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Mendeleev Communications, 2016, Volume 26, Issue 3, Pages 207–208
DOI: https://doi.org/10.1016/j.mencom.2016.04.009
(Mi mendc2160)
 

This article is cited in 1 scientific paper (total in 1 paper)

Communications

Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2

M. G. Khrenovaab, I. D. Solovyevab, V. N. Azevc, G. D. Lapshinb, A. P. Savitskyb

a Department of Chemistry, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
b A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russian Federation
c Branch of M.M. Shemyakin–Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation
Full-text PDF (164 kB) Citations (1)
Abstract: A mimetic of a natural substrate of the matrix metalloproteinase MMP-2, in which the amide group with the scissile peptide bond is replaced with the oxoethylene moiety, inhibits the enzyme.
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Document Type: Article
Language: English


Citation: M. G. Khrenova, I. D. Solovyev, V. N. Azev, G. D. Lapshin, A. P. Savitsky, “Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2”, Mendeleev Commun., 26:3 (2016), 207–208
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  • https://www.mathnet.ru/eng/mendc/v26/i3/p207
  • This publication is cited in the following 1 articles:
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