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Journal Abstract Search
458 related items for PubMed ID: 16870770
1. Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics. Wang F, Cassidy C, Sacchettini JC. Antimicrob Agents Chemother; 2006 Aug; 50(8):2762-71. PubMed ID: 16870770 [Abstract] [Full Text] [Related]
2. Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis. Egesborg P, Carlettini H, Volpato JP, Doucet N. Protein Sci; 2015 Apr; 24(4):534-44. PubMed ID: 25492589 [Abstract] [Full Text] [Related]
3. Structure of the covalent adduct formed between Mycobacterium tuberculosis beta-lactamase and clavulanate. Tremblay LW, Hugonnet JE, Blanchard JS. Biochemistry; 2008 May 13; 47(19):5312-6. PubMed ID: 18422342 [Abstract] [Full Text] [Related]
10. New Conformations of Acylation Adducts of Inhibitors of β-Lactamase from Mycobacterium tuberculosis. Tassoni R, Blok A, Pannu NS, Ubbink M. Biochemistry; 2019 Feb 19; 58(7):997-1009. PubMed ID: 30632739 [Abstract] [Full Text] [Related]
11. Search for non-lactam inhibitors of mtb β-lactamase led to its open shape in apo state: new concept for antibiotic design. Sagar A, Haleem N, Bashir YM, Ashish. Sci Rep; 2017 Jul 24; 7(1):6204. PubMed ID: 28740144 [Abstract] [Full Text] [Related]
17. A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis. Stojanoski V, Chow DC, Hu L, Sankaran B, Gilbert HF, Prasad BV, Palzkill T. J Biol Chem; 2015 Apr 17; 290(16):10382-94. PubMed ID: 25713062 [Abstract] [Full Text] [Related]
18. Kinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosis. Hazra S, Kurz SG, Wolff K, Nguyen L, Bonomo RA, Blanchard JS. Biochemistry; 2015 Sep 15; 54(36):5657-64. PubMed ID: 26237118 [Abstract] [Full Text] [Related]
20. The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop. Palacios AR, Mojica MF, Giannini E, Taracila MA, Bethel CR, Alzari PM, Otero LH, Klinke S, Llarrull LI, Bonomo RA, Vila AJ. Antimicrob Agents Chemother; 2019 Jan 15; 63(1):. PubMed ID: 30348667 [Abstract] [Full Text] [Related] Page: [Next] [New Search]