Concepedia

Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways

Francesco Bellia, Valeria Lanza, Sara García‐Viñuales, Ikhlas M. M. Ahmed, Adriana Pietropaolo, Claudio Iacobucci, Gaetano Malgieri, Gianluca D’Abrosca, Roberto Fattorusso, Vincenzo Giuseppe Nicoletti,

Chemical Science · 2019 · 60 citations · 39 references

DOIFull text

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Concepts

Abstract

studies addressing the role played by Aβ peptide in the malfunction of proteome maintenance occurring in AD.

References

39

Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

Maj-Linda B. Selenica, Milene L. Brownlow, Jeffy P. Jimenez et al. · Neurodegenerative Diseases · 2012 · 10.4K citations · Full text

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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Bruce A. Yankner, Lawrence K. Duffy, Daniel A. Kirschner · Science · 1990 · 2K citations

, , +17

Structure of ubiquitin refined at 1.8 Å resolution

Senadhi Vijay‐Kumar, Charles E. Bugg, William J. Cook · Journal of Molecular Biology · 1987 · 1.8K citations

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Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease

James Lowe, Andrew D. Blanchard, Ken Morrell et al. · The Journal of Pathology · 1988 · 542 citations

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The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes

Juri Rappsilber · Journal of Structural Biology · 2010 · 440 citations · Full text

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