메뉴 건너뛰기




Volumn 50, Issue , 2019, Pages 101-110

Will morphing boron-based inhibitors beat the β-lactamases?

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; VABORBACTAM; ANTIINFECTIVE AGENT; BETA LACTAMASE INHIBITOR; BORON;

EID: 85064319209     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2019.03.001     Document Type: Review
Times cited : (71)

References (71)
  • 1
    • 62449089680 scopus 로고    scopus 로고
    • Microbial drug discovery: 80 years of progress
    • Demain, A.L., Sanchez, S., Microbial drug discovery: 80 years of progress. J Antibiot 62 (2009), 5–16.
    • (2009) J Antibiot , vol.62 , pp. 5-16
    • Demain, A.L.1    Sanchez, S.2
  • 2
    • 84925441504 scopus 로고    scopus 로고
    • Molecular targets of β-lactam-based antimicrobials: beyond the usual suspects
    • Konaklieva, M.I., Molecular targets of β-lactam-based antimicrobials: beyond the usual suspects. Antibiotics 3 (2014), 128–142.
    • (2014) Antibiotics , vol.3 , pp. 128-142
    • Konaklieva, M.I.1
  • 3
    • 84900847839 scopus 로고    scopus 로고
    • Discovery and preclinical development of new antibiotics
    • Hughes, D., Karlen, A., Discovery and preclinical development of new antibiotics. Ups J Med Sci 119 (2014), 162–169.
    • (2014) Ups J Med Sci , vol.119 , pp. 162-169
    • Hughes, D.1    Karlen, A.2
  • 4
    • 29144477176 scopus 로고    scopus 로고
    • Bacterial cell wall synthesis: new insights from localization studies
    • Scheffers, D.J., Pinho, M.G., Bacterial cell wall synthesis: new insights from localization studies. Microbiol Mol Biol Rev 69 (2005), 585–607.
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 585-607
    • Scheffers, D.J.1    Pinho, M.G.2
  • 5
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D.J., Strominger, J.L., Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci U S A 54 (1965), 1133–1141.
    • (1965) Proc Natl Acad Sci U S A , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 6
    • 84977073918 scopus 로고    scopus 로고
    • The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam
    • Wang, D.Y., Abboud, M.I., Markoulides, M.S., Brem, J., Schofield, C.J., The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam. Future Med Chem 8 (2016), 1063–1084.
    • (2016) Future Med Chem , vol.8 , pp. 1063-1084
    • Wang, D.Y.1    Abboud, M.I.2    Markoulides, M.S.3    Brem, J.4    Schofield, C.J.5
  • 7
    • 0000123301 scopus 로고
    • An enzyme from bacteria able to destroy penicillin
    • Abraham, E.P., Chain, E., An enzyme from bacteria able to destroy penicillin. Nature, 146, 1940, 837.
    • (1940) Nature , vol.146 , pp. 837
    • Abraham, E.P.1    Chain, E.2
  • 8
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of β-lactamase inhibitors
    • Drawz, S.M., Bonomo, R.A., Three decades of β-lactamase inhibitors. Clin Microbiol Rev 23 (2010), 160–201.
    • (2010) Clin Microbiol Rev , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 9
    • 85011311161 scopus 로고    scopus 로고
    • Mechanisms of antibiotic resistance
    • Munita, J.M., Arias, C.A., Mechanisms of antibiotic resistance. Microbiol Spectr, 4, 2016, 10.1128/microbiolspec.VMBF-0016-2015.
    • (2016) Microbiol Spectr , vol.4
    • Munita, J.M.1    Arias, C.A.2
  • 11
    • 21244488243 scopus 로고    scopus 로고
    • Revised Ambler classification of β-lactamases
    • Hall, B.G., Barlow, M., Revised Ambler classification of β-lactamases. J Antimicrob Chemother 55 (2005), 1050–1051.
