The Campylobacter jejuni Porin Trimers Pack into Different Lattice Types when Reconstituted in the Presence of Lipid
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1997.t01-1-00575.x/fullpdf
Reference22 articles.
1. Electron Microscopy of the Major Outer Membrane Protein ofCampylobacter jejuni
2. Serological diversity and chemical structures of Campylobacter jejuni low-molecular-weight lipopolysaccharides
3. Precise localization of an overproduced periplasmic protein in Escherichia coli: use of double immuno-gold labelling
4. Identification and characterization of Campylobacter jejuni outer membrane proteins
5. Conformational analysis of the Campylobacter jejuni porin
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1. Peptide translocation across MOMP, the major outer membrane channel from Campylobacter jejuni;Biochemistry and Biophysics Reports;2017-09
2. MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a Ca 2+ Ion Bound at the Constriction Zone;Journal of Molecular Biology;2016-11
3. The Challenge of Efflux-Mediated Antibiotic Resistance in Gram-Negative Bacteria;Clinical Microbiology Reviews;2015-04
4. A novel O -linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization;Open Biology;2014-01
5. Crystallization and preliminary crystallographic studies of MOMP (major outer membrane protein) fromCampylobacter jejuni;Acta Crystallographica Section D Biological Crystallography;2004-11-26
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