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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Synuclein, beta

beta-Synuclein, SNCB
The protein encoded by this gene is highly homologous to alpha-synuclein. These proteins are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease. This protein has been shown to be highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson disease; however, no direct relation to Parkinson disease has been established. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: alpha-Synuclein, gamma-Synuclein, CAN, AGE, HAD
Papers on beta-Synuclein
Life-time expression of the proteins peroxiredoxin, beta-synuclein, PARK7/DJ-1, and stathmin in the primary visual and primary somatosensory cortices in rats.
Thanos et al., Münster, Germany. In Front Neuroanat, 2014
Four distinct proteins are regulated in the aging neuroretina and may be regulated in the cerebral cortex, too: peroxiredoxin, beta-synuclein, PARK[Parkinson disease(autosomal recessive, early onset)]7/DJ-1, and Stathmin.
New brain-specific beta-synuclein isoforms show expression ratio changes in Lewy body diseases.
Ariza et al., Barcelona, Spain. In Neurogenetics, 2012
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.
Genetic dissection of acute ethanol responsive gene networks in prefrontal cortex: functional and mechanistic implications.
Miles et al., Richmond, United States. In Plos One, 2011
Using a novel combination of genetic, bioinformatic and network-based approaches, we identified high priority cis-regulatory candidate genes, including Scn1b, Gria1, Sncb and Nell2.
Peculiarities of copper binding to alpha-synuclein.
Uversky et al., Santa Cruz, United States. In J Biomol Struct Dyn, 2011
Furthermore, based on the EPR studies of model peptides and Beta-synuclein, we concluded that the suspected His residue did not appear to participate in strong Cu21 binding.
Alpha- and beta-synuclein expression in Parkinson disease with and without dementia.
Ariza et al., Barcelona, Spain. In J Neurol Sci, 2011
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.
[Role of genetics in the etiology of synucleinopathies].
de Pancorbo et al., Vitoria-Gasteiz, Spain. In Rev Esp Geriatr Gerontol, 2011
In general, the β-synuclein protein, codified by the SNCB gene, acts as a regulator of processes triggered by α-synuclein and its function is altered by variations in the gene sequence, while γ-synuclein, codified by the SNCG gene, seems to play a major role in certain tumoral processes.
Defining the substrate specificity determinants recognized by the active site of C-terminal Src kinase-homologous kinase (CHK) and identification of β-synuclein as a potential CHK physiological substrate.
Cheng et al., Melbourne, Australia. In Biochemistry, 2011
beta-synuclein is a potential carboxyl-terminal Src kinase-homologous kinase substrate; tyrosine(127) in beta-synuclein is the preferential phosphorylation site.
Functional alterations to the nigrostriatal system in mice lacking all three members of the synuclein family.
Buchman et al., Oxford, United Kingdom. In J Neurosci, 2011
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.
Profiling of hypothalamic and hippocampal gene expression in chronically stressed rats treated with St. John's wort extract (STW 3-VI) and fluoxetine.
Butterweck et al., Gainesville, United States. In Psychopharmacology (berl), 2011
Genes involved in the pathways of inflammatory processes (Mapk8), oxidative stress (Gpx3, Gstm3, Sod3) or Alzheimer's disease (Sncb, Apbb1ip) were altered by both fluoxetine and SJW extract.
Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1.
Brown et al., Bath, United Kingdom. In Plos One, 2010
Transcriptional regulation of the beta-synuclein 5'-promoter metal response element by metal transcription factor-1.
Alpha- and beta-synucleins mRNA expression in lymphocytes of schizophrenia patients.
Mohammadi et al., Tehrān, Iran. In Genet Test Mol Biomarkers, 2010
beta-Synuclein mRNA expression in the control group was significantly higher than that in the schizophrenic group.
Association of alpha-, beta-, and gamma-Synuclein with diffuse lewy body disease.
Farrer et al., Jacksonville, United States. In Arch Neurol, 2010
members of the synuclein gene family, particularly SNCA and SNCG, affect the risk of developing diffuse lewy body disease.
Molecular cloning, characterization and developmental expression of porcine beta-synuclein.
Bendixen et al., Århus, Denmark. In Mol Biol Rep, 2010
The synuclein family includes three known proteins: alpha-synuclein, beta-synuclein and gamma-synuclein.
Effect of N-methyl-D-aspartate (NMDA) receptor antagonists on alpha-synuclein-evoked neuronal nitric oxide synthase activation in the rat brain.
Strosznajder et al., Warsaw, Poland. In Pharmacol Rep, 2009
beta-Synuclein, a homologous protein of ASN that lacks the NAC domain, had no effect on NOS activity.
Autoimmune spread to myelin is associated with experimental autoimmune encephalomyelitis induced by a neuronal protein, beta-synuclein.
Ben-Nun et al., Israel. In J Neuroimmunol, 2009
We have characterized T- and B-cell responses associated with experimental autoimmune encephalomyelitis (EAE) induced in Lewis rats with recombinant beta-Synuclein (betaSync), a neuronal component.
Beta-synuclein occurs in vivo in lipid-associated oligomers and forms hetero-oligomers with alpha-synuclein.
Sharon et al., Jerusalem, Israel. In J Neurochem, 2009
Alpha-synuclein (alphaS) and beta-synuclein (betaS) are homologous proteins implicated in Parkinson's disease and related synucleinopathies.
Early-onset familial lewy body dementia with extensive tauopathy: a clinical, genetic, and neuropathological study.
Lleó et al., Spain. In J Neuropathol Exp Neurol, 2009
Mutation screening that included all coding exons of presenilin 1 (PSEN1), presenilin 2 (PSEN2), alpha-synuclein (SNCA), beta-synuclein (SNCB), microtubule-associated protein tau (MAPT), leucine-rich repeat kinase 2 (LRRK2), glucocerebrosidase (GBA), and exons 16 and 17 of the amyloid precursor protein (APP) genes did not identify any mutation.
Global analysis of aberrant pre-mRNA splicing in glioblastoma using exon expression arrays.
Krahe et al., Houston, United States. In Bmc Genomics, 2007
RESULTS: In total, we confirmed 14 genes with glioma-specific splicing; seven were novel events identified by the exon expression array (A2BP1, BCAS1, CACNA1G, CLTA, KCNC2, SNCB, and TPD52L2).
Is alpha-synuclein pathology a target for treatment of neurodegenerative disorders?
Wronski et al., Graz, Austria. In Curr Alzheimer Res, 2007
Beta-synuclein (betaS) a protein of the same gene family seems to be a naturally occurring anti aggregatory factor preventing AS aggregation in vitro and in vivo.
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