SNCAIP Antibody

1. Differential expression of synphilin-1 isoforms (and alpha-synuclein and parkin) was found in multiple system atrophy brains compared to control brain. PMID: 26465922
2. Synphilin-1 binds ATP, but not CTP. PMID: 25545246
3. Overexpression of human synphilin-1 in mice resulted in hyperphagia and obesity. PMID: 24829096
4. Overexpression of SP1 in neurons, but not peripheral cells, increased the body weight of flies compared with that of non-transgenic controls. SP1 increased food intake but did not affect locomotor activity PMID: 22828940
5. Although serine-129 phosphorylation of alpha-synuclein facilitates tubulin polymerization promoting protein (TPPP)-mediated alpha-SYN oligomerization, this modification does not seem to play an inevitable role in the early step of alpha-SYN oligomer formation. PMID: 20849899
6. Mutation screening of SNCAIP identifies novel sequence variants using a bioinformatic approach; further studies are necessary to determine their possible functional consequences in South African patients with Parkinson's disease. PMID: 21344240
7. Neuronal survival factor MEF2D is decreased in human and experimental Parkinson's disease, a decrease that is specifically associated with alpha-synuclein accumulation and aggregation. PMID: 20816781
8. Synphilin-1 inhibits alpha-synuclein degradation by the proteasome. PMID: 21103907
9. Knockdown of Herp gene unexpectedly facilitated the degradation of synphilin-1, and improved cell viability during proteasomal inhibition. PMID: 20604806
10. Data show that periphilin displays an overlapping expression pattern with synphilin-1 in cellular and animal models and in Lewy bodies of Parkinson's disease (PD) patients, and support involvement of periphilin in PD. PMID: 19730898
11. expression of synphilin-1 shortens N1E-115 cell division doubling time, promotes neurite outgrowth, and protects against Rotenone-induced toxicity; synphilin-1 displays a neurotrophic effect in vitro, may play a neuroprotective role in Parkinson's disease PMID: 19857556
12. alpha-synuclein-synphilin-1 interaction significantly promotes the formation of cytoplasmic alpha-synuclein inclusions, which may have implications for Lewy body formation in neural cells PMID: 19762560
13. The amino acid sequence of synphilin-1 shows extensive homology with its human counterpart, especially in regions containing ankyrin-like motifs and the coiled-coil domain. Expression of mouse synphilin-1 in tissues is similar to its human counterpart. PMID: 11958831
14. results suggest that synphilin-1 has an important role in the formation of aggregates and cytotoxicity in Parkinson disease and that Dorfin may be involved in the pathogenic process by ubiquitylation of synphilin-1 PMID: 12750386
15. a causative role of the R621C mutation in the synphilin-1 gene in Parkinson's disease PMID: 12761037
16. Changes in synuclein expression presage neurodegeneration in a Drosophila model of Parkinson disease. PMID: 12915459
17. Siah-1 was found to abrogate the inhibitory effects of synphilin-1 on dopamine release PMID: 14506261
18. role of aggresomes in cell viability was addressed in the context of over-expressing alpha-synuclein and its interacting partner synphilin-1 PMID: 14627698
19. Casein kinase II (CKII) phosphorylates synphilin-1; beta subunit of this enzyme complex binds to synphilin-1. CKII-mediated phosphorylation of synphilin-1, rather than alpha-synuclein, modulates the aggregation into inclusion bodies. PMID: 14645218
20. role of synphilin-1 in synaptic function and protein degradation and in the molecular mechanisms leading to neurodegeneration in Parkinson disease PMID: 15322916
21. Parkin is a dual-function ubiquitin ligase. K63-linked ubiquitination of synphilin-1 by parkin may be involved in the formation of Lewy body inclusions associated with Parkinson disease. PMID: 15728840
22. We confirm that synphilin-1 and parkin are components of majority of Lewy Bodies in Parkinson's disease and that both proteins are susceptible to proteasomal degradation. PMID: 15894486
23. GSK3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH PMID: 16174773
24. Synphilin-1A may contribute to neuronal degeneration in alpha-synuclein mutations and provides insights into the role of inclusion bodies in neurodegenerative disorders. PMID: 16595633
25. These results suggest that NUB1 indeed targets synphilin-1 to the proteasome for its efficient degradation, which, because of the resultant reduction in synphilin-1, suppresses the formation of synphilin-1-positive inclusions. PMID: 16877356
26. a novel specific interaction of synphilin-1 with the regulatory proteasomal protein S6 ATPase (tbp7) in aggresome-like intracytoplasmic inclusions PMID: 17327361
27. These findings suggest that parkin and synphilin-1 isoform expression changes play a significant role in the pathogenesis of LB diseases. PMID: 17467279
28. review:Isoform Synphilin-1A inclusions recruit both alpha-synuclein and synphilin-1. Aggregation of synphilin-1 and synphilin-1A seems to be protective to cells PMID: 17982729
29. specific effects of C621 mutant synphilin-1 on gene expression that correlate with its role as a susceptibility factor in Parkinson's disease PMID: 18292964
30. All four alpha-synuclein isoforms were affected in dementia with LB (Lewy bodies), most parkin transcript variants in common LB disease, and all synphilin-1 isoforms in Parkinson disease. PMID: 18335262
31. We found no evidence for association between genetic variability in synphilin-1 and Parkinson's disease PMID: 18366718
32. translocation to aggresomes required a special aggresome-targeting signal within the sequence of synphilin 1, an ankyrin-like repeat domain. PMID: 18635553
33. Synphilin-1 might be involved in motor function, and its accumulation in the central nervous system can cause motor impairments. PMID: 18782602
34. synphilin-1A has a novel role as a regulator of SIAH activity, modulating alpha-synuclein, and formation of Lewy body-like inclusions PMID: 19224863

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HGNC: 11139

OMIM: 168600

KEGG: hsa:9627

STRING: 9606.ENSP00000261368

UniGene: Hs.426463