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PRPF40A  -  PRP40 pre-mRNA processing factor 40...

Homo sapiens

Synonyms: FBP-11, FBP11, FLAF1, FLJ20585, FNBP3, ...
 
 
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Disease relevance of PRPF40A

  • To test this hypothesis, we constructed a recombinant gene in which the full-size FBP11 cDNA was placed under the control of a strong cauliflower mosaic virus 35S promoter [1].
 

Psychiatry related information on PRPF40A

 

High impact information on PRPF40A

  • A maternally determined seed defect has been obtained by downregulation of the petunia MADS box genes Floral Binding Protein 7 (FBP7) and FBP11 [3].
  • Analysis of the expression pattern of FBP7 and FBP11 and genetic analysis confirmed the maternal inheritance of the phenotype [3].
  • RNA gel blot analysis was performed to investigate ectopic FBP11 expression in relation to the expression of the closely related FBP7 gene and the putative petunia class C-type homeotic genes FBP6 and pMADS3 [1].
  • Although HYPB and HYPC are novel, HYPA is human FBP-11, a protein implicated in spliceosome function [4].
  • Structure of FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group II/III WW domains [5].
 

Biological context of PRPF40A

 

Anatomical context of PRPF40A

  • Implanting hypa beads soaked with purified insulin antibody into regenerating adult newt forelimbs results in abnormal growth and differentiation of the regenerates, confirming that insulin plays an essential role in adult newt forelimb regeneration [7].
 

Associations of PRPF40A with chemical compounds

  • Hypa A, a novel macrocyclic polypeptide containing 30 amino acid residues, has been isolated from the n-butanol extract of the Argentine plant Hybanthus parviflorus [8].
 

Other interactions of PRPF40A

  • Secondly, 8-mm stents were coated with (1) HI, (2) HIP-10 microg/20 microg/40 microg (HIP5%/10%/20%), (3) P-40 microg (P), (4) IP-40 microg (IP), and (5) HP-40 microg (HP) [9].
 

Analytical, diagnostic and therapeutic context of PRPF40A

  • We have solved the structure of FBP11 WW1 and a Pro-Pro-Leu-Pro ligand complex, and demonstrated the binding mechanism with mutational analysis using surface plasmon resonance [5].
  • Ligand titration by 1H-15N HSQC NMR spectra revealed that the WW domain of FBP11/HYPA binds all the peptides with the PL, PP, and PR motifs [10].

References

  1. The petunia MADS box gene FBP11 determines ovule identity. Colombo, L., Franken, J., Koetje, E., van Went, J., Dons, H.J., Angenent, G.C., van Tunen, A.J. Plant Cell (1995) [Pubmed]
  2. Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain. Pires, J.R., Parthier, C., Aido-Machado, R., Wiedemann, U., Otte, L., Böhm, G., Rudolph, R., Oschkinat, H. J. Mol. Biol. (2005) [Pubmed]
  3. Downregulation of ovule-specific MADS box genes from petunia results in maternally controlled defects in seed development. Colombo, L., Franken, J., Van der Krol, A.R., Wittich, P.E., Dons, H.J., Angenent, G.C. Plant Cell (1997) [Pubmed]
  4. Huntingtin interacts with a family of WW domain proteins. Faber, P.W., Barnes, G.T., Srinidhi, J., Chen, J., Gusella, J.F., MacDonald, M.E. Hum. Mol. Genet. (1998) [Pubmed]
  5. Structure of FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group II/III WW domains. Kato, Y., Miyakawa, T., Kurita, J., Tanokura, M. J. Biol. Chem. (2006) [Pubmed]
  6. Identification and characterization of human FNBP3 gene in silico. Katoh, M., Katoh, M. Int. J. Mol. Med. (2003) [Pubmed]
  7. Detection of insulin receptors in newt liver and forelimb regenerates and the effects of local insulin deprivation on epimorphic regeneration. Foty, R.A., Liversage, R.A. J. Exp. Zool. (1993) [Pubmed]
  8. First cyclotide from Hybanthus (Violaceae). Broussalis, A.M., Göransson, U., Coussio, J.D., Ferraro, G., Martino, V., Claeson, P. Phytochemistry (2001) [Pubmed]
  9. Triple-coated stents (Hirudin/Iloprost/Paclitaxel): an in vitro approach for characterizing the antiproliferative potential of each individual compound. Voisard, R., Stemberger, A., Baur, R., Herter, T., Hähnel, I., Resch, A., Seliger, C., Hemmer, W., Hannekum, A., Hombach, V., Alt, E. International journal of cardiology. (2005) [Pubmed]
  10. Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III. Kato, Y., Hino, Y., Nagata, K., Tanokura, M. Proteins (2006) [Pubmed]
 
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