Common mechanisms of amyloid oligomer pathogenesis in degenerative disease.

By C. Glabe. Neurobiology of Aging, 2006

605 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/a006be6039a61076a06866a21e2d8f05a4a6179e

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. John C. Morris
2. A. Goate
3. D. Holtzman
4. Urmi Sengupta
5. Steven O. Smith
6. Takeshi Sato
7. J. Elliott
8. S. Aimoto

In Neurology

1. D. Holtzman
2. John C. Morris
3. A. Goate
4. Urmi Sengupta
5. Steven O. Smith
6. Takeshi Sato
7. J. Elliott
8. S. Aimoto

In Physiology

1. D. Holtzman
2. A. Goate
3. John C. Morris
4. Urmi Sengupta
5. Steven O. Smith
6. Takeshi Sato
7. J. Elliott
8. S. Aimoto

Citations in the corpus

• The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, background): “…recognizes conformational similarities would likely be therapeutically beneficial since many disease including AD are characterized by aggregates of multiple proteins (Guerrero-Munoz et al., 2014a; Rasool et al., 2013; Kayed and Glabe, 2006; Kayed et al., 2003; Kayed and Lasagna-Reeves, 2013).”
• Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (2010, positive): “A growing body of literature has implicated the pre-fibrillar oligomers, and not the fibrillar form, as the primary pathological species of AD 26 , 27 .”
• Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice (2011, background): “The role of soluble oligomeric forms of disease-associated protein has received considerable attention in several neurodegenerative diseases because of their association with toxicity [54-56].”
• Alzheimer’s Disease: The Challenge of the Second Century (2011, background): “In addition to the insoluble Ab and tau fibrils that are in plaques and tangles, oligomeric forms of Ab and tau may play important roles in the toxicity of these molecules [for reviews, see (178, 179)].”
• Oxidative stress and the amyloid beta peptide in Alzheimer’s disease (2017, background): “Oligomers accumulated in AD patient brains [39] are suggested to be the more toxic species for cells [40,41] as they can in particular permeabilize cellular membranes, thus initiating a series of events leading to cell dysfunction and death [42].”
• Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. (2008, background): “A third implication is that the mechanisms subserving formation of these toxic oligomers and their mechanism of action to induce cytotoxicity are likely to be similar in these diseases, now often referred to as unfolded protein diseases (70).”