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Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
TLDR
This study revealed, to the knowledge for the first time, the supermolecular structure of the EPEC type III secreton and its direct association with the EspA-sheath-like structure.
The ClpXP ATP-Dependent Protease Regulates Flagellum Synthesis in Salmonella enterica Serovar Typhimurium
TLDR
A new role is described in Salmonella enterica serovar Typhimurium in which ClpXP is involved in the regulation of flagellum synthesis and the DeltaflhD mutation abolished the enhanced effect by DeltaclpXP mutation on the production of flagingllar proteins.
Assembly of the Type III Secretion Apparatus of Enteropathogenic Escherichia coli
TLDR
Results indicate that EscC, EscD, and EscJ are required for the formation of the TTS apparatus, and thereby the secretion of the Esp proteins and Tir effector was abolished.
The cell envelope structure of the lipopolysaccharide-lacking gram-negative bacterium Sphingomonas paucimobilis
TLDR
From the cell envelope preparation of Sphingomonas paucimobilis two membrane fractions with different densities were separated by sucrose density gradient ultracentrifugation, and the glycosphingolipid was assumed to have a function similar to that of the lipopolysaccharide of other gram-negative bacteria.
Short Fimbriae of Porphyromonas gingivalis and Their Role in Coadhesion with Streptococcus gordonii
TLDR
Electron microscopy showed that isolated short fimbriae have an average length of 103 nm and exhibit a helical structure with a pitch of ca.
A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane
TLDR
On the basis of a model of the structure of SLO, some new details of the mechanisms of hemolysis by SLO toxin are proposed, and it is proposed that these parts are the constituents of a single SLO molecule.
Formation of Ring-Shaped Structures on Erythrocyte Membranes after Treatment with Botulinolysin, a Thiol-Activated Hemolysin from Clostridium botulinum
ABSTRACT Damage to erythrocyte membranes by botulinolysin (BLY) was studied by electron microscopy, which revealed ring-shaped structures with inner diameters and widths of approximately 32 and 6.7
Electron microscopic evaluation of a two-step theory of pore formation by streptolysin O
TLDR
The formation of pores by streptolysin O (SLO) was analyzed in erythrocyte membranes and liposomes by immunoelectron microscopy and electron spectroscopic imaging and suggest that proteins in ERYthrocytes membranes are not involved in the formation of SLO rings.
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