α-Synuclein Cooperates with CSPα in Preventing Neurodegeneration

By S. Chandra, Gilbert Gallardo, R. Fernández-Chacón, O. Schlüter, T. Sūdhof. 2005

888 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/fdef7be353330cd5306bc2a5d9f7a1c48368d496

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. H. Ko
2. Valina L. Dawson
3. T. Dawson
4. Christian Haass
5. Leonidas Stefanis
6. T. Sūdhof
7. J. Lipton
8. Mustafa Sahin

In Neurology

1. H. Ko
2. Valina L. Dawson
3. T. Dawson
4. A. Lutz
5. Christian Haass
6. Leonidas Stefanis
7. Edward A. Fon
8. T. Sūdhof

In Physiology

1. Christian Haass
2. Julie D. Forman-Kay
3. A. Lutz
4. Leonidas Stefanis
5. H. Ko
6. Edward A. Fon
7. Ayumu Sugiura
8. Valina L. Dawson

Citations in the corpus

• Neurotransmitter Release: The Last Millisecond in the Life of a Synaptic Vesicle (2013, background): “This neurodegeneration can be fully rescued by modest increases in a-synuclein levels, which indirectly enhance SNARE complex assembly and thereby rescue the CSPa knockout (KO) phenotype (Chandra et al., 2005).”
• Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death (2011, neutral): “…presynaptic terminal and previous reports indicate that it acts as a co-chaperone, in concert with another chaperone, cysteine-string protein α (CSPα), to maintain SNARE complex formation by binding to VAMP2/synaptobrevin 2 (Burre et al., 2010; Chandra et al., 2005; Greten-Harrison et al., 2010).”
• Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation (2006, background): “Recent evidence strongly suggests that the synucleins function as molecular chaperones (Souza et al. 2000; Jiang et al. 2004; Chandra et al. 2005).”
• A new pathway for mitochondrial quality control: mitochondrial‐derived vesicles (2014, background): “While a functional role for a-synuclein has been proposed in the assembly of presynaptic SNARE complexes (Chandra et al, 2005; Burre et al, 2010; Diao et al, 2013), a-synuclein has also been shown to function at mitochondria.”
• Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, positive): “Similarly, virus-mediated expression of a -synuclein in the SN of adult rats causes a reduction in striatal dopamine release (Lundblad et al , 2012). a -Synuclein has been reported to cooperate with presynaptic cysteine-string protein-a (CSP a ) to maintain neuronal integrity (Chandra et al , 2005).”
• Autophagy and apoptosis dysfunction in neurodegenerative disorders. (2014, neutral): “Alpha-syn seems to act as a molecular chaperone for SNARE synaptic proteins (Burre et al., 2010; Chandra et al., 2005).”
• Genetic Animal Models of Parkinson’s Disease (2010, positive): “However, this has not been settled, since a-synuclein may function as a cochaperone as transgenic expression of a-synuclein abolishes the lethality and neurodegeneration caused by deletion of the synaptic vesicle chaperone, cysteine-string protein-a (Chandra et al., 2005).”
• α-Synuclein in Parkinson's disease. (2012, background): “It is believed that a-synuclein, through a chaperone-like function, may act in synergy with CSP-a in the assembly of the SNARE complex (Chandra et al. 2005), and this effect may involve, in particular, binding to synaptotagmin-2 (Burree et al. 2010).”