Casaasgard p235

Comparison of AaL active site with AiiA, AiiB, and AidC. (A)

Por um escritor misterioso
Last updated 15 abril 2025
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity. - Abstract - Europe PMC
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
WO2020185861A1 - Proteins and methods for disrupting bacterial communication - Google Patents
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618T and its application in quorum quenching on Pseudomonas aeruginosa PAO1
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
SsoPox W263 saturation site screening and characterization. A. Relative
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Cloning and characterization of Aiia, an acylhomoserine lactonase from Bacillus cereus RC1 to control soft rot causing pathogen Lelliottia amnigena RCE
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Marine Drugs, Free Full-Text
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Aii20J, a wide-spectrum thermostable N-acylhomoserine lactonase from the marine bacterium Tenacibaculum sp. 20J, can quench AHL-mediated acid resistance in Escherichia coli
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control. - Abstract - Europe PMC
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Frontiers The exceptionally efficient quorum quenching enzyme LrsL suppresses Pseudomonas aeruginosa biofilm production
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks - ScienceDirect
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Lactonase - an overview
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Frontiers Effects of Signal Disruption Depends on the Substrate Preference of the Lactonase
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Visualizing the superfamily of metallo-β-lactamases through sequence similarity network neighborhood connectivity analysis - ScienceDirect
Recomendado para você
você pode gostar

© 2014-2025 atsrb.gos.pk. All rights reserved.