Alzheimer's disease: genes, proteins, and therapy.

By D. Selkoe. Physiological Reviews, 2001

5,955 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Pharmacology, Physiology

View Paper: https://www.semanticscholar.org/paper/682a975a638bfa37fa4b4ca53222dcee756fe826

How researchers see this paper

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

In Computational Theory and Mathematics

1. P. Reddy
2. D. Selkoe
3. M. Beal
4. M. Mańczak
5. George Bartzokis
6. G. Wenk
7. F. LaFerla
8. M. Calkins

In Pharmacology

1. D. Selkoe
2. P. Reddy
3. M. Beal
4. D. Holtzman
5. George Bartzokis
6. F. LaFerla
7. Kaj Blennow
8. M. Mańczak

In Physiology

1. D. Selkoe
2. D. Holtzman
3. P. Reddy
4. M. Beal
5. K. Del Tredici
6. Kaj Blennow
7. G. Shankar
8. M. Calkins

Citations in the corpus

• Human Monocyte Subsets and Phenotypes in Major Chronic Inflammatory Diseases (2019, background): “Studies have shown that these protein aggregates are strongly associated with neuroinflammation, synaptic loss and impaired neuronal function which ultimately lead to cognitive decline (135, 140, 141).”
• Synaptic activity regulates interstitial fluid amyloid-beta levels in vivo. (2005, background): “In the brain of individuals with Alzheimer’s disease (AD), Ab aggregates and accumulates in toxic forms as fibrils in neuritic plaques and as soluble oligomers (Selkoe, 2001).”
• Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies (2002, neutral): “The “peculiar substance” that Alzheimer observed (Alzheimer, 1907) in the cerebral cortex of this patient, August D., was later found to be composed of fibrils of the amyloid (cid:1) -protein (A (cid:1) ) (Teplow, 1998; Selkoe, 2001).”
• Metals, oxidative stress and neurodegenerative disorders (2010, neutral): “Ab is a peptide of 39–43 amino acids that appear to be the main constituent of amyloid plaques in the brains of Alzheimer’s disease (AD) patients [1–5].”
• Cathepsin D--many functions of one aspartic protease. (2008, background): “CD has een implicated in the processing of amyloid precursor proein (APP) [56], apolipoprotein E (apoE) [61] and the tau rotein [57], which are important factors of AD pathogensis [136,142].”
• S100A8/A9 in Inflammation (2018, background): “org June 2018 | Volume 9 | Article 1298 intraneuronal neurofibrillary tangles (92).”
• Design of therapeutic proteins with enhanced stability (2009, background): “Protein aggregation in vivo is also shown to be directly responsible for many diseases such as type II diabetes and Alzheimer’s (6, 7).”
• The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease (2002, background): “…evidence for this hypothesis comes from molecular genetic studies of amyloid precursor proteins (APPs) and presenilins in early-onset familial AD showing that all genetically linked mutations increase the propensity for A to aggregate in vitro (for review, see Golde et al., 2000; Selkoe, 2001).”
• Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006, background): “The Swedish mutation increases the production of total A , whereas APP Florida and London, and PS1 M146L and L286V, specifically increase the production of A 42 (for review, see Sisodia et al., 1999; Selkoe, 2001).”