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pro vyhledávání: '"Kayo N Suzuki"'
Autor:
Mitsuhide Hamaguchi, Hironari Kamikubo, Kayo N Suzuki, Yoshihisa Hagihara, Itaru Yanagihara, Ikuhiro Sakata, Mikio Kataoka, Daizo Hamada
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e71618 (2013)
Enterohaemorrhagic E. coli (EHEC) induces actin reorganization of host cells by injecting various effectors into host cytosol through type III secretion systems. EspB is the natively partially folded EHEC effector which binds to host α-catenin to pr
Externí odkaz:
https://doaj.org/article/4ce0a43ad1574e63841d00d6eeba227c
Publikováno v:
FEBS Journal. 277:2409-2415
Enterohemorrhagic and enteropathogenic Escherichia coli produce various effector proteins that are directly injected into the host-cell cytosol through the type III secretion system. E. coli secreted protein (Esp)B is one such effector protein, and a
Autor:
Takahisa Ikegami, Makoto Hayashi, Takeshi Honda, Itaru Yanagihara, Tomoaki Kato, Daizo Hamada, Yoshikatsu Murooka, Kayo N. Suzuki
Publikováno v:
FEBS Journal. 272:756-768
The structural properties of EspB, a virulence factor of the Escherichia coli O157 type III secretion system, were characterized. Far-UV and near-UV CD spectra, recorded between pH 1.0 and pH 7.0, show that the protein assumes alpha-helical structure
Publikováno v:
The FEBS journal. 277(11)
Enterohemorrhagic and enteropathogenic Escherichia coli produce various effector proteins that are directly injected into the host-cell cytosol through the type III secretion system. E. coli secreted protein (Esp)B is one such effector protein, and a
Publikováno v:
The FEBS journal. 275(24)
EspB is a multifunctional protein associated with the type III secretion system of enterohaemorrhagic Escherichia coli, and interacts with various biomolecules including alpha-catenin in the host cell. The binding of EspB to alpha-catenin is thought
Autor:
Daizo, Hamada, Tomoaki, Kato, Takahisa, Ikegami, Kayo N, Suzuki, Makoto, Hayashi, Yoshikatsu, Murooka, Takeshi, Honda, Itaru, Yanagihara
Publikováno v:
The FEBS journal. 272(3)
The structural properties of EspB, a virulence factor of the Escherichia coli O157 type III secretion system, were characterized. Far-UV and near-UV CD spectra, recorded between pH 1.0 and pH 7.0, show that the protein assumes alpha-helical structure