    • (2005) J Antimicrob Chemother , vol.55 , pp. 1050-1051
    • Hall, B.G.1    Barlow, M.2
  • 12
    • 0030292866 scopus 로고    scopus 로고
    • Molecular evolution of bacterial β-lactam resistance
    • Knox, J.R., Moews, P.C., Frere, J.-M., Molecular evolution of bacterial β-lactam resistance. Chem Biol 3 (1996), 937–947.
    • (1996) Chem Biol , vol.3 , pp. 937-947
    • Knox, J.R.1    Moews, P.C.2    Frere, J.-M.3
  • 13
    • 0035992370 scopus 로고    scopus 로고
    • Molecular analysis of β-lactamase structure and function
    • Majiduddin, F.K., Materon, I.C., Palzkill, T.G., Molecular analysis of β-lactamase structure and function. J Med Microbiol 292 (2002), 127–137.
    • (2002) J Med Microbiol , vol.292 , pp. 127-137
    • Majiduddin, F.K.1    Materon, I.C.2    Palzkill, T.G.3
  • 14
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Palzkill, T., Metallo-β-lactamase structure and function. Ann N Y Acad Sci 1277 (2013), 91–104.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 16
    • 85034739279 scopus 로고    scopus 로고
    • New Delhi metallo-β-lactamase 1 catalyzes avibactam and aztreonam hydrolysis
    • e01224-e01217
    • Lohans, C.T., Brem, J., Schofield, C.J., New Delhi metallo-β-lactamase 1 catalyzes avibactam and aztreonam hydrolysis. Antimicrob Agents Chemother, 61, 2017 e01224-e01217.
    • (2017) Antimicrob Agents Chemother , vol.61
    • Lohans, C.T.1    Brem, J.2    Schofield, C.J.3
  • 17
    • 84863905057 scopus 로고    scopus 로고
    • Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor
    • Demonstration that the diazabicyclooctane Avibactam reacts reversibly with serine-β lactamases to form a hydrolytically stable acyl–enzyme complex.
    • Ehmann, D.E., Jahić, H., Ross, P.L., Gu, R.-F., Hu, J., Kern, G., Walkup, G.K., Fisher, S.L., Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor. Proc Natl Acad Sci U S A 109 (2012), 11663–11668 Demonstration that the diazabicyclooctane Avibactam reacts reversibly with serine-β lactamases to form a hydrolytically stable acyl–enzyme complex.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 11663-11668
    • Ehmann, D.E.1    Jahić, H.2    Ross, P.L.3    Gu, R.-F.4    Hu, J.5    Kern, G.6    Walkup, G.K.7    Fisher, S.L.8
  • 20
    • 0003922509 scopus 로고    scopus 로고
    • Organic Chemistry
    • edn 1 Oxford University Press Oxford
    • Clayden, J., Greeves, N., Warren, S.G., Organic Chemistry. edn 1, 2001, Oxford University Press, Oxford.
    • (2001)
    • Clayden, J.1    Greeves, N.2    Warren, S.G.3
  • 21
    • 84885172034 scopus 로고    scopus 로고
    • New β-phospholactam as a carbapenem transition state analog: synthesis of a broad-spectrum inhibitor of metallo-β-lactamases
    • Yang, K.W., Feng, L., Yang, S.K., Aitha, M., LaCuran, A.E., Oelschlaeger, P., Crowder, M.W., New β-phospholactam as a carbapenem transition state analog: synthesis of a broad-spectrum inhibitor of metallo-β-lactamases. Bioorg Med Chem Lett 23 (2013), 5855–5859.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 5855-5859
    • Yang, K.W.1    Feng, L.2    Yang, S.K.3    Aitha, M.4    LaCuran, A.E.5    Oelschlaeger, P.6    Crowder, M.W.7
  • 23
    • 85026356593 scopus 로고    scopus 로고
    • The versatility of boron in biological target engagement
    • Analysis of the reactions of electrophiles with biological functional groups leading to the conclusion that boron has unique chameleon-like properties.
