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Chemical Communications (Cambridge, England)|July 7, 2023
A dual covalent binder for labelling and inhibiting serine and metallo-carbapenemasesCheng Chen, Yinsui Xu, Peter Oelschlaeger, et al.
ACS Medicinal Chemistry Letters|April 20, 2018
Rhodanine as a Potent Scaffold for the Development of Broad-Spectrum Metallo-β-lactamase InhibitorsYang Xiang, Cheng Chen, Wen-Ming Wang, et al.
Bioorganic & Medicinal Chemistry Letters|September 6, 2016
Optimization of amino acid thioesters as inhibitors of metallo-β-lactamase L1Xiao-Long Liu, Ke-Wu Yang, Yue-Juan Zhang, et al.
Bioorganic & Medicinal Chemistry Letters|September 26, 2013
New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamasesKe-Wu Yang, Lei Feng, Shao-Kang Yang, et al.
ACS Infectious Diseases|November 2, 2018
Real-Time Monitoring of NDM-1 Activity in Live Bacterial Cells by Isothermal Titration Calorimetry: A New Approach To Measure Inhibition of Antibiotic-Resistant BacteriaYue-Juan Zhang, Wen-Ming Wang, Peter Oelschlaeger, et al.
ACS Medicinal Chemistry Letters|April 21, 2016
Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) InhibitorsLe Zhai, Yi-Lin Zhang, Joon S Kang, et al.
ACS Medicinal Chemistry Letters|May 20, 2017
Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase InhibitorsYa-Nan Chang, Yang Xiang, Yue-Juan Zhang, et al.
Protein Science : a Publication of the Protein Society|August 19, 2014
Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262Kevin M Pegg, Eleanor M Liu, Alex C George, et al.
Physical Chemistry Chemical Physics : PCCP|August 9, 2013
Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force fieldSusanna Monti, Alessandro Corozzi, Peter Fristrup, et al.
Bioorganic & Medicinal Chemistry Letters|November 11, 2017
Azolylthioacetamides as a potent scaffold for the development of metallo-β-lactamase inhibitorsYang Xiang, Ya-Nan Chang, Ying Ge, et al.
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