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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1962 1
1964 1
1965 2
1966 2
1967 13
1968 15
1969 18
1970 22
1971 20
1972 34
1973 18
1974 31
1975 35
1976 37
1977 36
1978 35
1979 43
1980 32
1981 39
1982 77
1983 51
1984 73
1985 89
1986 76
1987 81
1988 132
1989 174
1990 180
1991 229
1992 301
1993 373
1994 432
1995 390
1996 461
1997 493
1998 492
1999 516
2000 659
2001 711
2002 821
2003 892
2004 988
2005 1162
2006 1234
2007 1287
2008 1521
2009 1868
2010 2019
2011 2034
2012 2336
2013 2344
2014 2313
2015 2535
2016 2371
2017 2579
2018 2416
2019 977
2020 13
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34,264 results
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Page 1
Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores.
Arbor SC, et al. Yale J Biol Med 2016 - Review. PMID 27505013 Free PMC article.
Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid precursor protein (APP) processing, and immune system activation continue to be investigated, the recent discovery that amyloid beta aggregates at lipid rafts and likely forms neurotoxic pores has led to a new paradigm regarding why past therapeutics may have failed and how to design the next round of compounds for clinical trials. ...
Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious in its low number aggregate form as oppose
Amyloid precursor protein processing and bioenergetics.
Wilkins HM and Swerdlow RH. Brain Res Bull 2017 - Review. PMID 27545490 Free PMC article.
The processing of amyloid precursor protein (APP) to amyloid beta (Aβ) is of great interest to the Alzheimer's disease (AD) field. ...
The processing of amyloid precursor protein (APP) to amyloid beta (Aβ) is of great interest to the Alzheimer's disease (AD) fi …
Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.
Polanco JC, et al. Nat Rev Neurol 2018 - Review. PMID 29242522
In Alzheimer disease, the peptide amyloid-β (Aβ) and the protein tau aggregate to form plaques and tangles, respectively, which comprise the histopathological hallmarks of this disease. ...
In Alzheimer disease, the peptide amyloid-β (Aβ) and the protein tau aggregate to form plaques and tangles, respectively, which compr …
Molecular mechanisms of amyloidosis
Merlini G and Bellotti V. N Engl J Med 2003 - Review. PMID 12904524
AA amyloidosis: pathogenesis and targeted therapy
Westermark GT, et al. Annu Rev Pathol 2015 - Review. PMID 25387054
The understanding of why and how proteins misfold and aggregate into amyloid fibrils has increased considerably during recent years. ...Generation of amyloid fibrils is nucleation dependent, and once formed, fibrils recruit and catalyze the conversion of native molecules. ...
The understanding of why and how proteins misfold and aggregate into amyloid fibrils has increased considerably during recent years. …
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer's brain tissue.
Kollmer M, et al. Nat Commun 2019. PMID 31664019 Free PMC article.
The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer's disease and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain tissue is poorly understood. ...These data underscore the importance to use patient-derived amyloid fibrils when investigating the structural basis of the disease....
The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer's disease and cerebral amyloid angiopathy. Ho …
Key Peptides and Proteins in Alzheimer's Disease
Penke B, et al. Curr Protein Pept Sci 2019 - Review. PMID 30605056
Different proteins (such as amyloid precursor protein (APP), β- amyloid (Aβ) and tau protein) play a key role in the initiation and progression of AD. ...The details of trafficking and processing of APP to Aβ, the cytosolic intracellular Aβ domain (AICD) and small soluble proteins are shown, together with other amyloid-forming proteins such as tau and α-synuclein (α-syn). ...
Different proteins (such as amyloid precursor protein (APP), β- amyloid (Aβ) and tau protein) play a key role in the initiatio …
Autophagy Modulation as a Treatment of Amyloid Diseases.
Mputhia Z, et al. Molecules 2019 - Review. PMID 31527516 Free PMC article.
Evidence demonstrates that amyloid diseases result from protein aggregation or impaired amyloid clearance, but the connection between amyloid accumulation and tissue degeneration is not clear. ...This review will focus on autophagy, an important clearance pathway of amyloid proteins, and strategies for using it as a potential therapeutic target for amyloid diseases. ...
Evidence demonstrates that amyloid diseases result from protein aggregation or impaired amyloid clearance, but the connection …
Differential effects of diet- and genetically-induced brain insulin resistance on amyloid pathology in a mouse model of Alzheimer's disease.
Wakabayashi T, et al. Mol Neurodegener 2019. PMID 30975165 Free PMC article.
Studies in humans and diabetic AD model mice have indicated a correlation between insulin resistance and increased amyloid deposition in the brain. ...CONCLUSIONS: Our results suggested a causal and reversible association of brain Aβ metabolism and amyloid pathology by diet-dependent, but not genetically-induced, insulin-resistance. ...
Studies in humans and diabetic AD model mice have indicated a correlation between insulin resistance and increased amyloid deposition …
Secondary nucleation in amyloid formation.
Törnquist M, et al. Chem Commun (Camb) 2018 - Review. PMID 29978862
Here, we present a short overview of this background and then review recent results regarding secondary nucleation of amyloid-forming peptides and proteins, focusing in particular on the amyloid β peptide (Aβ) from Alzheimer's disease, with some examples regarding α-synuclein from Parkinson's disease. ...At the end of this feature article we bring forward outstanding questions and testable mechanistic hypotheses regarding monomer-dependent secondary nucleation in amyloid formation....
Here, we present a short overview of this background and then review recent results regarding secondary nucleation of amyloid-forming …
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