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Volumn 463, Issue , 2014, Pages 70-74

A fluorescent carbapenem for structure function studies of penicillin-binding proteins, β-lactamases, and β-lactam sensors

Author keywords

Carbapenem; Fluorescent modification; Penicillin binding protein; Lactamase

Indexed keywords

ACYLATION; AMIDES; ELECTROPHORESIS; PROBES; PROTEINS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

EID: 84905837157     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2014.07.012     Document Type: Article
Times cited : (18)

References (23)
  • 1
    • 0032908481 scopus 로고    scopus 로고
    • BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • G. Zhao, T.I. Meier, S.D. Kahl, K.R. Gee, and L.C. Blaszczak BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins Antimicrob. Agents Chemother. 43 1999 1124 1128 (Pubitemid 29214735)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.5 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5
  • 2
    • 19944433679 scopus 로고    scopus 로고
    • Structure-activity relationships of different β-lactam antibiotics against a soluble form of Enterococcus faecium PBP5, a type II bacterial transpeptidase
    • DOI 10.1128/AAC.49.2.612-618.2005
    • A.M. Hujer, M. Kania, T. Gerken, V.E. Anderson, J.D. Buynak, X. Ge, P. Caspers, M.G. Page, L.B. Rice, and R.A. Bonomo Structure-activity relationships of different β-lactam antibiotics against a soluble form of Enterococcus faecium PBP5, a type II bacterial transpeptidase Antimicrob. Agents Chemother. 49 2005 612 618 (Pubitemid 40175670)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.2 , pp. 612-618
    • Hujer, A.M.1    Kania, M.2    Gerken, T.3    Anderson, V.E.4    Buynak, J.D.5    Ge, X.6    Caspers, P.7    Page, M.G.P.8    Rice, L.B.9    Bonomo, R.A.10
  • 3
    • 84885116586 scopus 로고    scopus 로고
    • Continuous fluorescence anisotropy-based assay of BOCILLIN FL penicillin reaction with penicillin binding protein 3
    • A.B. Shapiro, R.F. Gu, N. Gao, S. Livchak, and J. Thresher Continuous fluorescence anisotropy-based assay of BOCILLIN FL penicillin reaction with penicillin binding protein 3 Anal. Biochem. 439 2013 37 43
    • (2013) Anal. Biochem. , vol.439 , pp. 37-43
    • Shapiro, A.B.1    Gu, R.F.2    Gao, N.3    Livchak, S.4    Thresher, J.5
  • 5
    • 84859588905 scopus 로고    scopus 로고
    • Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: Effect of side chain polarity on enzyme carboxylation and substrate turnover
    • J.S. Buchman, K.D. Schneider, A.R. Lloyd, S.L. Pavlish, and D.A. Leonard Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover Biochemistry 51 2012 3143 3150
    • (2012) Biochemistry , vol.51 , pp. 3143-3150
    • Buchman, J.S.1    Schneider, K.D.2    Lloyd, A.R.3    Pavlish, S.L.4    Leonard, D.A.5
  • 8
    • 0030594997 scopus 로고    scopus 로고
    • Conformational analysis of meropenem and desmethyl meropenem: The effect of 1β-methyl group on carbapenem antibiotics
    • DOI 10.1016/0960-894X(96)00341-1
    • J.-E. Igarashi, T. Nishimura, A. Sasaki, and M. Sunagawa Conformational analysis of meropenem and desmethyl meropenem: the effect of 1β-methyl group on carbapenem antibiotics Bioorg. Med. Chem. Lett. 6 1996 1881 1886 (Pubitemid 26270465)
    • (1996) Bioorganic and Medicinal Chemistry Letters , vol.6 , Issue.16 , pp. 1881-1886
    • Igarashi, J.-E.1    Nishimura, T.2    Sasaki, A.3    Sunagawa, M.4
  • 9
    • 0032054929 scopus 로고    scopus 로고
    • Structural comparison of 1β-methylcarbapenem, carbapenem and penem: NMR studies and theoretical calculations
    • DOI 10.1016/S0968-0896(97)10054-2, PII S0968089697100542
