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Yvonne L. Woods

Department of Surgery and Molecular Oncology

Ninewells Hospital and Medical School

Dundee

Scotland

UK

[email]@dundee.ac.uk

Name/email consistency: high

 
 
 
 
 
 
 

Affiliations

  • Department of Surgery and Molecular Oncology, Ninewells Hospital and Medical School, Dundee, Scotland, UK. 2003 - 2004
  • MRC Protein Phosphorylation Unit, MSI/WTB Complex, University of Dundee, Dow Street, UK. 2001

References

  1. p14 Arf promotes small ubiquitin-like modifier conjugation of Werners helicase. Woods, Y.L., Xirodimas, D.P., Prescott, A.R., Sparks, A., Lane, D.P., Saville, M.K. J. Biol. Chem. (2004) [Pubmed]
  2. Exploiting the p53 pathway for cancer diagnosis and therapy. Woods, Y.L., Lane, D.P. Hematol. J. (2003) [Pubmed]
  3. The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site. Woods, Y.L., Rena, G., Morrice, N., Barthel, A., Becker, W., Guo, S., Unterman, T.G., Cohen, P. Biochem. J. (2001) [Pubmed]
  4. The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Woods, Y.L., Cohen, P., Becker, W., Jakes, R., Goedert, M., Wang, X., Proud, C.G. Biochem. J. (2001) [Pubmed]
 
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