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Items: 1 to 20 of 152


Biochemical characteristics of New Delhi metallo-β-lactamase-1 show unexpected difference to other MBLs.

Li T, Wang Q, Chen F, Li X, Luo S, Fang H, Wang D, Li Z, Hou X, Wang H.

PLoS One. 2013 Apr 12;8(4):e61914. doi: 10.1371/journal.pone.0061914.


Characterization of purified New Delhi metallo-β-lactamase-1.

Thomas PW, Zheng M, Wu S, Guo H, Liu D, Xu D, Fast W.

Biochemistry. 2011 Nov 22;50(46):10102-13. doi: 10.1021/bi201449r.


Purification and biochemical characterization of the VIM-1 metallo-beta-lactamase.

Franceschini N, Caravelli B, Docquier JD, Galleni M, Frère JM, Amicosante G, Rossolini GM.

Antimicrob Agents Chemother. 2000 Nov;44(11):3003-7.


Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.

Makena A, Brem J, Pfeffer I, Geffen RE, Wilkins SE, Tarhonskaya H, Flashman E, Phee LM, Wareham DW, Schofield CJ.

J Antimicrob Chemother. 2015 Feb;70(2):463-9. doi: 10.1093/jac/dku403.


NDM-12, a novel New Delhi metallo-β-lactamase variant from a carbapenem-resistant Escherichia coli clinical isolate in Nepal.

Tada T, Shrestha B, Miyoshi-Akiyama T, Shimada K, Ohara H, Kirikae T, Pokhrel BM.

Antimicrob Agents Chemother. 2014 Oct;58(10):6302-5. doi: 10.1128/AAC.03355-14.


Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism.

Zhang H, Hao Q.

FASEB J. 2011 Aug;25(8):2574-82. doi: 10.1096/fj.11-184036.


New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition.

King DT, Worrall LJ, Gruninger R, Strynadka NC.

J Am Chem Soc. 2012 Jul 18;134(28):11362-5. doi: 10.1021/ja303579d.


Effective antimicrobial activity of Cbf-K16 and Cbf-A7 A13 against NDM-1-carrying Escherichia coli by DNA binding after penetrating the cytoplasmic membrane in vitro.

Hao Q, Wang H, Wang J, Dou J, Zhang M, Zhou W, Zhou C.

J Pept Sci. 2013 Mar;19(3):173-80. doi: 10.1002/psc.2488.


Molecular basis of NDM-1, a new antibiotic resistance determinant.

Liang Z, Li L, Wang Y, Chen L, Kong X, Hong Y, Lan L, Zheng M, Guang-Yang C, Liu H, Shen X, Luo C, Li KK, Chen K, Jiang H.

PLoS One. 2011;6(8):e23606. doi: 10.1371/journal.pone.0023606.


Identification of New Delhi metallo-β-lactamase gene (NDM-1) from a clinical isolate of Acinetobacter junii in China.

Zhou Z, Guan R, Yang Y, Chen L, Fu J, Deng Q, Xie Y, Huang Y, Wang J, Wang D, Liao C, Gong S, Xia H.

Can J Microbiol. 2012 Jan;58(1):112-5. doi: 10.1139/W11-112.


Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme.

Horsfall LE, Izougarhane Y, Lassaux P, Selevsek N, Liénard BM, Poirel L, Kupper MB, Hoffmann KM, Frère JM, Galleni M, Bebrone C.

FEBS J. 2011 Apr;278(8):1252-63. doi: 10.1111/j.1742-4658.2011.08046.x.


Purification development and characterization of the zinc-dependent metallo-β-lactamase from Bacillus anthracis.

Schlesinger SR, Kim SG, Lee JS, Kim SK.

Biotechnol Lett. 2011 Jul;33(7):1417-22. doi: 10.1007/s10529-011-0569-9.


Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India.

Yong D, Toleman MA, Giske CG, Cho HS, Sundman K, Lee K, Walsh TR.

Antimicrob Agents Chemother. 2009 Dec;53(12):5046-54. doi: 10.1128/AAC.00774-09.


Inhibitor discovery of full-length New Delhi metallo-β-lactamase-1 (NDM-1).

Shen B, Yu Y, Chen H, Cao X, Lao X, Fang Y, Shi Y, Chen J, Zheng H.

PLoS One. 2013 May 13;8(5):e62955. doi: 10.1371/journal.pone.0062955.


Emergence of metallo-β-lactamase NDM-1-producing multidrug-resistant Escherichia coli in Australia.

Poirel L, Lagrutta E, Taylor P, Pham J, Nordmann P.

Antimicrob Agents Chemother. 2010 Nov;54(11):4914-6. doi: 10.1128/AAC.00878-10.


Role of Non-Active-Site Residue Trp-93 in the Function and Stability of New Delhi Metallo-β-Lactamase 1.

Khan AU, Rehman MT.

Antimicrob Agents Chemother. 2015 Nov 2;60(1):356-60. doi: 10.1128/AAC.01194-15.


High specificity of cphA-encoded metallo-beta-lactamase from Aeromonas hydrophila AE036 for carbapenems and its contribution to beta-lactam resistance.

Segatore B, Massidda O, Satta G, Setacci D, Amicosante G.

Antimicrob Agents Chemother. 1993 Jun;37(6):1324-8.


Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance.

Osano E, Arakawa Y, Wacharotayankun R, Ohta M, Horii T, Ito H, Yoshimura F, Kato N.

Antimicrob Agents Chemother. 1994 Jan;38(1):71-8.


Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase.

Chiou J, Leung TY, Chen S.

Antimicrob Agents Chemother. 2014 Sep;58(9):5372-8. doi: 10.1128/AAC.01977-13.

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