    • T. Nishimura, J. Igarashi, A. Sasaki, and M. Sunagawa Structural comparison of 1β-methylcarbapenem, carbapenem, and penem: NMR studies and theoretical calculations Bioorg. Med. Chem. 6 1998 367 375 (Pubitemid 28179578)
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.4 , pp. 367-375
    • Nishimura, T.1    Igarashi, J.-E.2    Sasaki, A.3    Sunagawa, M.4
  • 10
    • 0027195588 scopus 로고
    • Studies on the structures of meropenem(SM-7338) and it's primary metabolite
    • Y. Takeuchi, T. Inoue, and M. Sunagawa Studies on the structures of meropenem(SM-7338) and its primary metabolite J. Antibiot. 46 1993 827 832 (Pubitemid 23199087)
    • (1993) Journal of Antibiotics , vol.46 , Issue.5 , pp. 827-832
    • Takeuchi, Y.1    Inoue, T.2    Sunagawa, M.3
  • 12
    • 79951679429 scopus 로고    scopus 로고
    • Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem
    • K.D. Schneider, C.J. Ortega, N.A. Renck, R.A. Bonomo, R.A. Powers, and D.A. Leonard Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem J. Mol. Biol. 406 2011 583 594
    • (2011) J. Mol. Biol. , vol.406 , pp. 583-594
    • Schneider, K.D.1    Ortega, C.J.2    Renck, N.A.3    Bonomo, R.A.4    Powers, R.A.5    Leonard, D.A.6
  • 13
    • 0032542009 scopus 로고    scopus 로고
    • Three-dimensional structure of AmpC β-lactamase from Escherichia coli bound to a transition-state analogue: Possible implications for the oxyanion hypothesis and for inhibitor design
    • DOI 10.1021/bi981210f
    • K.C. Usher, L.C. Blaszczak, G.S. Weston, B.K. Shoichet, and S.J. Remington Three-dimensional structure of AmpC β-lactamase from Escherichia coli bound to a transition-state analogue: Possible implications for the oxyanion hypothesis and for inhibitor design Biochemistry 37 1998 16082 16092 (Pubitemid 28536245)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16082-16092
    • Usher, K.C.1    Blaszczak, L.C.2    Weston, G.S.3    Shoichet, B.K.4    Remington, S.J.5
  • 14
    • 0038381513 scopus 로고    scopus 로고
    • Resistance to β-lactam antibiotics and its mediation by the sensor domain of the transmembrane BlaR signaling pathway in Staphylococcus aureus
    • DOI 10.1074/jbc.M300611200
    • D. Golemi-Kotra, J.Y. Cha, S.O. Meroueh, S.B. Vakulenko, and S. Mobashery Resistance to β-lactam antibiotics and its mediation by the sensor domain of the transmembrane BlaR signaling pathway in Staphylococcus aureus J. Biol. Chem. 278 2003 18419 18425 (Pubitemid 36799464)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 18419-18425
    • Golemi-Kotra, D.1    Cha, J.Y.2    Meroueh, S.O.3    Vakulenko, S.B.4    Mobashery, S.5
  • 16
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 17
    • 84884254903 scopus 로고    scopus 로고
    • Structures of the class D carbapenemases OXA-23 and OXA-146: Mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam
    • K.C. Kaitany, N.V. Klinger, C.M. June, M.E. Ramey, R.A. Bonomo, R.A. Powers, and D.A. Leonard Structures of the class D carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam Antimicrob. Agents Chemother. 57 2013 4848 4855
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 4848-4855
    • Kaitany, K.C.1    Klinger, N.V.2    June, C.M.3    Ramey, M.E.4    Bonomo, R.A.5    Powers, R.A.6    Leonard, D.A.7
  • 19
    • 0036894235 scopus 로고    scopus 로고
    • Structural basis for imipenem inhibition of class C β-lactamases
    • DOI 10.1128/AAC.46.12.3978-3980.2002
    • B.M. Beadle, and B.K. Shoichet Structural basis for imipenem inhibition of class C β-lactamases Antimicrob. Agents Chemother. 46 2002 3978 3980 (Pubitemid 35403277)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.12 , pp. 3978-3980
    • Beadle, B.M.1    Shoichet, B.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.