Vivian Chen, Malik Moncalvo, Dominic Tringali, Lidia Tagliafierro, Ahila Shriskanda, Ekaterina Ilich, Wendy Dong, Boris Kantor, Ornit Chiba-Falek. Hum Mol Genet 2020
Times Cited: 14
Times Cited: 14
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Alpha-synuclein is a DNA binding protein that modulates DNA repair with implications for Lewy body disorders.
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Selective binding of nuclear alpha-synuclein to the PGC1alpha promoter under conditions of oxidative stress may contribute to losses in mitochondrial function: implications for Parkinson's disease.
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Proaggregant nuclear factor(s) trigger rapid formation of α-synuclein aggregates in apoptotic neurons.
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Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs.
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Identification of the amino acid sequence motif of alpha-synuclein responsible for macrophage activation.
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Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration.
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Red blood cells are the major source of alpha-synuclein in blood.
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α-Synuclein and astrocytes: tracing the pathways from homeostasis to neurodegeneration in Lewy body disease.
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Aggregated alpha-synuclein activates microglia: a process leading to disease progression in Parkinson's disease.
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Microglial activation and antioxidant responses induced by the Parkinson's disease protein α-synuclein.
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α-Synuclein-specific T cell reactivity is associated with preclinical and early Parkinson's disease.
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Immunoregulation of microglial polarization: an unrecognized physiological function of α-synuclein.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.