    • Diaz, D.B., Yudin, A.K., The versatility of boron in biological target engagement. Nat Chem 9 (2017), 731–742 Analysis of the reactions of electrophiles with biological functional groups leading to the conclusion that boron has unique chameleon-like properties.
    • (2017) Nat Chem , vol.9 , pp. 731-742
    • Diaz, D.B.1    Yudin, A.K.2
  • 25
    • 84884844714 scopus 로고    scopus 로고
    • Selective sensing of saccharides using simple boronic acids and their aggregates
    • Wu, X., Li, Z., Chen, X.X., Fossey, J.S., James, T.D., Jiang, Y.B., Selective sensing of saccharides using simple boronic acids and their aggregates. Chem Soc Rev 42 (2013), 8032–8048.
    • (2013) Chem Soc Rev , vol.42 , pp. 8032-8048
    • Wu, X.1    Li, Z.2    Chen, X.X.3    Fossey, J.S.4    James, T.D.5    Jiang, Y.B.6
  • 27
    • 0034625157 scopus 로고    scopus 로고
    • Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 β-lactamase
    • Ness, S., Martin, R., Kindler, A.M., Paetzel, M., Gold, M., Jensen, S.E., Jones, J.B., Strynadka, N.C., Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 β-lactamase. Biochemistry 39 (2000), 5312–5321.
    • (2000) Biochemistry , vol.39 , pp. 5312-5321
    • Ness, S.1    Martin, R.2    Kindler, A.M.3    Paetzel, M.4    Gold, M.5    Jensen, S.E.6    Jones, J.B.7    Strynadka, N.C.8
  • 28
    • 33846842713 scopus 로고    scopus 로고
    • CRC Handbook of Chemistry and Physics: A Ready-Reference Book of Chemical and Physical Data
    • edn 97 CRC Press Boca Raton (Florida)
    • Mettam, W.M., Adams, L.B., CRC Handbook of Chemistry and Physics: A Ready-Reference Book of Chemical and Physical Data. edn 97, 2016, CRC Press, Boca Raton (Florida).
    • (2016)
    • Mettam, W.M.1    Adams, L.B.2
  • 31
    • 0142245584 scopus 로고    scopus 로고
    • Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase
    • Cama, E., Shin, H., Christianson, D.W., Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase. J Am Chem Soc 125 (2003), 13052–13057.
    • (2003) J Am Chem Soc , vol.125 , pp. 13052-13057
    • Cama, E.1    Shin, H.2    Christianson, D.W.3
  • 32
    • 33748443001 scopus 로고    scopus 로고
    • Bortezomib (Velcade trade mark) in the treatment of multiple myeloma
    • Field-Smith, A., Morgan, G.J., Davies, F.E., Bortezomib (Velcade trade mark) in the treatment of multiple myeloma. Ther Clin Risk Manag 2 (2006), 271–279.
    • (2006) Ther Clin Risk Manag , vol.2 , pp. 271-279
    • Field-Smith, A.1    Morgan, G.J.2    Davies, F.E.3
  • 33
    • 84930188536 scopus 로고    scopus 로고
    • Bortezomib-resistant mutant proteasomes: structural and biochemical evaluation with carfilzomib and ONX 0914
    • Huber, E.M., Heinemeyer, W., Groll, M., Bortezomib-resistant mutant proteasomes: structural and biochemical evaluation with carfilzomib and ONX 0914. Structure 23 (2015), 407–417.
    • (2015) Structure , vol.23 , pp. 407-417
    • Huber, E.M.1    Heinemeyer, W.2    Groll, M.3
  • 34
    • 80051691845 scopus 로고    scopus 로고
    • In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells
    • Chauhan, D., Tian, Z., Zhou, B., Kuhn, D., Orlowski, R., Raje, N., Richardson, P., Anderson, K.C., In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells. Clin Cancer Res 17 (2011), 5311–5321.
