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.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

PPIL1  -  peptidylprolyl isomerase (cyclophilin)-like 1

Homo sapiens

Synonyms: CGI-124, CYPL1, PPIase, Peptidyl-prolyl cis-trans isomerase-like 1, Rotamase PPIL1, ...
 
 
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.
 

Disease relevance of PPIL1

  • Consistently, transfection of short-interfering RNA specific to PPIL1 into SNUC4 and SNUC5 cells effectively reduced expression of the gene and retarded growth of the colon cancer cells [1].
 

High impact information on PPIL1

  • To understand the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a proline-containing PPIase peptide substrate [2].
  • The human PPIL1 (peptidyl prolyl isomerase-like protein 1) is a specific component of human 35 S U5 small nuclear ribonucleoprotein particle and 45 S activated spliceosome [3].
  • Therefore, elevated expression of PPIL1 may play an important role in proliferation of cancer cells through the control of SNW1/SKIP and/or stathmin [1].
  • Among the genes that were up-regulated in the tumors, we selected for this study peptidyl-prolyl isomerase-like 1 (PPIL1) encoding PPIL1, a cyclophilin-related protein [1].
  • We further identified two PPIL1-interacting proteins, SNW1/SKIP (SKI-binding protein) and stathmin [1].
 

Biological context of PPIL1

 

Anatomical context of PPIL1

 

Other interactions of PPIL1

References

  1. Overexpression of peptidyl-prolyl isomerase-like 1 is associated with the growth of colon cancer cells. Obama, K., Kato, T., Hasegawa, S., Satoh, S., Nakamura, Y., Furukawa, Y. Clin. Cancer Res. (2006) [Pubmed]
  2. Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. Leulliot, N., Vicentini, G., Jordens, J., Quevillon-Cheruel, S., Schiltz, M., Barford, D., van Tilbeurgh, H., Goris, J. Mol. Cell (2006) [Pubmed]
  3. Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP. Xu, C., Zhang, J., Huang, X., Sun, J., Xu, Y., Tang, Y., Wu, J., Shi, Y., Huang, Q., Zhang, Q. J. Biol. Chem. (2006) [Pubmed]
  4. Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human chromosome region 6p21.1 by radiation hybrid mapping and fluorescence in situ hybridization. Mann, S.S., Pettenati, M.J., von Kap-herr, C., Hart, T.C. Cytogenet. Cell Genet. (1998) [Pubmed]
  5. Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain. Ozaki, K., Fujiwara, T., Kawai, A., Shimizu, F., Takami, S., Okuno, S., Takeda, S., Shimada, Y., Nagata, M., Watanabe, T., Takaichi, A., Takahashi, E., Nakamura, Y., Shin, S. Cytogenet. Cell Genet. (1996) [Pubmed]
  6. Transcriptional coregulator SNW/SKIP: the concealed tie of dissimilar pathways. Folk, P., Půta, F., Skruzný, M. Cell. Mol. Life Sci. (2004) [Pubmed]
  7. Pin1 in Alzheimer's disease. Butterfield, D.A., Abdul, H.M., Opii, W., Newman, S.F., Joshi, G., Ansari, M.A., Sultana, R. J. Neurochem. (2006) [Pubmed]
 
WikiGenes - Universities