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The protein encoded by SNCB is highly homologous to alpha-synuclein. Additionally we are shipping beta Synuclein Proteins (17) and beta Synuclein Kits (7) and many more products for this protein.
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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 (show GRIN1 Antibodies) residues appears to be involved in fibril formation.
loss of inhibitory C-terminal conformations in disease associated P123H beta-synuclein
beta-Synuclein expression was locally concentrated and rather modest, but nevertheless changed its effect on amyloid precursor protein (show APP Antibodies) expression and plaque load in a time- and concentration-dependent manner.
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.
Beta-synuclein protects against isoaspartate accumulation in alpha-synuclein (show SNCA Antibodies).
In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells
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.
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.
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.
Despite both synucleins sharing considerable sequence homology, the level of carboxy-terminal Src kinase (show CSK Antibodies)-homologous kinase (CHK (show CHKA Antibodies)) phosphorylation of beta-synuclein is significantly higher than that of alpha-synuclein (show SNCA Antibodies).
Immunoblot analysis of beta-synuclein and Akt (show AKT1 Antibodies) levels in the mice reveals selective increases in beta-synuclein and phosphorylated Akt (show AKT1 Antibodies) levels in ventral midbrain
Beta-synuclein decreased formation of Lewy bodies by 40%, and prevented functional deficits associated with overexpression of alpha-synuclein. This is a preliminary in vivo proof of antiaggregatory function of beta-synuclein.
Accelerated accumulation of beta-synuclein is found in axonal spheroids of gracile axonal dystrophy mice, which do not express ubiquitin carboxyl-terminal hydrolase L1.
beta-synuclein knockout mice show that synucleins are not essential components of the basic machinery for neurotransmitter release but may contribute to the long-term regulation and/or maintenance of presynaptic function.
Developmentally, gamma-synuclein (show SNCG Antibodies) can be seen in the region of the outer hair cells by E19, while alpha- and beta-synuclein do not clearly appear there until approximately P10 (show NUTF2 Antibodies)
Data show the sequences of zebrafish synucleins are very similar to those of the human proteins. Whole-mount in situ hybridization show that sncb were expressed strongly in the nervous system.
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.
, PNP 14
, phosphoneuroprotein 14
, synuclein, beta
, putative beta-synuclein variant 1