These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Journal Abstract Search


79 related items for PubMed ID: 7873581

  • 1. beta-Lactamase mutations far from the active site influence inhibitor binding.
    Bonomo RA, Dawes CG, Knox JR, Shlaes DM.
    Biochim Biophys Acta; 1995 Feb 22; 1247(1):121-5. PubMed ID: 7873581
    [Abstract] [Full Text] [Related]

  • 2. OHIO-1 beta-lactamase mutants: the Arg244Ser mutant and resistance to beta-lactams and beta-lactamase inhibitors.
    Lin S, Thomas M, Mark S, Anderson V, Bonomo RA.
    Biochim Biophys Acta; 1999 Jun 15; 1432(1):125-36. PubMed ID: 10366735
    [Abstract] [Full Text] [Related]

  • 3. Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase.
    Bonomo RA, Dawes CG, Knox JR, Shlaes DM.
    Biochim Biophys Acta; 1995 Feb 22; 1247(1):113-20. PubMed ID: 7873579
    [Abstract] [Full Text] [Related]

  • 4. Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 beta-lactamases.
    Giakkoupi P, Tzelepi E, Legakis NJ, Tzouvelekis LS.
    J Antimicrob Chemother; 1999 Jan 22; 43(1):23-9. PubMed ID: 10381097
    [Abstract] [Full Text] [Related]

  • 5. Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme.
    Lin S, Thomas M, Shlaes DM, Rudin SD, Knox JR, Anderson V, Bonomo RA.
    Biochem J; 1998 Jul 15; 333 ( Pt 2)(Pt 2):395-400. PubMed ID: 9735103
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 9. Tazobactam is a potent inactivator of selected inhibitor-resistant class A beta-lactamases.
    Bonomo RA, Rudin SA, Shlaes DM.
    FEMS Microbiol Lett; 1997 Mar 01; 148(1):59-62. PubMed ID: 9066111
    [Abstract] [Full Text] [Related]

  • 10. Substitutions at position 105 in SHV family β-lactamases decrease catalytic efficiency and cause inhibitor resistance.
    Li M, Conklin BC, Taracila MA, Hutton RA, Skalweit MJ.
    Antimicrob Agents Chemother; 2012 Nov 01; 56(11):5678-86. PubMed ID: 22908166
    [Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 16.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 17. Overcoming resistance to beta-lactamase inhibitors: comparing sulbactam to novel inhibitors against clavulanate resistant SHV enzymes with substitutions at Ambler position 244.
    Thomson JM, Distler AM, Bonomo RA.
    Biochemistry; 2007 Oct 09; 46(40):11361-8. PubMed ID: 17848099
    [Abstract] [Full Text] [Related]

  • 18. Substitution of Met-69 by Ala or Gly in TEM-1 beta-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors.
    Madec S, Blin C, Krishnamoorthy R, Picard B, Chaibi el B, Fouchereau-Péron M, Labia R.
    FEMS Microbiol Lett; 2002 May 21; 211(1):13-6. PubMed ID: 12052544
    [Abstract] [Full Text] [Related]

  • 19. 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; 2016 Jan 21; 60(1):356-60. PubMed ID: 26525789
    [Abstract] [Full Text] [Related]

  • 20. Structure-function studies of arginine at position 276 in CTX-M beta-lactamases.
    Pérez-Llarena FJ, Cartelle M, Mallo S, Beceiro A, Pérez A, Villanueva R, Romero A, Bonnet R, Bou G.
    J Antimicrob Chemother; 2008 Apr 21; 61(4):792-7. PubMed ID: 18281307
    [Abstract] [Full Text] [Related]


    Page: [Next] [New Search]
    of 4.