About: Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form

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rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) 2002 թուականի Յունուարին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в січні 2002 (uk) 2002 թվականի հունվարին հրատարակված գիտական հոդված (hy) wetenschappelijk artikel (gepubliceerd op 2002/01/04) (nl) vedecký článok (publikovaný 2002/01/04) (sk) مقالة علمية (نشرت في 4-1-2002) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Januar 2002 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28567172-2C96148B-FFC5-4B07-B979-5D1B1FEAD71E
publication date	2002-01-04 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28567172-B23B5A85-EDFF-4D6A-A67B-E29EE8899C5B
language of work or name	English
author name string	wds:Q28567172-1203B073-E933-45F6-B133-E07FA4CADB01 wds:Q28567172-A0D20B7A-E1B2-4ED9-B8A1-B0E1358C8642 wds:Q28567172-AC72276E-9C30-4BCA-B448-9DAD750D1E45
OpenCitations bibliographic resource ID	wds:Q28567172-52318E32-0A65-48CF-9B67-EC37DB1FE9C2
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/936938
author name string	Chan Choi He-Jin Lee Seung-Jae Lee
OpenCitations bibliographic resource ID	936938
rdfs:label	Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (en) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (nl) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (ast)
skos:prefLabel	Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (en) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (nl) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (ast)
name	Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (en) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (nl) Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (ast)
title	wds:Q28567172-E2FFA6D3-2F11-460C-800F-3D9A3D59A0EE
title	Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form (en)
page(s)	wds:Q28567172-049A95AD-B4B8-4DF3-93FE-9516B3065618
page(s)	671–678
instance of	wds:Q28567172-06391B78-C37E-4424-9E96-F7406E8937DD
instance of	scholarly article
main subject	wds:Q28567172-AF3AC451-B4A9-4F54-8108-702858596337
main subject	Synuclein
PubMed ID	wds:Q28567172-5E88FB08-94A7-4D2B-B397-0873F4F9CB5F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11679584
PubMed ID	11679584
published in	wds:Q28567172-0809EBCE-F1EB-4B61-8179-5BDF2DF5488C
published in	Journal of Biological Chemistry
issue	wds:Q28567172-F0464526-EC0A-40AD-83AD-A7087DAA98D3
volume	wds:Q28567172-4060F205-E747-4E80-94CE-AC8D19EC9615
issue	1
volume	277
DOI	wds:Q28567172-4B33570B-38D6-4E8F-97D7-589BD881C340
DOI	http://dx.doi.org/10.1074/JBC.M107045200
DOI	10.1074/JBC.M107045200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28567172
is cites work of	alpha-Synuclein and neuronal cell death The function of α-synuclein Genetic clues to the pathogenesis of Parkinson's disease Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion Basic fibroblast growth factor protects against rotenone-induced dopaminergic cell death through activation of extracellular signal-regulated kinases 1/2 and phosphatidylinositol-3 kinase pathways A critical evaluation of the ubiquitin-proteasome system in Parkinson's disease Recent advances in the genetics of Parkinson's disease Structure and topology of the non-amyloid-beta component fragment of human alpha-synuclein bound to micelles: implications for the aggregation process Neural activity controls the synaptic accumulation of alpha-synuclein. Structural and functional characterization of two alpha-synuclein strains Enhanced substantia nigra mitochondrial pathology in human alpha-synuclein transgenic mice after treatment with MPTP. Cellular polyamines promote the aggregation of alpha-synuclein Is tau ready for admission to the prion club? Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity The AAA-ATPase VPS4 regulates extracellular secretion and lysosomal targeting of α-synuclein. Helix periodicity, topology, and dynamics of membrane-associated alpha-synuclein Lipid dysfunction and pathogenesis of multiple system atrophy The impact of genetic research on our understanding of Parkinson's disease Folding and misfolding of alpha-synuclein on membranes. Specificity and kinetics of alpha-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probe Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration. Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Differential expression of alpha-synuclein isoforms in dementia with Lewy bodies. Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases A broken alpha -helix in folded alpha -Synuclein Definition of a molecular pathway mediating α-synuclein neurotoxicity Alpha-synuclein function and dysfunction on cellular membranes The rotenone model of Parkinson's disease: genes, environment and mitochondria Alpha-synuclein and presynaptic function: implications for Parkinson's disease. A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides Site-specific interaction between α-synuclein and membranes probed by NMR-observed methionine oxidation rates Lewy bodies Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation Different species of alpha-synuclein oligomers induce calcium influx and seeding. α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling Lipid rafts mediate the synaptic localization of alpha-synuclein. An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage. Aberrant alternative splicing events in Parkinson's disease Immunotherapy for neurodegenerative diseases: focus on α-synucleinopathies Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of α-synuclein Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration

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