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Chemical Compound Review

PubChem13763     1-chloropyrrolidine-2,5-dione

Synonyms: NSC-8748, ACMC-1BTMO, AG-C-95372, AG-D-58228, CHEMBL2107513, ...
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Disease relevance of NCS


High impact information on NCS


Biological context of NCS

  • Monoclonal antibodies to epitopes 2 and 3, which exhibit some overlap in binding to M protein but do not reverse transcription inhibition, were mapped by cleavage with N-chlorosuccinimide at regions in a carboxy direction from epitope 1 [11].
  • These MAbs, designated 36-6-6 and 36-6-8, react with N-chlorosuccinimide cleavage products of P. aeruginosa elastase, consistent with the recognition of a 13.9-kDa fragment which contains the active site [12].

Anatomical context of NCS

  • These results suggest that NCS potentiates cholinergically induced contraction by decreasing cholinesterase activity and that the oxidation of cholinesterase may cause hyperresponsiveness of airway smooth muscle by inhibition of the enzyme activity [13].
  • Removal of the epithelium shifted the dose-response curves to ACh to lower concentrations, but NCS showed similar effects on dose-response curves to ACh with and without the epithelium [13].
  • We incubated rSLPI and alpha 1-PI with N-chlorosuccinimide (NCS), chloramines, activated polymorphonuclear leucocytes (PMNs) and activated alveolar macrophages (AMs) [14].
  • The pure proteins were exposed to 1 of 4 different oxidizing systems: N-chlorosuccinimide (chemical oxidation), myeloperoxidase plus peroxide and halide (enzymatic oxidation), activated neutrophils (cellular oxidation), or gas-phase cigarette smoke [15].

Associations of NCS with other chemical compounds


Gene context of NCS

  • However, endoglycosidase digestion (using N-glycanase and endoglycosidase H) and peptide mapping (using V8 protease and N-chlorosuccinimide) strongly suggested that CD22 and CD21 are distinct gene products [21].
  • Inactivation of the antiprotease activity of SLPI or its C-terminal domain by an oxidizing agent (N-chlorosuccinimide) abolished their stimulatory effect on HGF production [22].
  • The profile of N-chlorosuccinimide cleavage products derived from each 32P-labeled p50 protein were also identical when resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis [23].
  • Oxidation of methionine(s) of fragment 78-148 with N-chlorosuccinimide removes the ability of this fragment to stimulate the ATPase [24].
  • Alpha 1 PI (MM type), modified by oxidation with N-chlorosuccinimide, shows a reduced binding affinity for FAnhCT (Kassoc = 6.5 x 10(5) M-1) and no measurable binding with FMeCT (Kassoc less than 1 x 10(4) M-1) [25].

Analytical, diagnostic and therapeutic context of NCS


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  3. Oxidative stress decreases pHi and Na(+)/H(+) exchange and increases excitability of solitary complex neurons from rat brain slices. Mulkey, D.K., Henderson, R.A., Ritucci, N.A., Putnam, R.W., Dean, J.B. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
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  10. Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the HeLa cell division cycle. Russo, G.L., Vandenberg, M.T., Yu, I.J., Bae, Y.S., Franza, B.R., Marshak, D.R. J. Biol. Chem. (1992) [Pubmed]
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  13. Chemical oxidant potentiates electrically and acetylcholine-induced contraction in rat trachea: possible involvement of cholinesterase inhibition. Ohrui, T., Sekizawa, K., Yamauchi, K., Ohkawara, Y., Nakazawa, H., Aikawa, T., Sasaki, H., Takishima, T. J. Pharmacol. Exp. Ther. (1991) [Pubmed]
  14. Comparative loss of activity of recombinant secretory leukoprotease inhibitor and alpha 1-protease inhibitor caused by different forms of oxidative stress. Vogelmeier, C., Biedermann, T., Maier, K., Mazur, G., Behr, J., Krombach, F., Buhl, R. Eur. Respir. J. (1997) [Pubmed]
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  22. Secretory leukoprotease inhibitor augments hepatocyte growth factor production in human lung fibroblasts. Kikuchi, T., Abe, T., Yaekashiwa, M., Tominaga, Y., Mitsuhashi, H., Satoh, K., Nakamura, T., Nukiwa, T. Am. J. Respir. Cell Mol. Biol. (2000) [Pubmed]
  23. A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein (hsp90) is the same protein complexed with pp60v-src hsp90 in cells transformed by the Rous sarcoma virus. Whitelaw, M.L., Hutchison, K., Perdew, G.H. J. Biol. Chem. (1991) [Pubmed]
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