David M. Hudson, Ph.D.

Research Associate Professor


Ph.D. - University of British Columbia - Biochemistry (2008)
M.Sc. - Dalhousie University - Biochemistry (2003)
B.Sc. - Memorial University of Newfoundland - Biochemistry (2001)


As an investigator in the Collagen Biology and Genetic Disorders Lab, my research is devoted to understanding underlying mechanisms of collagen-related musculoskeletal disease. My research focuses on collagen post-translational properties in skeletal aging and disease. I have recently become particularly fascinated in the adverse effects of aging on collagen cross-linking. Aging has many adverse effects on connective tissues, including limited joint mobility, increased risk of injury and impaired ability to heal. I am currently investigating the random addition of sugar molecules to collagen, a process called protein glycation, which is thought to contribute to these common musculoskeletal complications associated with aging and diabetes.

Contact Info

Email: dmhudson@u.washington.edu
Phone: (206) 543-4700

Fax: (206) 685-3139


  • Orthopaedic Research Society (Tendon Section Member)
  • Canadian Society for Biochemistry and Molecular & Cellular Biology
  • American Society for Matrix Biology
  • International Society for Matrix Biology
  • International Society for Matrix Biology

Recent Publications

  1. Hudson, D.M., Archer, M., King, K.B., and Eyre, D.R. (2018). Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase-mediated cross-linking. J Biol Chem 293, 15620-15627.
  2. Hudson, D.M., Garibov, M., Weis, M.A., Dixon, D., Popowics T.E., and Eyre, D.R. (2017) Distinct post-translational features of type I collagen are conserved in mouse and human periodontal ligament. J Periodontal Res. 52, 1042-1049.
  3. Hudson, D.M., Weis, M.A., Rai, J., Joeng, K.S., Dimori, M., Lee, B.H., Morello, R., and Eyre, D.R. (2017). P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA. J Biol Chem 292, 3877-3887.
  4. Heard, M.E., Besio, R., Weis, M.A., Rai, J., Hudson D.M., Dimori, M., Zimmerman, S., Kamykowski, J.A., Hogue, W.R., Swain, F.L., Burdine, M.S., Mackintosh, S.G., Tackett, A.J., Suva, L.J., Eyre, D.R. and Morello, R. (2016). Sc65-null mice provide evidence for a novel endoplasmic reticulum complex regulating collagen lysyl hydroxylation. PLOS Genetics. 12(4), e1006002.
  5. Hudson, D.M., Joeng, K.S., Werther, R., Weis, M.A., Lee, B.H., and Eyre, D.R. (2015). Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null mice offer a pathobiological mechanism for the high myopia linked to human LEPREL1 mutations. J Biol Chem 290, 8613-8622.
  6. Hudson, D.M., Werther, R., Weis, M.A., Wu, J.J., and Eyre, D.R. (2014). Evolutionary origins of C-terminal (GPP)n 3-hydroxyproline formation in vertebrate tendon collagen. PLoS ONE. 9(4), e93467.
  7. Hudson, D.M., and Eyre, D.R. (2013). Collagen prolyl 3-hydroxylation: A major role for a minor post-translational modification? Connective Tissue Reseach. 54, 245-251.
  8. Hudson, D.M., Kim, L.S., Weis, M.A., Cohn, D.H., and Eyre, D.R. (2012). Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly. Biochemistry. 51, 2417-2424.
  9. Hudson, D.M., Weis, M.A., and Eyre, D.R. (2011). Insights on the evolution of prolyl 3-hydroxylation sites from comparative analysis of chicken and xenopus fibrillar collagens. PLoS ONE. 6, e19336.
  10. Eyre, D.R., Weis, M.A., Hudson, D.M., Wu, J.J., and Kim, L.S. (2011). A novel 3-hydroxyproline (3HYP)-rich motif marks the triple-helical C-terminus of tendon type I collagen. J Biol Chem. 286, 7732-7736.