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Commun."},{"issue":"6","key":"10.1016\/j.micres.2022.127079_bib170","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.3390\/ijerph17062162","article-title":"Specific NDM-1 inhibitor of isoliquiritin enhances the activity of meropenem against NDM-1-positive Enterobacteriaceae in vitro","volume":"17","author":"Wang","year":"2020","journal-title":"Int. J. Environ. Res. Public Health"},{"key":"10.1016\/j.micres.2022.127079_bib171","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113667","article-title":"Recent research and development of NDM-1 inhibitors","volume":"223","author":"Wang","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.micres.2022.127079_bib172","unstructured":"Ma, L., Liu, H., Cui, N., 2020. New double-antibody sandwich ELISA detecting kit for detecting NDM-1 resistance protein in bacteria comprising enzyme plate coated with monoclonal antibody 3H5, detection antibody 4G1-HRP and NDM-1 protein standard. 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Lett."},{"issue":"4","key":"10.1016\/j.micres.2022.127079_bib177","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1021\/acsmedchemlett.7b00548","article-title":"Rhodanine as a potent scaffold for the development of broad-spectrum metallo-\u03b2-lactamase inhibitors","volume":"9","author":"Xiang","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"issue":"4","key":"10.1016\/j.micres.2022.127079_bib178","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1021\/ml500534c","article-title":"Azolylthioacetamide: a highly promising scaffold for the development of metallo-\u03b2-lactamase inhibitors","volume":"6","author":"Yang","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"issue":"27","key":"10.1016\/j.micres.2022.127079_bib179","doi-asserted-by":"crossref","first-page":"7836","DOI":"10.1002\/anie.201601621","article-title":"A vancomycin derivative with a pyrophosphate-binding group: a strategy to combat vancomycin-resistant bacteria","volume":"55","author":"Yarlagadda","year":"2016","journal-title":"Angew. Chem. Int. Ed."},{"issue":"7","key":"10.1016\/j.micres.2022.127079_bib180","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1021\/acsinfecdis.8b00011","article-title":"Vancomycin analogue restores meropenem activity against NDM-1 Gram-negative pathogens","volume":"4","author":"Yarlagadda","year":"2018","journal-title":"ACS Infect. 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