α-Synuclein as an intrinsically disordered monomer--fact or artefact? (Q24316089)

identical protein binding

GOA release 2020-03-11

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GOA release 2020-03-11

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Eduardo Coelho-Cerqueira

1

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Phelippe Carmo-Gonçalves

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Anderson Sá Pinheiro

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Juliana Cortines

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Cristian Follmer

Alpha-synuclein and neurodegenerative diseases

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language of work or name

English

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publication date

October 2013

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published in

FEBS Journal

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volume

280

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page(s)

4915-27

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issue

19

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cites work

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Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro

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

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The aggregation and fibrillation of alpha-synuclein

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

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α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

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A soluble α-synuclein construct forms a dynamic tetramer

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In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells

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α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

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N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein

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A new method for purification of recombinant human alpha-synuclein in Escherichia coli.

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Translocation of alpha-synuclein expressed in Escherichia coli

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Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein

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Dependence of alpha-synuclein aggregate morphology on solution conditions

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Assays for α-synuclein aggregation

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

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

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Detection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement

21 January 2018

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Alpha-synuclein: stable compact and extended monomeric structures and pH dependence of dimer formation

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Population of nonnative states of lysozyme variants drives amyloid fibril formation

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Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule.

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Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.

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Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder.

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

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Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?

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Properties of native brain α-synuclein

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Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

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Helix capping propensities in peptides parallel those in proteins

21 January 2018

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N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

21 January 2018

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Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties

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Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein

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N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer

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Effect of pseudorepeat rearrangement on alpha-synuclein misfolding, vesicle binding, and micelle binding

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Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro

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