A protein that replaces the entire cellular eIF4F complex.

@article{Mir2008APT,
  title={A protein that replaces the entire cellular eIF4F complex.},
  author={Mohammad Ayoub Mir and Antonito T. Panganiban},
  journal={The EMBO journal},
  year={2008},
  volume={27 23},
  pages={3129-39}
}
The eIF4F cap-binding complex mediates the initiation of cellular mRNA translation. eIF4F is composed of eIF4E, which binds to the mRNA cap, eIF4G, which indirectly links the mRNA cap with the 43S pre-initiation complex, and eIF4A, which is a helicase necessary for initiation. Viral nucleocapsid proteins (N) function in both genome replication and RNA encapsidation. Surprisingly, we find that hantavirus N has multiple intrinsic activities that mimic and substitute for each of the three peptides… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 41 extracted citations

Virus-induced translational arrest through 4EBP1/2-dependent decay of 5'-TOP mRNAs restricts viral infection.

Proceedings of the National Academy of Sciences of the United States of America • 2015
View 1 Excerpt

References

Publications referenced by this paper.
Showing 1-10 of 66 references

Translation initiation: adept at adapting.

Trends in biochemical sciences • 1999
View 4 Excerpts
Highly Influenced

Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.

Proceedings of the National Academy of Sciences of the United States of America • 2008
View 1 Excerpt

Poly(A) leader of eukaryotic mRNA bypasses the dependence of translation on initiation factors.

Proceedings of the National Academy of Sciences of the United States of America • 2008
View 2 Excerpts

Bunyavirus

JN Barr
mRNA • 2007
View 1 Excerpt

Similar Papers

Loading similar papers…