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348 related items for PubMed ID: 15779910
21. Hybrid QM/MM and DFT investigations of the catalytic mechanism and inhibition of the dinuclear zinc metallo-beta-lactamase CcrA from Bacteroides fragilis. Park H, Brothers EN, Merz KM. J Am Chem Soc; 2005 Mar 30; 127(12):4232-41. PubMed ID: 15783205 [Abstract] [Full Text] [Related]
22. Structure of metallo-beta-lactamase IND-7 from a Chryseobacterium indologenes clinical isolate at 1.65-A resolution. Yamaguchi Y, Takashio N, Wachino J, Yamagata Y, Arakawa Y, Matsuda K, Kurosaki H. J Biochem; 2010 Jun 30; 147(6):905-15. PubMed ID: 20305272 [Abstract] [Full Text] [Related]
24. Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases. Siemann S, Clarke AJ, Viswanatha T, Dmitrienko GI. Biochemistry; 2003 Feb 18; 42(6):1673-83. PubMed ID: 12578382 [Abstract] [Full Text] [Related]
25. Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in mono-zinc metallo-β-lactamases. Fonseca F, Bromley EH, Saavedra MJ, Correia A, Spencer J. J Mol Biol; 2011 Sep 02; 411(5):951-9. PubMed ID: 21762699 [Abstract] [Full Text] [Related]
26. Evidence for a dinuclear active site in the metallo-beta-lactamase BcII with substoichiometric Co(II). A new model for metal uptake. Llarrull LI, Tioni MF, Kowalski J, Bennett B, Vila AJ. J Biol Chem; 2007 Oct 19; 282(42):30586-95. PubMed ID: 17715135 [Abstract] [Full Text] [Related]
33. The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams. Badarau A, Damblon C, Page MI. Biochem J; 2007 Jan 01; 401(1):197-203. PubMed ID: 16961465 [Abstract] [Full Text] [Related]
35. X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria. Costello AL, Sharma NP, Yang KW, Crowder MW, Tierney DL. Biochemistry; 2006 Nov 14; 45(45):13650-8. PubMed ID: 17087519 [Abstract] [Full Text] [Related]
36. Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity. Rasia RM, Ceolín M, Vila AJ. Protein Sci; 2003 Jul 14; 12(7):1538-46. PubMed ID: 12824499 [Abstract] [Full Text] [Related]
38. Hydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lid. Oelschlaeger P, Pleiss J. J Mol Biol; 2007 Feb 09; 366(1):316-29. PubMed ID: 17157873 [Abstract] [Full Text] [Related]
39. An evolutionary classification of the metallo-beta-lactamase fold proteins. Aravind L. In Silico Biol; 1999 Feb 09; 1(2):69-91. PubMed ID: 11471246 [Abstract] [Full Text] [Related]