G
Garth J. S. Cooper
Researcher at University of Auckland
Publications - 309
Citations - 17579
Garth J. S. Cooper is an academic researcher from University of Auckland. The author has contributed to research in topics: Amylin & Insulin. The author has an hindex of 63, co-authored 299 publications receiving 16490 citations. Previous affiliations of Garth J. S. Cooper include Manchester Academic Health Science Centre & University of Manchester.
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Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process.
TL;DR: Comparative proteome analysis is a method with the power to develop important new insights into pathogenic mechanisms in the dementias and provide a unique snapshot illustrating the complexity of interrelated disease mechanisms at work in a complex, multifactorial disease.
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Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.
Janelle Green,Laurent Kreplak,Claire Goldsbury,X. Li Blatter,Martin Stolz,Garth J. S. Cooper,Anna Seelig,Joerg Kistler,Ueli Aebi +8 more
TL;DR: The interaction between lipid bilayers and the 37 amino acid residue polypeptide amylin, which is the primary constituent of the pancreatic amyloids associated with type 2 diabetes, is studied to provide an alternative theory to pore formation, and how amyloid peptides may cause membrane disruption and possibly cytotoxicity.
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Effects of calcitonin, amylin, and calcitonin gene-related peptide on osteoclast development.
TL;DR: The present data establish that this family of peptides not only acts on mature osteoclasts but also inhibits their development in bone marrow cultures, and this activity is shared by amylin and CGRP.
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Co-secretion of amylin and insulin from cultured islet beta-cells: modulation by nutrient secretagogues, islet hormones and hypoglycemic agents.
TL;DR: It is concluded that insulin and amylin are co-secreted from islet beta-cells, and HIT cell line is a useful model in which to studyAmylin metabolism.
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Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation.
TL;DR: Observations suggest that mature fibrils are assembled directly via longitudinal growth of full-width oligomers, making assembly by lateral association of protofibrils appear less likely.