    • (2011) Clin Cancer Res , vol.17 , pp. 5311-5321
    • Chauhan, D.1    Tian, Z.2    Zhou, B.3    Kuhn, D.4    Orlowski, R.5    Raje, N.6    Richardson, P.7    Anderson, K.C.8
  • 35
    • 84944742995 scopus 로고    scopus 로고
    • Analysis of the resistance mechanism of a benzoxaborole inhibitor reveals insight into the leucyl-tRNA synthetase editing mechanism
    • Zhao, H., Palencia, A., Seiradake, E., Ghaemi, Z., Cusack, S., Luthey-Schulten, Z., Martinis, S., Analysis of the resistance mechanism of a benzoxaborole inhibitor reveals insight into the leucyl-tRNA synthetase editing mechanism. ACS Chem Biol 10 (2015), 2277–2285.
    • (2015) ACS Chem Biol , vol.10 , pp. 2277-2285
    • Zhao, H.1    Palencia, A.2    Seiradake, E.3    Ghaemi, Z.4    Cusack, S.5    Luthey-Schulten, Z.6    Martinis, S.7
  • 37
    • 85052318433 scopus 로고    scopus 로고
    • Meropenem/vaborbactam: a review in complicated urinary tract infections
    • Dhillon, S., Meropenem/vaborbactam: a review in complicated urinary tract infections. Drugs 78 (2018), 1259–1270.
    • (2018) Drugs , vol.78 , pp. 1259-1270
    • Dhillon, S.1
  • 38
    • 84981356473 scopus 로고    scopus 로고
    • Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
    • Demonstration by biochemical, crystallographic and microbiological analyses that bicyclic boronates have potential as broad spectrum inhibitors of serine-β-lactamases and metalo-β-lactamases.
    • Brem, J., Cain, R., Cahill, S., McDonough, M.A., Clifton, I.J., Jiménez-Castellanos, J.-C., Avison, M.B., Spencer, J., Fishwick, C.W.G., Schofield, C.J., Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates. Nat Commun, 7, 2016, 12406 Demonstration by biochemical, crystallographic and microbiological analyses that bicyclic boronates have potential as broad spectrum inhibitors of serine-β-lactamases and metalo-β-lactamases.
    • (2016) Nat Commun , vol.7
    • Brem, J.1    Cain, R.2    Cahill, S.3    McDonough, M.A.4    Clifton, I.J.5    Jiménez-Castellanos, J.-C.6    Avison, M.B.7    Spencer, J.8    Fishwick, C.W.G.9    Schofield, C.J.10
  • 39
    • 85032861340 scopus 로고    scopus 로고
    • Structural/mechanistic insights into the efficacy of nonclassical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates
    • Calvopina, K., Hinchliffe, P., Brem, J., Heesom, K.J., Johnson, S., Cain, R., Lohans, C.T., Fishwick, C.W.G., Schofield, C.J., Spencer, J., et al. Structural/mechanistic insights into the efficacy of nonclassical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates. Mol Microbiol 106 (2017), 492–504.
    • (2017) Mol Microbiol , vol.106 , pp. 492-504
    • Calvopina, K.1    Hinchliffe, P.2    Brem, J.3    Heesom, K.J.4    Johnson, S.5    Cain, R.6    Lohans, C.T.7    Fishwick, C.W.G.8    Schofield, C.J.9    Spencer, J.10
  • 40
    • 84979133539 scopus 로고
    • Ueber Monophenylborchlorid und einige Derivate desselben
    • Michaelis, A., Becker, P., Ueber Monophenylborchlorid und einige Derivate desselben. Ber Dtsch Chem Ges 15 (1882), 180–185.
