Chaperone and anti‐chaperone: Two‐faced synuclein as stimulator of synaptic evolution
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Summary
The intriguing possibility that the dual syn proteins might have acquired a driving force for synaptic evolution is referred to, whereby the anti‐chaperone syn may provoke stress‐induced diverse responses, whereas, the chaperones may provide buffering for them, allowing accumulation of nonlethal phenotypic variations in synapses.
- Type
- review
- Published
- 2006-10-01
- Cited by
- 16
- References
- 72
- OpenAlex
- https://openalex.org/W1995299174
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:35598844
Keywords
Chaperone (clinical), Neurodegeneration, Biology, Cell biology, Protein aggregation
References
- β-Synuclein Inhibits α-Synuclein Aggregation: A Possible Role as an Anti-Parkinsonian Factor
- DJ-1, a novel regulator of the tumor suppressor PTEN.
- Neurodegenerative tauopathies: human disease and transgenic mouse models.
- Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons.
- A yeast prion provides a mechanism for genetic variation and phenotypic diversity
- Climate change (Communication arising): Recent temperature trends in the Antarctic
- Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing.
- Biophysical Properties of the Synucleins and Their Propensities to Fibrillate
- Doppel: the prion's double.
- α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins
- MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes.
- Hsp90 as a capacitor for morphological evolution
- A new brain-specific 14-kDa protein is a phosphoprotein. Its complete amino acid sequence and evidence for phosphorylation.
- Forcing nonamyloidogenic beta-synuclein to fibrillate.
- Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein.
- Trans-Suppression of Misfolding in an Amyloid Disease
- Long-term culture of mouse cortical neurons as a model for neuronal development, aging, and death.
- Absence of the prion protein homologue Doppel causes male sterility
- Distribution of PNP 14 (β‐synuclein) in neuroendocrine tissues: Localization in Sertoli cells
- The Copper Chaperone CCS Is Abundant in Neurons and Astrocytes in Human and Rodent Brain
Cited by
- Susceptibility of parkinson's disease following mild blast traumatic brain injury
- Molecular and cellular biology of synucleins.
- Neurotoxic conversion of β-synuclein: a novel approach to generate a transgenic mouse model of synucleinopathies?
- P2X7 Receptor Signaling Pathway as a Therapeutic Target for Neurodegenerative Diseases
- Transcriptional profiling of striatal neurons in response to single or concurrent activation of dopamine D2, adenosine A(2A) and metabotropic glutamate type 5 receptors: focus on beta-synuclein expression.
- Expression of alpha-synuclein, a presynaptic protein implicated in Parkinson's disease, in erythropoietic lineage.
- α-Synuclein and β-synuclein enhance secretion protein production in baculovirus expression vector system
- Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo
- Combined immunotherapy with “anti-insulin resistance” therapy as a novel therapeutic strategy against neurodegenerative diseases
- Evolvability of Amyloidogenic Proteins in Human Brain
- Possible Role of the Polyglutamine Elongation in Evolution of Amyloid-Related Evolvability
- Target Proteins in the Dorsal Hippocampal Formation Sustain the Memory-Enhancing and Neuroprotective Effects of Ginkgo biloba
- Acrolein-mediated alpha-synuclein pathology involvement in the early post-injury pathogenesis of mild blast-induced Parkinsonian neurodegeneration
- Molecular Chaperones in the Mammalian Brain: Regional Distribution, Cellular Compartmentalization and Synaptic Interactions
- Chaperone and Anti‐Chaperone Properties of Synuclein: Implications for Development, Aging, and Neurodegenerative Disease
- Alpha-synuclein and cortico-striatal plasticity in animal models of Parkinson disease.
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