Mahmoud Kandeel, Aya Kato, Yoshiaki Kitamura, Yukio Kitade
{"title":"胸苷激酶:丢失的化疗靶点。","authors":"Mahmoud Kandeel, Aya Kato, Yoshiaki Kitamura, 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, Aya Kato, Yoshiaki Kitamura, 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}
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.