Familial Mutants of α-Synuclein with Increased Neurotoxicity Have a Destabilized Conformation (Q58484320)

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31 December 2019

title

Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation (English)

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31 December 2019

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31 December 2019

Claudio O. Fernandez

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31 December 2019

author name string

Christian Griesinger

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31 December 2019

Markus Zweckstetter

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31 December 2019

Thomas M Jovin

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31 December 2019

language of work or name

English

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publication date

14 July 2005

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Journal of Biological Chemistry

31 December 2019

published in

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31 December 2019

volume

280

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31 December 2019

issue

35

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31 December 2019

page(s)

30649-30652

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Alpha-synuclein and neurodegenerative diseases

31 December 2019

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alpha-Synuclein locus triplication causes Parkinson's disease

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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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Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

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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

21 January 2018

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Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease

21 January 2018

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Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system

21 January 2018

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

21 January 2018

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Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro

21 January 2018

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Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations

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Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein

21 January 2018

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Structural characterization of copper(II) binding to alpha-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

21 January 2018

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Dependence of alpha-synuclein aggregate morphology on solution conditions

21 January 2018

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

21 January 2018

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Unfolded proteins and protein folding studied by NMR.

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Alpha-synuclein structures from fluorescence energy-transfer kinetics: implications for the role of the protein in Parkinson's disease

21 January 2018

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Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T.

21 January 2018

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Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c

21 January 2018

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The protein folding 'speed limit'.

21 January 2018

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Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings

21 January 2018

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Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

21 January 2018

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

21 January 2018

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Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease.

21 January 2018

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Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis

21 January 2018

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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.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.C500288200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16020550%20AND%20SRC:MED&resulttype=core&format=json

31 December 2019

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