Edward Parkin

Summary

Affiliation: Lancaster University
Country: UK

Publications

  1. pmc Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease
    Mallory Gough
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    Biochem Res Int 2011:721463. 2011
  2. doi request reprint Copper modulates zinc metalloproteinase-dependent ectodomain shedding of key signaling and adhesion proteins and promotes the invasion of prostate cancer epithelial cells
    Catherine A Parr-Sturgess
    Division of Biomedical and Life Sciences, Lancaster University, Lancaster, UK
    Mol Cancer Res 10:1282-93. 2012
  3. doi request reprint A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10
    Edward Parkin
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    J Neurochem 108:1464-79. 2009
  4. doi request reprint Development of a proteolytically stable retro-inverso peptide inhibitor of beta-amyloid oligomerization as a potential novel treatment for Alzheimer's disease
    Mark Taylor
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    Biochemistry 49:3261-72. 2010
  5. doi request reprint Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
    Benjamin Harris
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster, LA1 4YQ, UK
    Brain Res 1296:203-15. 2009

Collaborators

  • David M A Mann
  • Michael D Brown
  • Marten Beeg
  • Catherine A Parr-Sturgess
  • Mallory Gough
  • Mark Taylor
  • Benjamin Harris
  • Noel W Clarke
  • Claire A Hart
  • Claire L Tinker
  • Catherine Parr-Sturgess
  • Marco Gobbi
  • David Allsop
  • Mara Canovi
  • Jennifer Mayes
  • Susan Moore
  • Isabel Pereira

Detail Information

Publications5

  1. pmc Zinc metalloproteinases and amyloid Beta-Peptide metabolism: the positive side of proteolysis in Alzheimer's disease
    Mallory Gough
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    Biochem Res Int 2011:721463. 2011
    ..It is the role of zinc metalloproteinases in this "positive side of proteolysis in Alzheimer's disease" that is discussed in the current paper...
  2. doi request reprint Copper modulates zinc metalloproteinase-dependent ectodomain shedding of key signaling and adhesion proteins and promotes the invasion of prostate cancer epithelial cells
    Catherine A Parr-Sturgess
    Division of Biomedical and Life Sciences, Lancaster University, Lancaster, UK
    Mol Cancer Res 10:1282-93. 2012
    ..Collectively, these data implicate copper as an important factor in promoting prostate cancer cell invasion and indicate that the selective posttranslational activation of ZMP-mediated protein shedding might play a role in this process...
  3. doi request reprint A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10
    Edward Parkin
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    J Neurochem 108:1464-79. 2009
    ..In conclusion, this is a new mechanism by which levels of ADAM10 are regulated and may have implications in a range of human diseases including Alzheimer's disease...
  4. doi request reprint Development of a proteolytically stable retro-inverso peptide inhibitor of beta-amyloid oligomerization as a potential novel treatment for Alzheimer's disease
    Mark Taylor
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK
    Biochemistry 49:3261-72. 2010
    ..Thus, RI-OR2 represents a strong candidate for further development as a novel treatment for Alzheimer's disease...
  5. doi request reprint Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
    Benjamin Harris
    Division of Biomedical and Life Sciences, School of Health and Medicine, Lancaster University, Lancaster, LA1 4YQ, UK
    Brain Res 1296:203-15. 2009
    ..These results indicate that it is the exclusion of ADAM10 from rafts rather than simply the raft localization of beta- and gamma-secretases that underlies A beta-peptide generation within these cellular structures...