+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity



Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity



Biochemistry 43(22): 6959-6967



beta-Amyloid (Abeta) is a major pathological determinant of Alzheimer's disease (AD). Both active and passive immunization studies have shown that antibodies against Abeta are effective in decreasing cerebral Abeta levels, reducing Abeta accumulation, and attenuating cognitive deficits in animal models of AD. However, the therapeutic potential of these antibodies in human AD patients is limited because of adverse inflammatory reactions and cerebral hemorrhaging associated with the treatments.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 012560634

Download citation: RISBibTeXText

PMID: 15170333

DOI: 10.1021/bi049933o


Related references

An alternative approach to amyloid fibrils morphology: CdSe/ZnS quantum dots labelled beta-amyloid peptide fragments Abeta (31-35), Abeta (1-40) and Abeta (1-42). Colloids and Surfaces. B, Biointerfaces 50(2): 104-111, 2006

Human anti-Abeta antibodies block Abeta fibril formation and prevent Abeta-induced neurotoxicity. Neurology 60(5 Supplement 1): A69, March 11, 2003

Central amyloid-beta-specific single chain variable fragment ameliorates Abeta aggregation and neurotoxicity. 2013

Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay. Analytical Biochemistry 266(1): 66-76, 1999

RNA aptamers selected against amyloid beta-peptide (Abeta) inhibit the aggregation of Abeta. Molecular Biosystems 5(9): 986-991, 2009

Autoantibodies to amyloid beta-peptide (Abeta) are increased in Alzheimer's disease patients and Abeta antibodies can enhance Abeta neurotoxicity: implications for disease pathogenesis and vaccine development. Neuromolecular Medicine 3(1): 29-39, 2003

Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity. Journal of Neuroscience 28(46): 11950-8, 2008

Attenuation of amyloid beta (Abeta)-induced inhibition of phosphatidylinositol 4-kinase activity by Abeta fragments, Abeta20-29 and Abeta31-35. Neuroscience Letters 396(2): 148-152, 2005

Protective effects of Abeta-derived tripeptide, Abeta(32-34), on Abeta(1-42)-induced phosphatidylinositol 4-kinase inhibition and neurotoxicity. Neuroscience Letters 419(3): 247-252, 2007

Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects. Proceedings of the National Academy of Sciences of the United States of America 99(22): 14126-14131, 2002

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proceedings of the National Academy of Sciences of the United States of America 100(1): 330-335, 2002

Angiotensin-converting enzyme converts amyloid beta-protein 1-42 (Abeta(1-42)) to Abeta(1-40), and its inhibition enhances brain Abeta deposition. Journal of Neuroscience 27(32): 8628-8635, 2007

Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Molecular and Cellular Neurosciences 15(2): 183-198, 2000

Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells. Journal of Molecular Biology 384(4): 917-928, 2008

Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer's disease. Journal of Neuroscience 31(6): 2313-2320, 2011