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Human SNCA Protein expressed in Escherichia coli (E. coli) - ABIN2005039
Lee, Choi, Lee: Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. in The Journal of biological chemistry 2002
Show all 2 Pubmed References
Rat (Rattus) SNCA Protein expressed in Rabbit - ABIN1742284
Jüttner, Moré, Das, Babich, Meier, Henning, Erdmann, Mu Ller, Otto, Grantyn, Rathjen: Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity. in Neuron 2005
study examined the spatial and temporal expression patterns of three synuclein genes (snca, sncbb, sncg) during embryogenesis
alpha-synuclein amyloids hijack prion protein to gain cell entry, facilitate cell-to-cell spreading and block prion replication.
at an early stage, SNCA-overexpressed increase mtROS accumulation, mitochondrial dysfunction and mtDNA decrement.
these results suggest that baicalein could prevent the progression of alpha-syn accumulation in PD mouse model partly by inhibiting formation of the alpha-syn oligomers.
findings thus support that AEP-mediated cleavage of alpha-Syn at N103 is required for the association and activation of MAO-B, mediating Parkinson's disease pathogenesis.
Radotinib HCl protects the alpha-synuclein preformed fibrils (PFF)-induced neuronal toxicity, reduces the alpha-synuclein PFF-induced Lewy bodies (LB)/Lewy neurites (LN)-like pathology and inhibits the alpha-synuclein PFF-induced c-Abl activation in primary cortical neurons.
these results provide for the first time evidence that a decrease of GCase or overexpression of mutant GCase in a chronic in vivo setting can affect ASYN secretion. Such effects may mediate enhanced propagation of ASYN, driving pathology in GBA-associated Parkinson's disease .
Taken together, these data suggest that PREP can enhance alpha-synuclein toxicity in vivo.
oligodendrocytes but not neurons transform misfolded alpha-Syn into a glial cytoplasmic inclusions-like strain, highlighting the fact that distinct alpha-Syn strains are generated by different intracellular milieus
Cardiolipin exposure on the outer mitochondrial membrane modulates alpha-synuclein in Parkinson's disease and cultured cardiomyocyte models.
A53T SNCA missense mutation caused impaired light entrainment of the circadian system in mice.
Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in alpha-Synuclein Aggregation Disorders
In this study, we assessed the spread of pathology following a localized induction of alphaS inclusions in the lumbar spinal cord following a unilateral injection in the sciatic nerve. Using this paradigm, we demonstrated the ability for alphaS inclusion spread and/or induction along neuroanatomical tracts within the CNS of two alphaS-overexpressing mouse models.
These results indicated that integrin CD11b mediates alpha-synuclein-induced NOX2 activation through a RhoA-dependent pathway.
High SNCA expression is associated with Parkinson's disease.
Snca regulates bone network homeostasis and ovariectomy-induced bone loss
These findings provide evidence for a novel mechanism underlying the protective effects of PINK1 against alpha-syn-induced neurodegeneration and highlight a novel therapeutic target for Parkinson's disease treatment.
study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner
the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32.
alpha-synuclein levels can be reduced in neurons without impairing (or improving) mitochondrial bioenergetics or distribution
Study shows that the age-dependent alpha-syn accumulation is correlated with an elevation of TRPC3 in the mitochondrial fractions isolated from monkey and mouse brains. In animal and cell models, alpha-syn overexpression was accompanied by an elevation of alpha-syn and TRPC3 in the mitochondrial fractions, and alpha-syn downregulation was associated with a reduction of the mitochondrial alpha-syn and TRPC3.
C-terminal truncated forms of alpha-synuclein (1-115, 1-119, 1-122, 1-124, 1-125, 1-129,1-133, and 1-135) are more prone to aggregation than full-length alpha-synuclein. They also can modulate the prion-like aggregation of full-length alpha-synuclein.
The Point mutations in SCNA is a rare cause of autosomal dominant Parkinson's disease in Turkey.