    • (1882) Ber Dtsch Chem Ges , vol.15 , pp. 180-185
    • Michaelis, A.1    Becker, P.2
  • 41
    • 78651380622 scopus 로고    scopus 로고
    • Natural and synthetic small boron-containing molecules as potential inhibitors of bacterial and fungal quorum sensing
    • Dembitsky, V.M., Al Quntar, A.A., Srebnik, M., Natural and synthetic small boron-containing molecules as potential inhibitors of bacterial and fungal quorum sensing. Chem Rev 111 (2011), 209–237.
    • (2011) Chem Rev , vol.111 , pp. 209-237
    • Dembitsky, V.M.1    Al Quntar, A.A.2    Srebnik, M.3
  • 42
    • 0015183523 scopus 로고
    • Effect of electrolytes on the activity and iodine sensitivity of penicillinase from B. cereus
    • Dobozy, O., Mile, I., Ferencz, I., Csanyi, V., Effect of electrolytes on the activity and iodine sensitivity of penicillinase from B. cereus. Acta Biochim Biophys Acad Sci Hung 6 (1971), 97–105.
    • (1971) Acta Biochim Biophys Acad Sci Hung , vol.6 , pp. 97-105
    • Dobozy, O.1    Mile, I.2    Ferencz, I.3    Csanyi, V.4
  • 44
    • 85013654812 scopus 로고    scopus 로고
    • Exploring the potential of boronic acids as inhibitors of OXA-24/40 β-lactamase
    • Werner, J.P., Mitchell, J.M., Taracila, M.A., Bonomo, R.A., Powers, R.A., Exploring the potential of boronic acids as inhibitors of OXA-24/40 β-lactamase. Protein Sci 26 (2017), 515–526.
    • (2017) Protein Sci , vol.26 , pp. 515-526
    • Werner, J.P.1    Mitchell, J.M.2    Taracila, M.A.3    Bonomo, R.A.4    Powers, R.A.5
  • 46
    • 17644390560 scopus 로고    scopus 로고
    • Structure, function, and inhibition along the reaction coordinate of CTX-M β-lactamases
    • Chen, Y., Shoichet, B., Bonnet, R., Structure, function, and inhibition along the reaction coordinate of CTX-M β-lactamases. J Am Chem Soc 127 (2005), 5423–5434.
    • (2005) J Am Chem Soc , vol.127 , pp. 5423-5434
    • Chen, Y.1    Shoichet, B.2    Bonnet, R.3
  • 49
    • 84908191838 scopus 로고    scopus 로고
    • Interactions of “bora-penicilloates” with serine β-lactamases and DD-peptidases
    • Studies on the interaction of penicilloanate analogues in which the β-lactam derived carboxylate is replaced with a boronic acid.
    • Dzhekieva, L., Adediran, S.A., Pratt, R.F., Interactions of “bora-penicilloates” with serine β-lactamases and DD-peptidases. Biochemistry 53 (2014), 6530–6538 Studies on the interaction of penicilloanate analogues in which the β-lactam derived carboxylate is replaced with a boronic acid.
    • (2014) Biochemistry , vol.53 , pp. 6530-6538
    • Dzhekieva, L.1    Adediran, S.A.2    Pratt, R.F.3
  • 50
    • 0032708345 scopus 로고    scopus 로고
    • Arginase-boronic acid complex highlights a physiological role in erectile function
    • Cox, J.D., Kim, N.N., Traish, A.M., Christianson, D.W., Arginase-boronic acid complex highlights a physiological role in erectile function. Nat Struct Biol 6 (1999), 1043–1047.
    • (1999) Nat Struct Biol , vol.6 , pp. 1043-1047
    • Cox, J.D.1    Kim, N.N.2    Traish, A.M.3    Christianson, D.W.4
  • 53
    • 85064317578 scopus 로고    scopus 로고
    • VenatoRx Pharmaceuticals to present its lead clinical antibacterial candidate, VNRX-5133
    • Reveals the bicyclic boronate VNRX-5133 as a broad-spectrum β-lactamase inhibitor.
