[1] |
Breijyeh, Z.; Jubeh, B.; Karaman, R. Resistance of Gram-Negative Bacteria to Current Antibacterial Agents and Approaches to Resolve It. Molecules. 2020, 25, 1340.
|
[2] |
Fritzenwanker, M.; Imirzalioglu, C.; Herold, S.; Wagenlehner, F.M.; Zimmer, K.P.; Chakraborty, T. Treatment options for carbapenem-resistant gram-negative infections. Dtsch. Arztebl. Int. 2018, 115, 345–352.
|
[3] |
Nordmann, P.; Poirel, L. Epidemiology and diagnostics of carbapenem resistance in gram-negative bacteria. Clin. Infect. Dis. 2019, 69, S521–S528.
|
[4] |
Global priority list of antibiotic-resistant bacteria to guide research, discovery, and development of new antibiotics. World Health Organization. http://www.who.int/medicines/publications/WHO-PPL-Short_Summary_ 25Feb-ET_NM_WHO.pdf.
|
[5] |
Bonomo, R.A.; Burd, E.M.; Conly, J.; Limbago, B.M.; Poirel, L.; Segre, J.A.; Westblade, L.F. Carbapenemase-producing organisms: a global scourge. Clin. Infect. Dis. 2018, 66, 1290–1297.
|
[6] |
Shi, C.; Chen, J.; Kang, X.; Shen, X.; Lao, X.; Zheng, H. Approaches for the discovery of metallo-β-lactamase inhibitors: A review. ChemBiol. Drug Des. 2019, 94, 1427–1440.
|
[7] |
Tooke, C.L.; Hinchliffe, P.; Bragginton, E.C.; Colenso, C.K.; Hirvonen, V.H.A.; Takebayashi, Y.; Spencer, J. Β-lactamases and β-lactamase inhibitors in the 21st century. J. Mol. Biol. 2019, 431, 3472–3500.
|
[8] |
Linciano, P.; Cendron, L.; Gianquinto, E.; Spyrakis, F.; Tondi, D. Ten years with new Delhi metallo-β-lactamase-1 (NDM-1): from structural insights to inhibitor design. ACS Infect. Dis. 2019, 5, 9–34.
|
[9] |
Liu, B.; Trout, R.E.L.; Chu, G.H.; McGarry, D.; Jackson, R.W.; Hamrick, J.C.; Daigle, D.M.; Cusick, S.M.; Pozzi, C.; De Luca, F.; Benvenuti, M.; Mangani, S.; Docquier, J.D.; Weiss, W.J.; Pevear, D.C.; Xerri, L.; Burns, C.J. Discovery of taniborbactam (VNRX-5133): a broad-spectrum serine- and metallo-β-lactamase inhibitor for carbapenem-resistant bacterial infections. J. Med. Chem. 2020, 63, 2789–2801.
|
[10] |
Fu, B.; Zeng, Q.H.; Zhang, Z.T.; Qian, M.Y.; Chen, J.C.; Dong, W.L.; Li, M. Epicatechin gallate protects HBMVECs from ischemia/reperfusion injury through ameliorating apoptosis and autophagy and promoting neovascularization. Oxidative Med. Cell. Longev. 2019, 2019, 7824684.
|
[11] |
Esmaeelpanah, E.; Razavi, B.M.; Vahdati Hasani, F.; Hosseinzadeh, H. Evaluation of epigallocatechin gallate and epicatechin gallate effects on acrylamide-induced neurotoxicity in rats and cytotoxicity in PC 12 cells. Drug Chem. Toxicol. 2018, 41, 441–448.
|
[12] |
Sánchez-Tena, S.; Alcarraz-Vizán, G.; Marín, S.; Torres, J.L.; Cascante, M. Epicatechin gallate impairs colon cancer cell metabolic productivity. J. Agric. Food Chem. 2013, 61, 4310–4317.
|
[13] |
Satsu, H.; Awara, S.; Unno, T.; Shimizu, M. Suppressive effect of nobiletin and epicatechin gallate on fructose uptake in human intestinal epithelial Caco-2 cells. Biosci. Biotechnol. Biochem. 2018, 82, 636–646.
|
[14] |
Stevens, C.S.; Rosado, H.; Harvey, R.J.; Taylor, P.W. Epicatechin gallate, a naturally occurring polyphenol, alters the course of infection with β-lactam-resistant Staphylococcus aureus in the zebrafish embryo. Front Microbiol. 2015, 6, 1043.
|
[15] |
Huang, C.C.; Wu, W.B.; Fang, J.Y.; Chiang, H.S.; Chen, S.K.; Chen, B.H.; Chen, Y.T.; Hung, C.F. (–)-Epicatechin-3-gallate, a Green Tea Polyphenol Is a Potent Agent Against UVB-induced Damage in HaCaT Keratinocytes. Molecules. 2007, 12, 1845–1858.
|
[16] |
Han, J.X.; Xiao, C.L.; Gan, M.L.; Li, X.H.; Wang, Y.; Zheng, J.Y.; Li, D.S.; Liu, C.C.; Guan, Y.; Meng, J.Z.; Huang, S.C.; Liu, Y.S. IMB-XH1 identified as a novel inhibitor of New Delhi metallo-β-lactamase-1. J. Chin. Pharm. Sci. 2019, 28, 238–246.
|
[17] |
Farhat, N.; Khan, A.U. Evolving trends of New Delhi Metallo-betalactamse (NDM) variants: a threat to antimicrobial resistance. Infect. Genet. Evol. 2020, 86, 104588.
|
[18] |
Iovleva, A.; Doi, Y. Carbapenem-Resistant Enterobacteriaceae. Clin. Lab. Med. 2017, 37, 303–315.
|
[19] |
Tamma, P.D.; Rodriguez-Bano, J. The Use of Noncarbapenem β-Lactams for the Treatment of Extended-Spectrum β-Lactamase Infections. Clin Infect Dis. 2017, 64, 972–980.
|
[20] |
Groundwater, P.W.; Xu, S.; Lai, F.; Váradi, L.; Tan, J.; Perry, J.D.; Hibbs, D.E. New Delhi metallo-β-lactamase-1: structure, inhibitors and detection of producers. Future Med. Chem. 2016, 8, 993–1012.
|
[21] |
King, A.M.; Reid-Yu, S.A.; Wang, W.; King, D.T.; De Pascale, G.; Strynadka, N.C.; Walsh, T.R.; Coombes, B.K.; Wright, G.D. AMA overcomes antibiotic resistance by NDM and VIM metallo-β-lactamases. Nature. 2014, 510, 503–506.
|
[22] |
Porter, N.J.; Christianson, D.W. Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases. Curr. Opin. Struct. Biol. 2019, 59, 9–18.
|
[23] |
Bernstein, K.E.; Khan, Z.; Giani, J.F.; Cao, D.Y.; Bernstein, E.A.; Shen, X.Z. Angiotensin-converting enzyme in innate and adaptive immunity. Nat. Rev. Nephrol. 2018, 14, 325–336.
|
[24] |
Wang, X.; Khalil, R.A. Matrix metalloproteinases, vascular remodeling, and vascular disease. Adv. Pharmacol. 2018, 81, 241–330.
|