• Nenhum resultado encontrado

The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation.

N/A
N/A
Protected

Academic year: 2017

Share "The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation."

Copied!
9
0
0

Texto

Loading

Imagem

Figure 3. E3 ligase activity of NleL is involved in modulating EHEC pedestal formation
Figure 4. The E3 ligase activity of EHEC NleL down modulates EPEC pedestal formation. HeLa cells were infected at a multiplicity of infection of 100 with wild type EPEC, or EPEC harboring plasmid expressing wild-type EHEC NleL or NleL C753A
Figure 5. Contribution of nleL to C. rodentium virulence. (A) C. rodentium NleL is an E3 ubiquitin ligase

Referências

Documentos relacionados

Cullin serves as a scaffold protein for the assembly of the multisubunit ubiquitin ligase complex that contains a RING domain protein at its C-terminus and a cullin-specific

Riddley - Notes on the botany of Fernando Noronha.. Desmidiaeeae "in" Symbolae

Human Scribble (Vartul) Is Targeted for Ubiquitin- Mediated Degradation by the High-Risk Papillomavirus E6 Proteins and the E6AP Ubiquitin- Protein Ligase. A strategy for

These genetic and biochemical results suggest that the Rtt101 Mms22 E3 ligase counteracts a function of Mrc1 that is linked to the replicative helicase at stalled replication forks,

When considered together with the failure of ANBR to rescue the Roc1a mutant, these results suggest that, within the context of the male germ line- specific Cul3 E3 ligase complex,

To determine whether the intracellular tail of ICAM-1 is required for the shift of clustered ICAM-1 to the immobile fraction, we used an ICAM-1-GFP mutant that lacks the

Recent- ly, GRAIL (the E3-ubiquitin ligase gene related to anergy in lymphocytes) was shown to be responsible for the Th2 hypore- sponsiveness in a mouse model of

In the susceptibility test (where the diameter of the growth inhibition disc produced by an antibiotic is used to assess whether a strain exhibits complete