Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins (Q34111411)

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English	Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

31 July 2017

Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins (English)

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Europe PubMed Central

PubMed publication ID

31 July 2017

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Sebastian Doniach

5

object named as

Sebastian Doniach

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Europe PubMed Central

PubMed publication ID

31 July 2017

Vladimir N. Uversky

1

object named as

Vladimir N Uversky

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31 July 2017

author name string

Jie Li

2

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31 July 2017

Pierre Souillac

3

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31 July 2017

Ian S Millett

4

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31 July 2017

Ross Jakes

6

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31 July 2017

Michel Goedert

7

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31 July 2017

Anthony L Fink

8

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31 July 2017

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publication date

25 January 2002

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31 July 2017

number of pages

9

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Journal of Biological Chemistry

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31 July 2017

277

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31 July 2017

14

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31 July 2017

11970-11978

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Europe PubMed Central

PubMed publication ID

31 July 2017

Alpha-synuclein and neurodegenerative diseases

1 reference

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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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Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

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Identification of two distinct synucleins from human brain

1 reference

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Cloning and characterization of the cDNA encoding a novel brain-specific 14-kDa protein

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Organization, expression and polymorphism of the human persyn gene

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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

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

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Evidence for a partially folded intermediate in alpha-synuclein fibril formation

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Cell and tissue distribution and developmental change of neuron specific 14 kDa protein (phosphoneuroprotein 14)

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NACP, a synaptic protein involved in Alzheimer's disease, is differentially regulated during megakaryocyte differentiation

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Distribution of phosphoneuroprotein 14 (PNP 14) in vertebrates: its levels as determined by enzyme immunoassay

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Developmentally regulated expression of persyn, a member of the synuclein family, in skin.

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Alpha-synuclein in Lewy bodies

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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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Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

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Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

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Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders

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A Drosophila model of Parkinson's disease

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Degenerative terminals of the perforant pathway are human alpha-synuclein-immunoreactive in the hippocampus of patients with diffuse Lewy body disease

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Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia

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Antibodies to alpha-synuclein detect Lewy bodies in many Down's syndrome brains with Alzheimer's disease

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Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for alpha-synuclein

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Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies

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Axon pathology in Parkinson's disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein

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Synthetic filaments assembled from C-terminally truncated alpha-synuclein

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Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease

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Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease

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Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation

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alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease

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Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation

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Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

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Parkinson's disease-associated alpha-synuclein is more fibrillogenic than beta- and gamma-synuclein and cannot cross-seed its homologs

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A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.

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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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Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism

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Protein Denaturation

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beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor

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Changes in biomolecular conformation seen by small angle X-ray scattering

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Identifiers

10.1074/JBC.M109541200

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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