Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kenzo Nishiguchi"'
Autor:
Kenzo Nishiguchi, Motoki Azuma, Tasuku Tsukamoto, Ken-ichi Setsukinai, Yoshito Numata, Yousuke Okuno, Masatomo Rokushima, Hiroshi Takemoto, Hideki Maki, Kazuhiko Maekawa
Publikováno v:
Bioorganic & Medicinal Chemistry. 23:7234-7239
Pseudomonas aeruginosa is one of the most common and clinically important pathogens because of its resistance to a wide variety of antibiotics. A number of treatments of P. aeruginosa have been developed, but there is still no definitive one. Antisen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1164ba74f1d0eed5211a5c48261c29d5
https://doi.org/10.1016/j.bmc.2015.10.020
https://doi.org/10.1016/j.bmc.2015.10.020
Autor:
Hiroshi Kamimori, Kenzo Nishiguchi, Masako Oka, Hideki Maki, Hiroki Kinouchi, Hirokazu Arimoto, Hiroshi Kitagawa
Publikováno v:
Analytical Biochemistry. 452:67-75
We developed a surface plasmon resonance (SPR) assay to estimate the interactions of antimicrobial agents with the dipeptide terminal of lipid II ( d -alanyl- d -alanine) and its analogous dipeptides ( l -alanyl- l -alanine and d -alanyl- d -lactate)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddc221a82ec07f9c7a3a720fe6cbeaef
https://doi.org/10.1016/j.ab.2014.02.012
https://doi.org/10.1016/j.ab.2014.02.012
Autor:
Hidenori Yamashiro, Jun Nakamura, Hideki Maki, Kenzo Nishiguchi, Hiroto Miya, Hirokazu Arimoto
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Vancomycin-resistant Staphylococcus aureus (S. aureus) (VRSA) uses depsipeptide-containing modified cell-wall precursors for the biosynthesis of peptidoglycan. Transglycosylase is responsible for the polymerization of the peptidoglycan, and the penic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6dc1d7bf2eee5a435016cb3278acb0
http://europepmc.org/articles/PMC4235313
http://europepmc.org/articles/PMC4235313
Publikováno v:
Journal of Bacteriology. 191:641-650
The expression of pathogenicity-related extracellular proteases, namely, gelatinase and serine protease, in Enterococcus faecalis is positively regulated by a quorum-sensing system mediated by an autoinducing peptide called gelatinase biosynthesis-ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e818b559e86dac6c0e9801450bcc5c34
https://doi.org/10.1128/jb.01029-08
https://doi.org/10.1128/jb.01029-08
Autor:
Pikyee Ma, Hayley M. Yuille, Victor Blessie, Nadine Göhring, Zsófia Iglói, Kenzo Nishiguchi, Jiro Nakayama, Peter J. F. Henderson, Mary K. Phillips-Jones
Publikováno v:
Molecular Membrane Biology. 25:449-473
Two-component signal transduction systems are the main mechanism by which bacteria sense and respond to their environment, and their membrane-located histidine protein kinases generally constitute the sensory components of these systems. Relatively l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76b312d90b3c9903b11e5a4fb43a4b88
https://doi.org/10.1080/09687680802359885
https://doi.org/10.1080/09687680802359885
Autor:
Paul Williams, Takeshi Zendo, Yasuhiro Igarashi, Kenzo Nishiguchi, Kenji Sonomoto, Said E. Desouky, Jiro Nakayama
Publikováno v:
Bioscience, biotechnology, and biochemistry. 77(5)
Staphylococcus aureus and Enterococcus faecalis employ cyclic peptide-mediated quorum sensing (QS) systems, termed agr and fsr respectively, to regulate the expression of a series of virulence genes. To identify quorum sensing inhibitors (QSIs) that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f08cd845cafdde11a3c44ebcfb681285
https://pubmed.ncbi.nlm.nih.gov/23649251
https://pubmed.ncbi.nlm.nih.gov/23649251
Autor:
Kenji Sonomoto, Mami Sato, Takahisa Matsufuji, Takeshi Kawai, Ryoji Yokohata, Yosuke Yamanaka, Jiro Nakayama, Koji Nagata, Masaru Tanokura, Takashi Suzuki, Kenzo Nishiguchi
Publikováno v:
ACS chemical biology. 8(4)
Enterococcus faecalis fsr quorum sensing (QS) involves an 11-residue cyclic peptide named gelatinase biosynthesis-activating pheromone (GBAP) that autoinduces two pathogenicity-related extracellular proteases in a cell density-dependent fashion. To i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::650795dc7fb824b5626e679e84dc5baa
https://pubmed.ncbi.nlm.nih.gov/23362999
https://pubmed.ncbi.nlm.nih.gov/23362999
Autor:
Kenzo Nishiguchi, Hayley M. Yuille, Pikyee Ma, Lianne M. Davis, Jiro Nakayama, Mary K. Phillips-Jones
Publikováno v:
FEBS letters. 585(17)
Siamycin I disrupts growth and quorum sensing in Enterococcus faecalis. Using purified intact protein, we demonstrate here that quorum membrane sensor kinase FsrC is a direct target of siamycin I, reducing pheromone-stimulated autophosphorylation act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34cb28e82ad7d605fab85aa61624dc98
https://pubmed.ncbi.nlm.nih.gov/21803040
https://pubmed.ncbi.nlm.nih.gov/21803040
Autor:
Kenji Sonomoto, Jiro Nakayama, Norito Yoshimura, Yumi Uemura, Kenzo Nishiguchi, Yasuhiro Igarashi
Quorum sensing is a cell-density-dependent regulatory system in gram-positive bacteria and is often regulated by cyclic peptides called “quormones,” which function as extracellular communication signals. With an aim to discover an antipathogenic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::984a0f74c48d79d68bdaa5a1e40f49c2
https://europepmc.org/articles/PMC2630657/
https://europepmc.org/articles/PMC2630657/
Autor:
Yumi Uemura, Ritsuko Mitsuhata, Koji Nagata, Masaru Tanokura, Reiko Kariyama, Hiromi Kumon, Emi Tanaka, Kenji Sonomoto, Jiro Nakayama, Kenzo Nishiguchi
Publikováno v:
Journal of bacteriology. 189(4)
The expression of two Enterococcus faecalis virulence-related proteases, gelatinase (GelE) and serine protease (SprE), is positively regulated by a quorum-sensing system encoded by the fsr gene cluster. In this system, E. faecalis secretes an autoind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cba3c8e9d0b316a510dd1a1a16bcf7f7
https://pubmed.ncbi.nlm.nih.gov/17071762
https://pubmed.ncbi.nlm.nih.gov/17071762