The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes (Q24316619)

identical protein binding

GOA release 2020-03-11

1 reference

Jannik Nedergaard Pedersen

GOA release 2020-03-11

1 reference

object named as

Jannik Nedergaard Pedersen

3

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Daniel Otzen

object named as

Daniel Erik Otzen

5

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author name string

Nikolai Lorenzen

1

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Lasse Lemminger

2

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Søren Bang Nielsen

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

4

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language of work or name

English

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publication date

31 January 2014

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published in

FEBS Letters

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volume

588

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page(s)

497-502

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issue

3

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cites work

1 reference

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

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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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Spin-label EPR on alpha-synuclein reveals differences in the membrane binding affinity of the two antiparallel helices

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Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers

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Site-specific interaction between α-synuclein and membranes probed by NMR-observed methionine oxidation rates

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Structure and dynamics of micelle-bound human alpha-synuclein

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Conformational properties of alpha-synuclein in its free and lipid-associated states

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Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy

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The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding

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The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast

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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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Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing

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Assays for α-synuclein aggregation

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Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

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α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling

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Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins

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Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core.

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Asymmetric flow field-flow fractionation of liposomes: optimization of fractionation variables

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7 January 2021

inferred from DOI database lookup

The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.12.015

7 January 2021

inferred from DOI database lookup

Membrane interaction of α-synuclein in different aggregation states

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.12.015

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1016/J.FEBSLET.2013.12.015

1 reference

Consolidated OpenCitations Corpus – April 2017

release_zorcxyotg5burjizbmlbhb72aq

4064027

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/zorcxyotg5burjizbmlbhb72aq

24 November 2022

mapped directly with Wikidata item

4064027

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference