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Advances in Mycobacterial Isocitrate Lyase Targeting and Inhibitors

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F12%3A10127171" target="_blank" >RIV/00216208:11160/12:10127171 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.ingentaconnect.com/content/ben/cmc/2012/00000019/00000036/art00005" target="_blank" >http://www.ingentaconnect.com/content/ben/cmc/2012/00000019/00000036/art00005</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.2174/092986712804485782" target="_blank" >10.2174/092986712804485782</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Advances in Mycobacterial Isocitrate Lyase Targeting and Inhibitors

  • Original language description

    Isocitrate lyase plays a key role for survival of Mycobacterium tuberculosis in the latent form during a chronic stage of infection. This enzyme is important for M. tuberculosis during steady stage growth when it converts isocitrate to succinate and glyoxylate. Then, the glyoxylate is condensed with acetyl-CoA to form malate by malate synthase. The carbon conserving glyoxylate pathway has not been observed in mammals; therefore, it has been determined as a potential drug target for discovery of a new antituberculosis agent. Novel active molecules should shorten the duration of therapy, prevent resistance development and eliminate latent disease. The review summarizes recent progresses in isocitrate lyase inhibitors, overviews structural analogues of several metabolic intermediates (3-nitropropionate, 3-bromopyruvate, itaconate, itaconic anhydride), peptide inhibitors, and recently developed inhibitors with various chemical structures. The largest inhibitory activity against isocitrate

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FR - Pharmacology and apothecary chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/NT13346" target="_blank" >NT13346: Design and enzyme targeting of antibacterial active compounds against multidrug resistant strains</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Current Medicinal Chemistry

  • ISSN

    0929-8673

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    36

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    12

  • Pages from-to

    6126-6137

  • UT code for WoS article

    000311959800005

  • EID of the result in the Scopus database