Literature DB >> 12121917

N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-beta-lactamase.

Stefan Siemann1, Darryl P Evanoff, Laura Marrone, Anthony J Clarke, Thammaiah Viswanatha, Gary I Dmitrienko.   

Abstract

Members of a family of N-arylsulfonyl hydrazones have been identified as novel inhibitors of IMP-1, a metallo-beta-lactamase of increasing prevalence. Structure-activity relationship studies have indicated a requirement for bulky aromatic substituents on each side of the sulfonyl hydrazone backbone for these compounds to serve as efficient inhibitors of IMP-1. Molecular modeling has provided insight into the structural basis for the anti-metallo-beta-lactamase activity exhibited by this class of compounds.

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Year:  2002        PMID： 12121917      PMCID： PMC127367          DOI： 10.1128/AAC.46.8.2450-2457.2002

Source DB:  PubMed          Journal:  Antimicrob Agents Chemother        ISSN： 0066-4804            Impact factor:   5.191


  40 in total

1.  Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-beta-lactamase.

Authors:  M L Greenlee; J B Laub; J M Balkovec; M L Hammond; G G Hammond; D L Pompliano; J H Epstein-Toney
Journal:  Bioorg Med Chem Lett       Date:  1999-09-06       Impact factor: 2.823

Review 2.  Metallo-beta-lactamase: structure and mechanism.

Authors:  Z Wang; W Fast; A M Valentine; S J Benkovic
Journal:  Curr Opin Chem Biol       Date:  1999-10       Impact factor: 8.822

Review 3.  Class B beta-lactamases: the importance of being metallic.

Authors:  J A Cricco; A J Vila
Journal:  Curr Pharm Des       Date:  1999-11       Impact factor: 3.116

4.  Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism.

Authors:  R Paul-Soto; R Bauer; J M Frère; M Galleni; W Meyer-Klaucke; H Nolting; G M Rossolini; D de Seny; M Hernandez-Valladares; M Zeppezauer; H W Adolph
Journal:  J Biol Chem       Date:  1999-05-07       Impact factor: 5.157

5.  Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.

Authors:  C Prosperi-Meys; G Llabres; D de Seny; R P Soto; M H Valladares; N Laraki; J M Frere; M Galleni
Journal:  FEBS Lett       Date:  1999-01-25       Impact factor: 4.124

6.  The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase.

Authors:  S Bounaga; A P Laws; M Galleni; M I Page
Journal:  Biochem J       Date:  1998-05-01       Impact factor: 3.857

7.  Structure-activity relationships of biphenyl tetrazoles as metallo-beta-lactamase inhibitors.

Authors:  J H Toney; K A Cleary; G G Hammond; X Yuan; W J May; S M Hutchins; W T Ashton; D E Vanderwall
Journal:  Bioorg Med Chem Lett       Date:  1999-09-20       Impact factor: 2.823

8.  Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases.

Authors:  R Nagano; Y Adachi; H Imamura; K Yamada; T Hashizume; H Morishima
Journal:  Antimicrob Agents Chemother       Date:  1999-10       Impact factor: 5.191

9.  Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli.

Authors:  N Laraki; N Franceschini; G M Rossolini; P Santucci; C Meunier; E de Pauw; G Amicosante; J M Frère; M Galleni
Journal:  Antimicrob Agents Chemother       Date:  1999-04       Impact factor: 5.191

10.  Structure of In31, a blaIMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes.

Authors:  N Laraki; M Galleni; I Thamm; M L Riccio; G Amicosante; J M Frère; G M Rossolini
Journal:  Antimicrob Agents Chemother       Date:  1999-04       Impact factor: 5.191
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  21 in total

1.  Docking and scoring of metallo-beta-lactamases inhibitors.

Authors:  Lars Olsen; Ingrid Pettersson; Lars Hemmingsen; Hans-Werner Adolph; Flemming Steen Jørgensen
Journal:  J Comput Aided Mol Des       Date:  2004-04       Impact factor: 3.686

2.  Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance.

Authors:  Peter Oelschlaeger; Stephen L Mayo; Juergen Pleiss
Journal:  Protein Sci       Date:  2005-03       Impact factor: 6.725

3.  Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.

Authors:  Shao-Kang Yang; Joon S Kang; Peter Oelschlaeger; Ke-Wu Yang
Journal:  ACS Med Chem Lett       Date:  2015-02-12       Impact factor: 4.345

Review 4.  Metallo-beta-lactamases: the quiet before the storm?

Authors:  Timothy R Walsh; Mark A Toleman; Laurent Poirel; Patrice Nordmann
Journal:  Clin Microbiol Rev       Date:  2005-04       Impact factor: 26.132

5.  Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors.

Authors:  Xiao-Long Liu; Ying Shi; Joon S Kang; Peter Oelschlaeger; Ke-Wu Yang
Journal:  ACS Med Chem Lett       Date:  2015-04-23       Impact factor: 4.345

6.  Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors.

Authors:  Ya-Nan Chang; Yang Xiang; Yue-Juan Zhang; Wen-Ming Wang; Cheng Chen; Peter Oelschlaeger; Ke-Wu Yang
Journal:  ACS Med Chem Lett       Date:  2017-04-24       Impact factor: 4.345

7.  Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.

Authors:  Susann Skagseth; Tony Christopeit; Sundus Akhter; Annette Bayer; Ørjan Samuelsen; Hanna-Kirsti S Leiros
Journal:  Antimicrob Agents Chemother       Date:  2017-07-25       Impact factor: 5.191

8.  New benzenesulphonohydrazide derivatives as potential antitumour agents.

Authors:  Łukasz Popiołek; Monika Gawrońska-Grzywacz; Anna Berecka-Rycerz; Kinga Paruch; Iwona Piątkowska-Chmiel; Dorota Natorska-Chomicka; Mariola Herbet; Anna Gumieniczek; Jarosław Dudka; Monika Wujec
Journal:  Oncol Lett       Date:  2020-09-02       Impact factor: 2.967

Review 9.  Three decades of beta-lactamase inhibitors.

Authors:  Sarah M Drawz; Robert A Bonomo
Journal:  Clin Microbiol Rev       Date:  2010-01       Impact factor: 26.132

10.  Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.

Authors:  Susann Skagseth; Trine Josefine Carlsen; Gro Elin Kjæreng Bjerga; James Spencer; Ørjan Samuelsen; Hanna-Kirsti S Leiros
Journal:  Antimicrob Agents Chemother       Date:  2015-12-07       Impact factor: 5.191
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