List of works - Tim Bartels

A traffic jam leads to Lewy bodies

scientific article published on 01 July 2019

Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease.

scientific article

Defining the native state of α-synuclein

scientific article published on 30 October 2013

E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity

scientific article published on 02 May 2019

ExPLAining early synucleinopathies.

scientific article

Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons.

scientific article

KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity

scientific article

Microglia modulate neurodegeneration in Alzheimer's and Parkinson's diseases

scientific article published on 01 October 2020

N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation

scientific article

New insights into cellular α-synuclein homeostasis in health and disease.

scientific article published on 14 August 2015

Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.

scientific article

Raftlike mixtures of sphingomyelin and cholesterol investigated by solid-state 2H NMR spectroscopy.

scientific article published on 08 October 2008

Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.

scientific article published on 10 April 2018

Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes

scientific article

Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.

scientific article

The N-Terminus of the Intrinsically Disordered Protein α-Synuclein Triggers Membrane Binding and Helix Folding ⬇️

scientific article published on October 6, 2010

pTSara-NatB, an improved N-terminal acetylation system for recombinant protein expression in E. coli.

scientific article

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

scientific article

β2-Adrenoreceptor is a regulator of the α-synuclein gene driving risk of Parkinson's disease.

scientific article

List of works by Tim Bartels

A traffic jam leads to Lewy bodies

Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease.

Defining the native state of α-synuclein

E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity

ExPLAining early synucleinopathies.

Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons.

KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity

Microglia modulate neurodegeneration in Alzheimer's and Parkinson's diseases

N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation

New insights into cellular α-synuclein homeostasis in health and disease.

Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.

Raftlike mixtures of sphingomyelin and cholesterol investigated by solid-state 2H NMR spectroscopy.

Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.

Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes

Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.

The N-Terminus of the Intrinsically Disordered Protein α-Synuclein Triggers Membrane Binding and Helix Folding ⬇️

pTSara-NatB, an improved N-terminal acetylation system for recombinant protein expression in E. coli.

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

β2-Adrenoreceptor is a regulator of the α-synuclein gene driving risk of Parkinson's disease.