{"title":"肽去甲酰基酶抑制剂解决细菌耐药性问题","authors":"T. Kumari, R. Arora, R. Kakkar","doi":"10.15866/IREBIC.V4I1.1582","DOIUrl":null,"url":null,"abstract":"Peptide Deformylase (PDF) is an attractive antibacterial target, and is gaining much momentum in contemporary research because of its remarkable features. This article reviews the bacterial PDF structure and criteria required for designing novel PDF inhibitors. It also presents a summary of the known and recently explored classes of PDF inhibitors, both peptidic and non-peptidic","PeriodicalId":14377,"journal":{"name":"International Review of Biophysical Chemistry","volume":"125 1 1","pages":"19-48"},"PeriodicalIF":0.0000,"publicationDate":"2013-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Peptide Deformylase Inhibitors for Addressing the Issue of Bacterial Resistance\",\"authors\":\"T. Kumari, R. Arora, R. Kakkar\",\"doi\":\"10.15866/IREBIC.V4I1.1582\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Peptide Deformylase (PDF) is an attractive antibacterial target, and is gaining much momentum in contemporary research because of its remarkable features. This article reviews the bacterial PDF structure and criteria required for designing novel PDF inhibitors. It also presents a summary of the known and recently explored classes of PDF inhibitors, both peptidic and non-peptidic\",\"PeriodicalId\":14377,\"journal\":{\"name\":\"International Review of Biophysical Chemistry\",\"volume\":\"125 1 1\",\"pages\":\"19-48\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-02-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Review of Biophysical Chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15866/IREBIC.V4I1.1582\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Review of Biophysical Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15866/IREBIC.V4I1.1582","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Peptide Deformylase Inhibitors for Addressing the Issue of Bacterial Resistance
Peptide Deformylase (PDF) is an attractive antibacterial target, and is gaining much momentum in contemporary research because of its remarkable features. This article reviews the bacterial PDF structure and criteria required for designing novel PDF inhibitors. It also presents a summary of the known and recently explored classes of PDF inhibitors, both peptidic and non-peptidic