SCHIFF BASES AS POTENTIAL INHIBITORS OF AMINOPEPTIDASE N AS ANTICANCER AGENTS
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14160%2F22%3A00126659" target="_blank" >RIV/00216224:14160/22:00126659 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
SCHIFF BASES AS POTENTIAL INHIBITORS OF AMINOPEPTIDASE N AS ANTICANCER AGENTS
Original language description
Many Schiff bases appear to be important intermediates in a number of enzymatic reactions. The presence of the azomethine group, as well as their interesting physical and chemical properties, cause the widespread application of their metal complexes. Synthesized groups of basic thiosemicarbazone and semicarbazone derivatives of acetophenone have these properties as well. Aminopeptidase N (AP-N), or membrane alanyl aminopeptidase (m-AAP), is a neutral zinc-binding metallopeptidase that cleaves N-terminal residues from protein and peptides. This aminopeptidase turns out to be identical to the human cluster differentiation antigen CD13 expressed on the surface of myeloid progenitors and myeloid leukemia cells.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
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OECD FORD branch
30107 - Medicinal chemistry
Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů