Exploring Aspartate Transcarbamoylase: A Promising Broad-Spectrum Target for Drug Development
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F25%3A73630592" target="_blank" >RIV/61989592:15110/25:73630592 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15640/25:73630592
Result on the web
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202401009" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202401009</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/cbic.202401009" target="_blank" >10.1002/cbic.202401009</a>
Alternative languages
Result language
angličtina
Original language name
Exploring Aspartate Transcarbamoylase: A Promising Broad-Spectrum Target for Drug Development
Original language description
Pyrimidine nucleotides are essential for a wide variety of cellular processes and are synthesized either via a salvage pathway or through de novo biosynthesis. The latter is particularly important in proliferating cells, such as infectious diseases and cancer cells. Aspartate transcarbamoylase (ATCase) catalyzes the first committed and rate-limiting step in the de novo pyrimidine biosynthesis pathway, making it an attractive therapeutic target for various diseases. This review summarizes the development of a series of allosteric ATCase inhibitors, advancing them as potential candidates for malarial, tuberculosis and cancer therapies. Furthermore, it explores the potential for these compounds to be expanded into drugs targeting neglected tropical diseases, antimicrobial-resistant infections caused by the ESKAPE pathogens, and their possible application as herbicides. We identify the likely equivalent allosteric pocket in these systems and perform a structure and sequence-based analysis of the residues comprising it, providing a rationale for continued exploration of this compound series as both specific and broad-range inhibitors. The review concludes by emphasizing the importance of continued research into ATCase inhibitors, given their potential broad applicability in treating diverse diseases to enhance both human health and agricultural practices.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30104 - Pharmacology and pharmacy
Result continuities
Project
<a href="/en/project/LX22NPO5102" target="_blank" >LX22NPO5102: National institute for cancer research</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
CHEMBIOCHEM
ISSN
1439-4227
e-ISSN
1439-7633
Volume of the periodical
26
Issue of the periodical within the volume
7
Country of publishing house
DE - GERMANY
Number of pages
11
Pages from-to
nestránkováno
UT code for WoS article
001454045000001
EID of the result in the Scopus database
2-s2.0-105000274221