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“Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death”. Diabetes55 (8): 2192–201. (August 2006). doi:10.2337/db05-1566. PMID16873681.
“Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets”. Diabetologia49 (6): 1237–46. (June 2006). doi:10.1007/s00125-006-0206-7. PMID16570161.
“Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction”. Proteomics10 (8): 1621–33. (April 2010). doi:10.1002/pmic.200900651. PMID20186753.
“Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells”. Endocrinology146 (4): 1808–17. (April 2005). doi:10.1210/en.2004-1175. PMID15618358.
“Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial”. Diabetic Medicine21 (11): 1204–12. (2004). doi:10.1111/j.1464-5491.2004.01319.x. PMID15498087.
“Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation”. Diabetes54 (7): 2117–25. (July 2005). doi:10.2337/diabetes.54.7.2117. PMID15983213.
“Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death”. Diabetes55 (8): 2192–201. (August 2006). doi:10.2337/db05-1566. PMID16873681.
“Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets”. Diabetologia49 (6): 1237–46. (June 2006). doi:10.1007/s00125-006-0206-7. PMID16570161.
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“Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction”. Proteomics10 (8): 1621–33. (April 2010). doi:10.1002/pmic.200900651. PMID20186753.