Evidence of an Intramolecular Interaction between the Two Domains of the BlaR1 Penicillin Receptor during the Signal Transduction
Open Access
- 1 April 2004
- journal article
- Published by Elsevier
- Vol. 279 (14) , 14264-14272
- https://doi.org/10.1074/jbc.m313488200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Solution Structural Study of BlaI: Implications for the Repression of Genes Involved in β-Lactam Antibiotic ResistanceJournal of Molecular Biology, 2003
- Three-dimensional Structure of MecIPublished by Elsevier ,2003
- The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance 1 1Edited by R. HuberJournal of Molecular Biology, 2000
- Display of active subtilisin 309 on phage: analysis of parameters influencing the selection of subtilisin variants with changed substrate specificity from libraries using phosphonylating inhibitorsJournal of Molecular Biology, 2000
- The penicillin sensory transducer, BlaR, involved in the inducibility of β‐lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four‐α‐helix bundleMolecular Microbiology, 1997
- Selection of β-Lactamase on Filamentous Bacteriophage by Catalytic ActivityJournal of Molecular Biology, 1994
- Making antibody fragments using phage display librariesNature, 1991
- Phage antibodies: filamentous phage displaying antibody variable domainsNature, 1990
- Differential transcription of the bla regulatory region during induction of β‐lactamase in Bacillus licheniformisFEBS Letters, 1988
- Analysis by Transformation of the Penicillinase System in Bacillus licheniformisJournal of General Microbiology, 1973