Comparison between PD-1/PD-L1 inhibitors (nivolumab, pembrolizumab, and atezolizumab) in pretreated NSCLC patients: Evidence from a Bayesian network model.
lowering parkin levels by extracellular ASN may significantly contribute to the propagation of neurodegeneration in Parkinson's disease pathology.
The authors show that SNCA Triplication pluripotent stem cell-derived macrophages (pMac), but not A53T pMac, have significantly increased intracellular alpha-synuclein versus controls and release significantly more alpha-synuclein to the medium. SNCA Triplication pMac, but not A53T pMac, show significantly reduced phagocytosis capability and this can be phenocopied by adding monomeric alpha-synuclein to the cell cultur...
the structure of cytotoxic alpha-synuclein fibrils (residues 1-121), determined by cryo-electron microscopy at a resolution of 3.4 A, is reported.
In rotenone-mediated dopaminergic cell models, the enhancement of p75 contributed to alpha-syn expression. The elevation of p75 also boosts the expression of ubiquitin ligase absentia homolog (siAH) and nuclear p65. Thus, p75 may enhance alpha-syn expression by promoting the activation of siAH, which is associated with ubiquitination.
FcgammaRIIB expressed in neurons functions as a receptor for alpha-syn fibrils and mediates cell-to-cell transmission of alpha-syn. SHP-1 and 2 are activated downstream by alpha-syn fibrils through FcgammaRIIB and play an important role in cell-to-cell transmission of alpha-syn.
Findings show that, despite the fact that alpha-synuclein is intrinsically disordered in solution, selective phosphorylation can modulate significantly its interactions with other molecules and suggest how this particular form of modification could play a key role in regulating the normal and aberrant function of alpha-synuclein.
The results of this study suggest that the recessive loss of function mutations act together with alpha-synuclein to cause Parkinson's disease, and that alpha-synuclein lowering strategies may be effective in genetic forms of Parkinson's disease.
Structural analysis shows that the lipid-binding domain of alpha-synuclein in fluorinated alcohols solutions resembling the vesicle-bound extended-helix state, indeed adopts a single continuous helix and that the ends of this helix do not come into detectable proximity to each other.
Alpha-synuclein is partitioned between water-soluble and membrane-bound states, and this highly regulated equilibrium influences its biological behavior under both physiological and pathological conditions. (Review)
Study shows that 14-3-3 protein sigma isoform co-localizes with phosphorylated alpha-synuclein in Lewy bodies and Lewy neurites in patients with Lewy body disease.
the prion-like seeding was reconstructed in reactions seeded with oligomer-like species, but not with insoluble aggregates of recombinant-alphaSyn, regardless of Ser129 phosphorylation status.
Results show that pathological alpha-synuclein in nigro-striatal axonal terminals leads to early axonal pathology, synaptic disruption, dysfunction of dopaminergic neurotransmission, motor impairment, and measurable change of VMAT2 in the absence of cell loss.
this study provides compelling evidence that a)autophagy-lysosome pathway (ALP) inhibition increases SNCA in neuronal autophagy-lysosome pathway (EVs), b) distinct ALP components are present in EVs, and c) CSF EVs transfer SNCA from cell to cell in vivo.
Refolding of helical soluble alpha-synuclein through transient interaction with lipid interfaces
alpha-synuclein influences calcium signaling and the aggregation and toxicity of alpha-synuclein is linked to Parkinson's disease.
Selective and durable downregulation of PD-L1 on CLL cells by 3 months post-treatment.
Our results confirm that the p. A53T SNCA mutation is relatively common in Greek patients with Parkinson disease or Parkinson disease plus dementia, particularly in cases with early onset and/or autosomal dominant family history.
analysis of membrane curvature sensing by amphipathic helices using alpha-synuclein and annexin B12 [ANXB12]
Immunocytochemistry shows alpha synuclein localized to the Golgi apparatus and vesicles of bovine adrenal medullary chromaffin cells, consistent with its putative role in vesicular function within synapses.
Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene.
, alpha SYN
, non-A beta component of AD amyloid
, non-A4 component of amyloid
, non A-beta component of AD amyloid
, synuclein alpha-140
, alpha synuclein