    • VenatoRx, VenatoRx Pharmaceuticals to present its lead clinical antibacterial candidate, VNRX-5133. American Chemical Society National Meeting, 2018 Reveals the bicyclic boronate VNRX-5133 as a broad-spectrum β-lactamase inhibitor.
    • (2018) American Chemical Society National Meeting
    • VenatoRx1
  • 56
    • 85060161135 scopus 로고    scopus 로고
    • Ceftazidime/Avibactam, Meropenem/Vaborbactam, or both? Clinical and formulary considerations
    • Pogue, J.M., Bonomo, R.A., Kaye, K.S., Ceftazidime/Avibactam, Meropenem/Vaborbactam, or both? Clinical and formulary considerations. Clin Infect Dis 68 (2018), 519–524.
    • (2018) Clin Infect Dis , vol.68 , pp. 519-524
    • Pogue, J.M.1    Bonomo, R.A.2    Kaye, K.S.3
  • 57
    • 84891340003 scopus 로고    scopus 로고
    • Why bortezomib cannot go with ‘green’?
    • Jia, L., Liu, F.T., Why bortezomib cannot go with ‘green’?. Cancer Biol Med 10 (2013), 206–213.
    • (2013) Cancer Biol Med , vol.10 , pp. 206-213
    • Jia, L.1    Liu, F.T.2
  • 58
    • 4444332516 scopus 로고    scopus 로고
    • Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum-sensing signal AI-2
    • Miller, S.T., Xavier, K.B., Campagna, S.R., Taga, M.E., Semmelhack, M.F., Bassler, B.L., Hughson, F.M., Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum-sensing signal AI-2. Mol Cell 15 (2004), 677–687.
    • (2004) Mol Cell , vol.15 , pp. 677-687
    • Miller, S.T.1    Xavier, K.B.2    Campagna, S.R.3    Taga, M.E.4    Semmelhack, M.F.5    Bassler, B.L.6    Hughson, F.M.7
  • 60
    • 0036007875 scopus 로고    scopus 로고
    • Biosynthesis and attachment of novel bacterial polyketide synthase starter units
    • Moore, B.S., Hertweck, C., Biosynthesis and attachment of novel bacterial polyketide synthase starter units. Nat Prod Rep 19 (2002), 70–99.
    • (2002) Nat Prod Rep , vol.19 , pp. 70-99
    • Moore, B.S.1    Hertweck, C.2
  • 61
    • 85034105163 scopus 로고    scopus 로고
    • The importance of boron in biological systems
    • Uluisik, I., Karakaya, H.C., Koc, A., The importance of boron in biological systems. J Trace Elem Med Biol 45 (2018), 156–162.
    • (2018) J Trace Elem Med Biol , vol.45 , pp. 156-162
    • Uluisik, I.1    Karakaya, H.C.2    Koc, A.3
  • 62
    • 84883481349 scopus 로고    scopus 로고
    • Small molecule inhibitors of AI-2 signalling in bacteria: state-of-the-art and future perspectives for anti-quorum sensing agents
    • Guo, M., Gamby, S., Zheng, Y., Sintim, H.O., Small molecule inhibitors of AI-2 signalling in bacteria: state-of-the-art and future perspectives for anti-quorum sensing agents. Int J Mol Sci 14 (2013), 17694–17728.
    • (2013) Int J Mol Sci , vol.14 , pp. 17694-17728
    • Guo, M.1    Gamby, S.2    Zheng, Y.3    Sintim, H.O.4
  • 66
    • 85042369576 scopus 로고    scopus 로고
    • The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis
    • Feng, H., Liu, X., Wang, S., Fleming, J., Wang, D.C., Liu, W., The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis. Nat Commun, 8, 2017, 2242.
    • (2017) Nat Commun , vol.8
    • Feng, H.1    Liu, X.2    Wang, S.3    Fleming, J.4    Wang, D.C.5    Liu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.