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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1998 2
1999 6
2000 8
2001 15
2002 19
2003 19
2004 35
2005 16
2006 1
2008 2
2009 2
2010 1
2011 1
2012 9
2013 8
2014 11
2015 7
2016 13
2017 13
2018 8
2019 4
2020 0
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180 results
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Page 1
Autophagy modulates SNCA/α-synuclein release, thereby generating a hostile microenvironment.
Poehler AM, et al. Autophagy 2014. PMID 25484190 Free PMC article.
In summary, our study revealed a novel role of the ALP by linking protein degradation to nonclassical secretion for toxic SNCA species. ...These findings suggest that the major toxic role of SNCA is related to its extracellular species and further supports a protective role of intracellular SNCA aggregation....
In summary, our study revealed a novel role of the ALP by linking protein degradation to nonclassical secretion for toxic SNCA
Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
Cuervo AM, et al. Science 2004. PMID 15333840 Free article.
Aberrant alpha-synuclein degradation is implicated in Parkinson's disease pathogenesis because the protein accumulates in the Lewy inclusion bodies associated with the disease. ...
Aberrant alpha-synuclein degradation is implicated in Parkinson's disease pathogenesis because the protein accumulates in the Lewy in …
Brain-derived exosomes from dementia with Lewy bodies propagate α-synuclein pathology
Ngolab J, et al. Acta Neuropathol Commun 2017. PMID 28599681 Free PMC article.
Proteins implicated in neurodegenerative conditions such as Alzheimer's disease (AD) and Dementia with Lewy Bodies (DLB) have been identified in bodily fluids encased in extracellular vesicles called exosomes. ...Exosomes extracted from brains diagnosed with either AD or DLB contained aggregate-prone proteins. Furthermore, injection of brain-derived exosomes from DLB patients into the brains of wild type mice induced α-synuclein (α-syn) aggregation. ...
Proteins implicated in neurodegenerative conditions such as Alzheimer's disease (AD) and Dementia with Lewy Bodies (DLB) have been id
Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates
Arawaka S, et al. Acta Neuropathol Commun 2017. PMID 28619113 Free PMC article.
This elevation was suppressively controlled by targeting Ser129-phosphorylated α-synuclein to the proteasome pathway. Rotenone-induced insoluble α-synuclein was also targeted by Ser129-phosphoryation to the proteasome pathway. Experiments with epoxomicin and chloroquine showed that proteasomal targeting of insoluble Ser129-phosphorylated α-synuclein was enhanced under lysosome inhibition and it reduced accumulation of insoluble total α-synuclein. ...
This elevation was suppressively controlled by targeting Ser129-phosphorylated α-synuclein to the proteasome pathway. Rotenone-induce …
Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein.
Oláh J, et al. J Biol Chem 2011. PMID 21832049 Free PMC article.
Here we identified TPPP/p25 as an interacting partner of the soluble Aβ oligomers as major risk factors for Alzheimer disease using ProtoArray human protein microarray. ...We showed that the Aβ(42) tightly bound to TPPP/p25 (K(d) = 85 nm) and caused aberrant protein aggregation by inhibiting the physiologically relevant TPPP/p25-derived microtubule assembly. ...
Here we identified TPPP/p25 as an interacting partner of the soluble Aβ oligomers as major risk factors for Alzheimer disease using ProtoArr …
Necrosis, apoptosis, necroptosis, three modes of action of dopaminergic neuron neurotoxins
Callizot N, et al. PLoS One 2019. PMID 31022188 Free PMC article.
Several pathways are central in PD pathogenesis: protein aggregation linked to proteasomal impairments, mitochondrial dysfunctions and impairment in dopamine (DA) release. ...We demonstrated that any of induced mitochondrial disturbances and processes of death led to α-syn protein aggregation and finally to cell death. ...
Several pathways are central in PD pathogenesis: protein aggregation linked to proteasomal impairments, mitochondrial dysfunct …
FKBP12 contributes to α-synuclein toxicity by regulating the calcineurin-dependent phosphoproteome
Caraveo G, et al. Proc Natl Acad Sci U S A 2017. PMID 29229832 Free PMC article.
Calcineurin can be inhibited with Tacrolimus through the recruitment and inhibition of the 12-kDa cis-trans proline isomerase FK506-binding protein (FKBP12). ...Using a rat model of PD, partial elimination of the functional interaction between FKBP12 and calcineurin, with low doses of the Food and Drug Administration (FDA)-approved compound Tacrolimus, blocks calcineurin's activity toward those proteins and protects against the toxic hallmarks of α-syn pathology. ...
Calcineurin can be inhibited with Tacrolimus through the recruitment and inhibition of the 12-kDa cis-trans proline isomerase FK506-binding …
Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation
van Diggelen F, et al. PLoS One 2019. PMID 30901378 Free PMC article.
Aggregation of the pre-synaptic protein α-synuclein (aSN) into oligomers (αSOs) is believed to play a key role in PD pathology, but little is known about αSO formation in vivo and how they induce neurodegeneration. ...
Aggregation of the pre-synaptic protein α-synuclein (aSN) into oligomers (αSOs) is believed to play a key role in PD pathology, but l …
α‑synuclein induces apoptosis of astrocytes by causing dysfunction of the endoplasmic reticulum‑Golgi compartment
Liu M, et al. Mol Med Rep 2018. PMID 29749529 Free PMC article.
In the present study, it was revealed that the mutant α‑syn (A53T and A30P) in astrocytes triggered ER stress via the protein kinase RNA‑like ER kinase/eukaryotic translation initiation factor 2α signaling pathway. Astrocyte apoptosis was induced through a CCAAT‑enhancer‑binding protein homologous protein‑mediated pathway. In addition, Golgi fragmentation was observed in the process. ...
In the present study, it was revealed that the mutant α‑syn (A53T and A30P) in astrocytes triggered ER stress via the protein kinase …
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