{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["He R"],"funding":["NCI NIH HHS"],"pagination":["2051-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3117672"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(12)"],"pubmed_abstract":["Tuberculosis (TB), which is caused by Mycobacterium tuberculosis (Mtb), is a major worldwide threat to public health. Mycobacterium protein tyrosine phosphatase B (mPTPB) is a virulent phosphatase secreted by Mtb, which is essential for the survival and persistence of the bacterium in the host. Consequently, small-molecule inhibitors of mPTPB are expected to serve as anti-TB agents with a novel mode of action. Herein, we report the discovery of highly potent and selective mPTPB inhibitors using a novel, double Click chemistry strategy. The most potent mPTPB inhibitor from this approach possesses a K(i) value of 160 nM and a >25-fold selectivity for mPTPB over 19 other protein tyrosine phosphatases (PTBs). Molecular docking study of the enzyme-inhibitor complex provides a rationale for the "],"journal":["ChemMedChem"],"pubmed_title":["Double click reaction for the acquisition of a highly potent and selective mPTPB inhibitor."],"pmcid":["PMC3117672"],"funding_grant_id":["R01 CA126937","CA69202","R01 CA069202","CA126937"],"pubmed_authors":["Zeng LF","Wu L","He Y","Gunawan AM","Zhang ZY","Jiang ZX","Yu Z","He R","Xu J","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"Double click reaction for the acquisition of a highly potent and selective mPTPB inhibitor.","description":"Tuberculosis (TB), which is caused by Mycobacterium tuberculosis (Mtb), is a major worldwide threat to public health. Mycobacterium protein tyrosine phosphatase B (mPTPB) is a virulent phosphatase secreted by Mtb, which is essential for the survival and persistence of the bacterium in the host. Consequently, small-molecule inhibitors of mPTPB are expected to serve as anti-TB agents with a novel mode of action. Herein, we report the discovery of highly potent and selective mPTPB inhibitors using a novel, double Click chemistry strategy. The most potent mPTPB inhibitor from this approach possesses a K(i) value of 160 nM and a >25-fold selectivity for mPTPB over 19 other protein tyrosine phosphatases (PTBs). Molecular docking study of the enzyme-inhibitor complex provides a rationale for the ","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2026-04-30T22:28:17.265Z","creation":"2026-04-07T16:22:48.713Z"},"accession":"S-EPMC3117672","cross_references":{"pubmed":["20957718"],"doi":["10.1002/cmdc.201000348"]}}