Similar articles for PMID: 21739563

Year	Number of Results
1977	1
1985	1
1996	2
1997	1
1998	3
1999	1
2000	1
2002	2
2003	2
2004	2
2005	7
2006	5
2007	4
2008	3
2009	4
2010	4
2011	5
2012	2
2013	1
2014	3
2015	1
2018	1
2024	0

1

A demetallation method for IMP-1 metallo-β-lactamase with restored enzymatic activity upon addition of metal ion(s).

Yamaguchi Y, Ding S, Murakami E, Imamura K, Fuchigami S, Hashiguchi R, Yutani K, Mori H, Suzuki S, Arakawa Y, Kurosaki H. Yamaguchi Y, et al. Chembiochem. 2011 Sep 5;12(13):1979-83. doi: 10.1002/cbic.201100342. Epub 2011 Jul 7. Chembiochem. 2011. PMID: 21739563 No abstract available.

2

Structural and kinetic studies on metallo-β-lactamase IMP-1.

Griffin DH, Richmond TK, Sanchez C, Moller AJ, Breece RM, Tierney DL, Bennett B, Crowder MW. Griffin DH, et al. Biochemistry. 2011 Oct 25;50(42):9125-34. doi: 10.1021/bi200839h. Epub 2011 Sep 28. Biochemistry. 2011. PMID: 21928807

3

68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-beta-lactamase.

Siemann S, Badiei HR, Karanassios V, Viswanatha T, Dmitrienko GI. Siemann S, et al. Chem Commun (Camb). 2006 Feb 7;(5):532-4. doi: 10.1039/b514227j. Epub 2005 Dec 14. Chem Commun (Camb). 2006. PMID: 16432573

4

Metal content and localization during turnover in B. cereus metallo-beta-lactamase.

Llarrull LI, Tioni MF, Vila AJ. Llarrull LI, et al. J Am Chem Soc. 2008 Nov 26;130(47):15842-51. doi: 10.1021/ja801168r. J Am Chem Soc. 2008. PMID: 18980306

5

Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1.

Yang H, Aitha M, Hetrick AM, Richmond TK, Tierney DL, Crowder MW. Yang H, et al. Biochemistry. 2012 May 8;51(18):3839-47. doi: 10.1021/bi300056y. Epub 2012 Apr 25. Biochemistry. 2012. PMID: 22482529

6

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

Thomas PW, Zheng M, Wu S, Guo H, Liu D, Xu D, Fast W. Thomas PW, et al. Biochemistry. 2011 Nov 22;50(46):10102-13. doi: 10.1021/bi201449r. Epub 2011 Nov 1. Biochemistry. 2011. PMID: 22029287

7

Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis.

Crowder MW, Wang Z, Franklin SL, Zovinka EP, Benkovic SJ. Crowder MW, et al. Biochemistry. 1996 Sep 17;35(37):12126-32. doi: 10.1021/bi960976h. Biochemistry. 1996. PMID: 8810919

8

Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily.

Bebrone C. Bebrone C. Biochem Pharmacol. 2007 Dec 15;74(12):1686-701. doi: 10.1016/j.bcp.2007.05.021. Epub 2007 Jun 2. Biochem Pharmacol. 2007. PMID: 17597585 Free article. Review.

9

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.

Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ. Fabiane SM, et al. Biochemistry. 1998 Sep 8;37(36):12404-11. doi: 10.1021/bi980506i. Biochemistry. 1998. PMID: 9730812

10

Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.

Li Z, Rasmussen BA, Herzberg O. Li Z, et al. Protein Sci. 1999 Jan;8(1):249-52. doi: 10.1110/ps.8.1.249. Protein Sci. 1999. PMID: 10210203 Free PMC article.

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