Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation. (Q45057099)

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1 January 2020

title

Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation (English)

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2

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author name string

Roberto Hodara

1

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1 January 2020

Benoit I Giasson

3

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Amanda J Mishizen-Eberz

4

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David R Lynch

5

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Virginia M-Y Lee

6

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Harry Ischiropoulos

7

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language of work or name

English

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publication date

9 September 2004

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Journal of Biological Chemistry

1 January 2020

published in

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volume

279

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page(s)

47746-47753

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issue

46

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The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

1 January 2020

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Characterization of a novel protein regulated during the critical period for song learning in the zebra finch.

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Identification of two distinct synucleins from human brain

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Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

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Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins

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Structural changes in alpha-synuclein affect its chaperone-like activity in vitro

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Structural and functional implications of C-terminal regions of alpha-synuclein

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alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

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Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble alpha-synuclein.

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Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease alpha-synuclein fibrillogenesis

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Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

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Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein

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Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

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Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications

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Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

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Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis.

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Distinct cleavage patterns of normal and pathologic forms of alpha-synuclein by calpain I in vitro

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Cytochrome c nitration by peroxynitrite.

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Endoproteolytic activity of the proteasome

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Distinct roles of the N-terminal-binding domain and the C-terminal-solubilizing domain of alpha-synuclein, a molecular chaperone

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Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function

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Proteasomal function is impaired in substantia nigra in Parkinson's disease

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α-Synuclein Is Degraded by Both Autophagy and the Proteasome

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Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease

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Parkin cleaves intracellular alpha-synuclein inclusions via the activation of calpain

21 January 2018

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Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease

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Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct

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Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro

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Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila

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Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein

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Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes.

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The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation

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Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism.

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Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

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Alpha-synuclein has a high affinity for packing defects in a bilayer membrane: a thermodynamics study.

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Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation.

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Lipid binding inhibits alpha-synuclein fibril formation

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Membrane binding and self-association of alpha-synucleins.

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Identifiers

DOI

10.1074/JBC.M408906200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15364911%20AND%20SRC:MED&resulttype=core&format=json

1 January 2020

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