SNCB Antibody

1. Cells that overexpress alpha-syn showed increased susceptibility to the toxicity of the oligomers, while those that overexpressed beta-syn showed increased resistance to the toxic oligomers. PMID: 29054856
2. alterations in the plasma alpha-synuclein and beta-synuclein levels might be implicated in the association between synaptic abnormalities and autism spectrum disorder pathogenesis. PMID: 29850516
3. Study suggests that beta-synuclein changes in Dementia with Lewy bodies may exacerbate neuronal dysfunction caused by accumulation of alpha-synuclein by influencing protein degradation. PMID: 29278715
4. Data suggest that pH serves as an on/off switch for beta- synuclein to form aggregates/fibrils (as seem in Parkinson disease); hydrogen bonding between glutamate residues appears to be involved in fibril formation. PMID: 28710275
5. Cellular pathways affected by bSyn are similar to those affected by aSyn, including impairment of vesicular trafficking and induction of oxidative stress. PMID: 26586132
6. loss of inhibitory C-terminal conformations in disease associated P123H beta-synuclein PMID: 26332674
7. beta-Synuclein expression was locally concentrated and rather modest, but nevertheless changed its effect on amyloid precursor protein expression and plaque load in a time- and concentration-dependent manner. PMID: 26111745
8. The differing aggregation propensities of alpha-synuclein and beta-synuclein are associated with differences in the degree of residual structure in the C-terminus coupled to the shorter separation between the N- and C-termini in beta-synuclein. PMID: 25389903
9. Beta-synuclein protects against isoaspartate accumulation in alpha-synuclein. PMID: 23630590
10. both alphaS- and P123H betaS-globules were formed through similar but distinct pathogenic mechanisms. PMID: 23013868
11. In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells PMID: 23319586
12. Thermodynamic studies in conjunction with EPR confirm that alpha-synuclein, beta-synuclein, and gamma-synuclein bind copper(II) in a high affinity 1:1 stoichiometry. PMID: 21117662
13. Data provide evidence for the role of beta-synuclein minor transcript variants in the development of complex diseases and provide new insights into the pathogenesis of Lewy body diseases. PMID: 22205345
14. This study suggested that the pathogenesis of dementia in Parkinson disease, indicating that differential sncb expression in the caudate nucleus may represent one of the molecular mechanisms involved in these complex diseases. PMID: 21683963
15. Despite both synucleins sharing considerable sequence homology, the level of carboxy-terminal Src kinase-homologous kinase (CHK) phosphorylation of beta-synuclein is significantly higher than that of alpha-synuclein. PMID: 21699177
16. Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1. PMID: 21386983
17. Synuclein-alpha, -beta, and -gamma are important in regulating neurotransmitter release from specific populations of midbrain dopamine neurons through mechanisms that differ from those reported in other neurons. PMID: 21593311
18. Studies identified molecular interaction domains within the beta-synuclein polypeptide that specifically binds alpha-synuclein. PMID: 21085664
19. beta-Synuclein mRNA expression in the control group was significantly higher than that in the schizophrenic group. PMID: 20854101
20. A drastic diminution of beta-synuclein expression was observed in cortical areas of all samples that presented neuropathological features corresponding to pure diffuse Lewy body pathology PMID: 20959308
21. Human beta-synuclein rendered fibrillogenic by designed mutations. PMID: 20833719
22. Data show that alpha-synuclein, beta-synuclein, and apolipoprotein A-1 have the conserved functional ability to induce membrane curvature and to convert large vesicles into highly curved membrane tubules and vesicles. PMID: 20693280
23. members of the synuclein gene family, particularly SNCA and SNCG, affect the risk of developing diffuse lewy body disease. PMID: 20697047
24. Gamma-synuclein protein is valuable for evaluation of progression of colorectal carcinoma; it is more sensitive to predict advanced stage and lymph node invasion when combined with either alpha- or beta-synuclein protein. PMID: 20043104
25. Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins PMID: 11812782
26. Of medulloblastomas, 76% have immunoreactivity for either alpha- or beta-synuclein or both; no immunoreactivity for gamma-synuclein is seen in medulloblastomas. PMID: 12783249
27. Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease. PMID: 12867415
28. 2 new AA changes were found in unrelated Lewy body dementia index cases: V70M & P123H, at conserved residues in highly conserved regions of the beta-synuclein protein. Mutations in the beta-synuclein gene may predispose to DLB. PMID: 15365127
29. the alpha- and gamma-synucleins regulate proteasomal function and beta-synuclein acts as a negative regulator of alpha-synuclein PMID: 15591046
30. An 11-residue deletion in the lipid-binding domain of beta-synuclein leads to the destabilization of an entire segment of the micelle-bound helical structure containing the deletion site. PMID: 16597821
31. findings indicate that increased expression of beta-synuclein protein results in a reduction of alpha-synuclein protein expression PMID: 16959793
32. The accumulation of beta-synuclein was detectable only in the pons of Sandhoff disease cases. This differential accumulation of alpha- and beta-synucleins in human lipidoses may be related to functional differences between these two proteins. PMID: 17653558
33. A comparison of the structural and dynamic properties of the free states of all three synucleins, is reported in order to shed light on differences that may help to explain their different propensities to aggregate. PMID: 17681534
34. Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic. PMID: 17692832
35. structural and functional properties of beta-synuclein were characterized using biochemical and bio-physical methods including: a functional assay, mass spectrometry, size exclusion chromatography, circular dichroism (CD), and fluorescence spectroscopy PMID: 18221001
36. The aggregation behavior of alpha- and beta-synuclein as well as a series of chimeric variants were compared by exploring the structural transitions that occur in the presence of a widely used lipid mimetic, sodium dodecyl sulfate (SDS). PMID: 18436957

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HGNC: 11140

OMIM: 602569

KEGG: hsa:6620

STRING: 9606.ENSP00000308057

UniGene: Hs.90297