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Lim, Mi Hee
MetalloNeuroChemistry Lab (MNCL)
Research Interests
  • Neurodegenerative disease, small molecule design, network between metal, proteins, and ROS

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Misfolded proteins in Alzheimer's disease and type II diabetes

Cited 87 times inthomson ciCited 73 times inthomson ci
Title
Misfolded proteins in Alzheimer's disease and type II diabetes
Author
DeToma, Alaina S.Salamekh, SamerRamamoorthy, AyyalusamyLim, Mi Hee
Keywords
ISLET AMYLOID POLYPEPTIDE; BETA-PEPTIDE; FIBRIL FORMATION; IN-VITRO; NEURODEGENERATIVE DISEASES; PRECURSOR PROTEIN; FIBER FORMATION; METAL-BINDING; HUMAN AMYLIN; INSULIN
Issue Date
2012-01
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL SOCIETY REVIEWS, v.41, no.2, pp.608 - 621
Abstract
This tutorial review presents descriptions of two amyloidogenic proteins, amyloid-β (Aβ) peptides and islet amyloid polypeptide (IAPP), whose misfolding propensities are implicated in Alzheimer's disease (AD) and type II diabetes, respectively. Protein misfolding diseases share similarities, as well as some unique protein-specific traits, that could contribute to the initiation and/or development of their associated conditions. Aβ and IAPP are representative amyloidoses and are used to highlight some of the primary considerations for studying misfolded proteins associated with human diseases in this review. Among these factors, their physiological formation, aggregation, interactions with metal ions and other protein partners, and toxicity are presented. Small molecules that target and modulate the metal-Aβ interaction and neurotoxicity are included to illustrate one of the current approaches for uncovering the complexities of protein misfolding at the molecular level.
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DOI
10.1039/c1cs15112f
ISSN
0306-0012
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PHY_Journal Papers
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