胸苷激酶:丢失的化疗靶点。

Mahmoud Kandeel, Aya Kato, Yoshiaki Kitamura, Yukio Kitade
{"title":"胸苷激酶:丢失的化疗靶点。","authors":"Mahmoud Kandeel,&nbsp;Aya Kato,&nbsp;Yoshiaki Kitamura,&nbsp;Yukio Kitade","doi":"10.1093/nass/nrp142","DOIUrl":null,"url":null,"abstract":"<p><p>Here we highlight the unusual substrate specificity of Plasmodium falciparum thymidylate kinase (PfTMK) and the validity of the enzyme as a new drug target. Furthermore, we predict that the Anaplasma marginale enzyme has attractive domain constituents and may be functionally different from other TMPKs. We postulate that thymidylate kinases could have multiple attractive functions in pathogens and may be a new drug target against numerous microorganisms.</p>","PeriodicalId":87448,"journal":{"name":"Nucleic acids symposium series (2004)","volume":" 53","pages":"283-4"},"PeriodicalIF":0.0000,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/nrp142","citationCount":"9","resultStr":"{\"title\":\"Thymidylate kinase: the lost chemotherapeutic target.\",\"authors\":\"Mahmoud Kandeel,&nbsp;Aya Kato,&nbsp;Yoshiaki Kitamura,&nbsp;Yukio Kitade\",\"doi\":\"10.1093/nass/nrp142\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Here we highlight the unusual substrate specificity of Plasmodium falciparum thymidylate kinase (PfTMK) and the validity of the enzyme as a new drug target. Furthermore, we predict that the Anaplasma marginale enzyme has attractive domain constituents and may be functionally different from other TMPKs. We postulate that thymidylate kinases could have multiple attractive functions in pathogens and may be a new drug target against numerous microorganisms.</p>\",\"PeriodicalId\":87448,\"journal\":{\"name\":\"Nucleic acids symposium series (2004)\",\"volume\":\" 53\",\"pages\":\"283-4\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2009-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1093/nass/nrp142\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nucleic acids symposium series (2004)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1093/nass/nrp142\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleic acids symposium series (2004)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/nass/nrp142","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 9

摘要

在这里,我们强调了恶性疟原虫胸苷激酶(PfTMK)不同寻常的底物特异性,以及该酶作为新的药物靶点的有效性。此外,我们预测无原体边缘酶具有吸引域成分,可能在功能上不同于其他tmpk。我们推测胸苷酸激酶可能在病原体中具有多种吸引人的功能,并可能成为对抗多种微生物的新药物靶点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Thymidylate kinase: the lost chemotherapeutic target.

Here we highlight the unusual substrate specificity of Plasmodium falciparum thymidylate kinase (PfTMK) and the validity of the enzyme as a new drug target. Furthermore, we predict that the Anaplasma marginale enzyme has attractive domain constituents and may be functionally different from other TMPKs. We postulate that thymidylate kinases could have multiple attractive functions in pathogens and may be a new drug target against numerous microorganisms.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信