outer membrane lipoprotein Blc ; Escherichia coli






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1 9659382 E. coli HPII catalase interaction with high spin ligands: formate and fluoride as active site probes. Biochim Biophys Acta 1998 May 19 3
2 15044022 The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding. FEBS Lett 2004 Mar 26 2
3 16920109 The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids. FEBS Lett 2006 Sep 4 8
4 21123871 Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc. Acta Crystallogr D Biol Crystallogr 2010 Dec 1
5 22561882 Direct isopropanol production from cellobiose by engineered Escherichia coli using a synthetic pathway and a cell surface display system. J Biosci Bioeng 2012 Jul 2
6 24156762 Creation of cellobiose and xylooligosaccharides-coutilizing Escherichia coli displaying both β-glucosidase and β-xylosidase on its cell surface. ACS Synth Biol 2014 Jul 18 1
7 32169530 Genetic analysis and plasmid-mediated bla<sub>CMY-2</sub> in Salmonella and Shigella and the Ceftriaxone Susceptibility regulated by the ISEcp-1 tnpA-bla<sub>CMY-2</sub>-blc-sugE. J Microbiol Immunol Infect 2021 Aug 1
8 33210733 Lipocalin Blc is a potential heme-binding protein. FEBS Lett 2021 Jan 4