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Träfflista för sökning "WFRF:(Schmidt Maria) srt2:(2000-2004)"

Sökning: WFRF:(Schmidt Maria) > (2000-2004)

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1.
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2.
  • Lerm, Maria, et al. (författare)
  • Bacterial protein toxins targeting rho GTPases
  • 2000
  • Ingår i: FEMS Microbiology Letters. - : Wiley-Blackwell. - 0378-1097 .- 1574-6968. ; 188:1, s. 1-6
  • Tidskriftsartikel (refereegranskat)abstract
    • Several bacterial protein toxins target eukaryotic cells by modulating the functions of Rho GTPases that are involved in various signal processes and in the regulation of the actin cytoskeleton. The toxins inhibit Rho functions by ADP-ribosylation or glucosylation and activate them by deamidation and transglutamination. New findings indicate that the GTPases are also targeted by various 'injected' toxins which are introduced into the eukaryotic cells by the type-III secretion system. The injected toxins do not covalently modify Rho GTPases, but manipulate their regulatory GTPase cycle by acting as GTPase-activating proteins or guanine nucleotide exchange factors.
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3.
  • Lerm, Maria, et al. (författare)
  • Proteasomal degradation of cytotoxic necrotizing factor 1-activated rac
  • 2002
  • Ingår i: Infection and Immunity. - : American Society for Microbiology. - 0019-9567 .- 1098-5522. ; 70:8, s. 4053-4058
  • Tidskriftsartikel (refereegranskat)abstract
    • The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli has been shown to activate members of the Rho family by deamidation of glutamine 63. This amino acid is essential for hydrolysis of GTP, and any substitution results in a constitutively active Rho. Activation of Rho induces the formation of stress fibers, filopodia, and membrane ruffles due to activation of RhoA, Cdc42, and Rac, respectively. Here we show that the level of endogenous Rac decreased in CNF1-treated HEK293 and HeLa cells. The amount of mRNA remained unaffected, leaving the possibility that Rac is subject to proteolytic degradation. Treatment of cells with lactacystin, an inhibitor of the 26S proteasome, protected Rac from degradation. We have previously shown that CNF1 activates the c-Jun N-terminal kinase (JNK) only transiently in HeLa cells (M. Lerm, J. Selzer, A. Hoffmeyer, U. R. Rapp, K. Aktories, and G. Schmidt, Infect. Immun. 67:496-503, 1998). Here we show that CNF1-induced JNK activation is stabilized in the presence of lactacystin. The data indicate that Rac is degraded by a proteasome-dependent pathway in CNF1-treated cells.
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4.
  • Schmidt de Graaf, Pia, 1957, et al. (författare)
  • Två Taubearkiv
  • 2002
  • Ingår i: Årsskrift / Evert Taube-sällskapet. - 0349-1005. ; 2002, s. 115-119
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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  • Resultat 1-4 av 4

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