Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication (Q24317181)

identical protein binding

GOA release 2020-03-11

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GOA release 2020-03-11

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Yuan-Yuan Xie

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Chen-Jie Zhou

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Zi-Ren Zhou

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Jing Hong

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Mei-Xia Che

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Qing-Shan Fu

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Ai-Xin Song

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Dong-Hai Lin

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Hong-Yu Hu

Synphilin-1 is present in Lewy bodies in Parkinson's disease

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language of work or name

English

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publication date

January 2010

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196-205

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cites work

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Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments

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The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease

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Transfected synphilin-1 forms cytoplasmic inclusions in HEK293 cells

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Sequence conservation between mouse and human synphilin-1

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Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay

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Aggresomes, inclusion bodies and protein aggregation

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NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Prospects for new restorative and neuroprotective treatments in Parkinson's disease

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α-Synuclein in Lewy bodies

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Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions

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Interaction of alpha-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations

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Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients

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NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation

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Induction of neuronal cell death by Rab5A-dependent endocytosis of alpha-synuclein

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Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein

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Dorfin Localizes to Lewy Bodies and Ubiquitylates Synphilin-1

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Siah-1 facilitates ubiquitination and degradation of synphilin-1

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Prolyl-isomerase Pin1 accumulates in lewy bodies of parkinson disease and facilitates formation of alpha-synuclein inclusions

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Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1

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Aggregate formation and toxicity by wild-type and R621C synphilin-1 in the nigrostriatal system of mice using adenoviral vectors.

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The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity

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