ArticleThe Journal of biological chemistry2008
Noninvasive measurement of protein aggregation by mutant huntingtin fragments or alpha-synuclein in the lens.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- The significance of growth shells in development of symmetry, transparency, and refraction of the human lens.Frontiers in ophthalmology · 2024Review
- Small heat shock proteins in neurodegenerative diseases.Cell stress & chaperones · 2020Review
- Mutant Huntingtin Inhibits αB-Crystallin Expression and Impairs Exosome Secretion from Astrocytes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- αB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's disease.Human molecular genetics · 2016Article
- Beta-amyloid, phospho-tau and alpha-synuclein deposits similar to those in the brain are not identified in the eyes of Alzheimer's and Parkinson's disease patients.Brain pathology (Zurich, Switzerland) · 2014Article
- Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Article
- The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy.PloS one · 2010Article
- Absence of SPARC leads to impaired lens circulation.Experimental eye research · 2009Article
- Apoptosis gene profiling reveals spatio-temporal regulated expression of the p53/Mdm2 pathway during lens development.Experimental eye research · 2009Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Many diverse human diseases are associated with protein aggregation in ordered fibrillar structures called amyloid. Amyloid formation may mediate aberrant protein interactions that culminate in neurodegeneration in Alzheimer, Huntington, and Parkinson diseases and in prion encephalopathies. Studies of protein aggregation in the brain are hampered by limitations in imaging techniques and often require invasive methods that can only be performed postmortem. Here we describe transgenic mice in which aggregation-prone proteins that cause Huntington and Parkinson disease are expressed in the ocular lens. Expression of a mutant huntingtin fragment or alpha-synuclein in the lens leads to protein aggregation and cataract formation, which can be monitored in real time by noninvasive, highly sensitive optical techniques. Expression of a mutant huntingtin fragment in mice lacking the major lens chaperone, alphaB-crystallin, markedly accelerated the onset and severity of aggregation, demonstrating that the endogenous chaperone activity of alphaB-crystallin suppresses aggregation in vivo. These novel mouse models will facilitate the characterization of protein aggregation in vivo and are being used in efficient and economical screens for chemical and genetic modifiers of disease-relevant protein aggregation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.