Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

MeSH Review:

Protein Modification, Translational

Utsumi, T. et al., Davila, S. et al., Drenth, J.P. et al.

Utsumi, Sato, Nakano, Takemura, Iwata, Ishisaka, Drenth, Martina, van de Kerkhof, Bonifacino, Jansen,

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Protein Modification, Translational

These findings are suggestive of a role for cotranslational protein-processing pathways in maintaining epithelial luminal structure and implicate noncilial ER proteins in human polycystic disease [1].
Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation [2].
Thus, the amino acid residue penultimate to the N-terminal Gly residue strongly affected two cotranslational protein modifications, N-myristoylation and N-acetylation, and the amino acid requirements at this position for these two modifications were significantly affected by downstream residues [2].
Polycystic liver disease is a disorder of cotranslational protein processing [3].

References

Mutations in SEC63 cause autosomal dominant polycystic liver disease. Davila, S., Furu, L., Gharavi, A.G., Tian, X., Onoe, T., Qian, Q., Li, A., Cai, Y., Kamath, P.S., King, B.F., Azurmendi, P.J., Tahvanainen, P., Kääriäinen, H., Höckerstedt, K., Devuyst, O., Pirson, Y., Martin, R.S., Lifton, R.P., Tahvanainen, E., Torres, V.E., Somlo, S. Nat. Genet. (2004) [Pubmed]
Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation. Utsumi, T., Sato, M., Nakano, K., Takemura, D., Iwata, H., Ishisaka, R. J. Biol. Chem. (2001) [Pubmed]
Polycystic liver disease is a disorder of cotranslational protein processing. Drenth, J.P., Martina, J.A., van de Kerkhof, R., Bonifacino, J.S., Jansen, J.B. Trends in molecular medicine. (2005) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

Editor

Share