. A new route for the synthesis of [18F]fluoroaromatic substituted amino acids: no carrier added L-p-[18F]fluorophenylalanine. Lemaire, C., Guillaume, M., Christiaens, L., Palmer, A.J., Cantineau, R. International journal of radiation applications and instrumentation. Part A, Applied radiation and isotopes. (1987) [Pubmed]
  24. Affinity purification and properties of porcine brain aldose reductase. Boghosian, R.A., McGuinness, E.T. Biochim. Biophys. Acta (1979) [Pubmed]
 
WikiGenes - Universities