Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Vered Ozeri"'
Autor:
Malcolm J. McConville, Dennis M. Dwyer, Avigail Erlanger, Hanoch Goldshmidt, Vered Ozeri, James E Vince, Shulamit Michaeli, Yaron Vagima, Yaniv Lustig, Scott M. Landfear
Publikováno v:
Eukaryotic Cell. 6:1865-1875
Protein translocation across the endoplasmic reticulum is mediated by the signal recognition particle (SRP). In this study, the SRP pathway in trypanosomatids was down-regulated by two approaches: RNA interference (RNAi) silencing of genes encoding S
Publikováno v:
Molecular Microbiology. 41:561-573
Graduate Institute of Clinical Medicine, College ofMedicine, National Taiwan University, Taipei, 100 Taiwan.SummaryGroup A streptococcus (GAS) induces its own entryinto eukaryotic cells in vitro and in vivo. Fibronectin(Fn) bound to protein F1, a GAS
Autor:
Martin G. Ensenberger, Vered Ozeri, Bianca R. Tomasini-Johansson, Emanuel Hanski, Jane Sottile, Deane F. Mosher
Publikováno v:
Journal of Biological Chemistry. 276:35606-35613
Protein F1 is a surface protein ofStreptococcus pyogenes that mediates high affinity binding to fibronectin (Fn) and facilitates S. pyogenes adherence and penetration into cells. The smallest portion of F1 known to retain the full binding potential o
Publikováno v:
Molecular Microbiology. 30:625-637
Entry of group A streptococcus (GAS) into cells has been suggested as an important trait in GAS pathogenicity. Protein F1, a fibronectin (Fn) binding protein, mediates GAS adherence to cells and the extracellular matrix, and efficient cell internaliz
Publikováno v:
Journal of Infectious Diseases. 178:147-158
It was recently reported that strains of Streptococcus pyogenes are capable of inducing entry of the bacterium into epithelial cells; however, nothing is known regarding the gene(s) and the underlying mechanism(s) involved. Using isogenic mutants of
Autor:
Shira Natanson-Yaron, Kenneth M. Yamada, Vered Ozeri, Emanuel Hanski, Israel Burstein, Aviva Tovi, I Vlodavsky, S K Akiyama, Michael G. Caparon
Publikováno v:
ResearcherID
Streptococcus pyogenes binds to the extracellular matrix (ECM) and a variety of host cells and tissues, causing diverse human diseases. Protein F, a S.pyogenes adhesin that binds fibronectin (Fn), contains two binding domains. A repeated domain (RD2)
Autor:
Deane F. Mosher, Vered Ozeri, Martin G. Ensenberger, Nicole R. Kaufman, Emanuel Hanski, Bianca R. Tomasini-Johansson
Publikováno v:
The Journal of biological chemistry. 276(26)
F1 is an adhesin of Streptococcus pyogenes which binds the N-terminal 70-kDa region of fibronectin with high affinity. The fibronectin binding region of F1 is comprised of a 43-residue upstream domain and a repeat domain comprised of five tandem 37-r
Autor:
Gary M. Bokoch, Goni Ben-Ami, Klaus M. Hahn, Klaus Aktories, Fred Hofmann, Vered Ozeri, Ilan Rosenshine, Emanuel Hanski
Publikováno v:
ResearcherID
Enteropathogenic Escherichia coli (EPEC) induces formation of actin pedestals in infected host cells. Agents that inhibit the activity of Rho, Rac, and Cdc42, including Clostridium difficile toxin B (ToxB), compactin, and dominant negative Rho, Rac,
Publikováno v:
Toward Anti-Adhesion Therapy for Microbial Diseases ISBN: 9781461380429
Microbial adhesion to host tissues is the initial event in the pathogenesis of most infections and, as a such, is an attractive target for the development of new antimicrobial therapeutics. Fibronectin (Fn) is a multifunctional glycoprotein present i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee7585159aa81289ca1517b137ac339c
https://doi.org/10.1007/978-1-4613-0415-9_16
https://doi.org/10.1007/978-1-4613-0415-9_16