Peptidoglycan-associated outer membrane protein Mep45 of rumen anaerobeSelenomonas ruminantiumforms a non-specific diffusion pore via its C-terminal transmembrane domain

High Salt Concentrations Increase Permeability through OmpC Channels ofEscherichia coli

(2014) Seiji Kojima et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channels

(2013) S. Kojima et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Molecular Basis for the Maintenance of Envelope Integrity in Selenomonas ruminantium: Cadaverine Biosynthesis and Covalent Modification into the Peptidoglycan Play a Major Role

(2012) Seiji KOJIMA et al.   JOURNAL OF NUTRITIONAL SCIENCE AND VITAMINOLOGY

Cadaverine Covalently Linked to the Peptidoglycan Serves as the Correct Constituent for the Anchoring Mechanism between the Outer Membrane and Peptidoglycan in Selenomonas ruminantium

(2011) S. Kojima et al.   JOURNAL OF BACTERIOLOGY

Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium

(2010) S. Kojima et al.   JOURNAL OF BACTERIOLOGY

Physical and genetic characterization of an outer-membrane protein (OmpM1) containing an N-terminal S-layer-like homology domain from the phylogenetically Gram-positive gut anaerobe Mitsuokella multacida

(2009) M.L. Kalmokoff et al.   ANAEROBE