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How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?

Frontiers in neuroscience, 2022-11, Vol.16, p.1003997-1003997

2022

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Evaluation of Fluorophores to Label SNAP-Tag Fused Proteins for Multicolor Single-Molecule Tracking Microscopy in Live Cells

Biophysical journal, 2014-08, Vol.107 (4), p.803-814

2014

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

PloS one, 2010-12, Vol.5 (12), p.e14292-e14292

2010

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Solubilization of lipids and lipid phases by the styrene–maleic acid copolymer

European biophysics journal, 2017-01, Vol.46 (1), p.91-101

2017

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Classification of Dynamical Diffusion States in Single Molecule Tracking Microscopy

Biophysical journal, 2014-08, Vol.107 (3), p.588-598

2014

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Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells

PloS one, 2016-04, Vol.11 (4), p.e0153020-e0153020

2016

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Lipid-Conjugated Rigidochromic Probe Discloses Membrane Alteration in Model Cells of Krabbe Disease

Biophysical journal, 2019-02, Vol.116 (3), p.477-486

2019

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Refractive Index Sensing of Green Fluorescent Proteins in Living Cells Using Fluorescence Lifetime Imaging Microscopy

Biophysical journal, 2008-04, Vol.94 (8), p.L67-L69

2008

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Parkinson's Protein α-Synuclein Binds Efficiently and with a Novel Conformation to Two Natural Membrane Mimics

PloS one, 2015-11, Vol.10 (11), p.e0142795-e0142795

2015

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Integrin-dependent activation of the JNK signaling pathway by mechanical stress

PloS one, 2011-12, Vol.6 (12), p.e26182-e26182

2011

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p53 Specifically Binds Triplex DNA In Vitro and in Cells

PloS one, 2016-12, Vol.11 (12), p.e0167439-e0167439

2016

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Micromechanical bending of single collagen fibrils using atomic force microscopy

Journal of biomedical materials research. Part A, 2007-07, Vol.82A (1), p.160-168

2007

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Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates

Scientific reports, 2017-08, Vol.7 (1), p.7699-11, Article 7699

2017

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Spatiotemporal proliferation of human stromal cells adjusts to nutrient availability and leads to stanniocalcin-1 expression in vitro and in vivo

Biomaterials, 2015-08, Vol.61, p.190-202

2015

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EGFP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy

FEBS letters, 2000-08, Vol.479 (3), p.131-135

2000

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One- and Two-Photon Excited Fluorescence Lifetimes and Anisotropy Decays of Green Fluorescent Proteins

Biophysical journal, 2000-03, Vol.78 (3), p.1589-1598

2000

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Membrane interactions of oligomeric alpha-synuclein: potential role in Parkinson's disease

Current protein & peptide science, 2010-08, Vol.11 (5), p.334

2010

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Solution conditions define morphological homogeneity of α-synuclein fibrils

Biochimica et biophysica acta. Proteins and proteomics, 2014-12, Vol.1844 (12), p.2127-2134

2014

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Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy

Scientific reports, 2017-01, Vol.7 (1), p.41051-41051, Article 41051

2017

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Repeats in the α-Synuclein Sequence Determine its Conformation on Membranes and Influence Aggregation Properties

Biophysical journal, 2014-01, Vol.106 (2), p.268a-268a

2014

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Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils

Amyloid, 2018-07, Vol.25 (3), p.189-196

2018

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Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cellElectronic supplementary information (ESI) available: Experimental details, sample preparation, raw data, and analysis. See DOI: 10.1039/c7cp03432f

2017-07

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150 Getting a grip on alpha-synuclein amyloid oligomers

Journal of biomolecular structure & dynamics, 2013-01, Vol.31 (sup1), p.97-97

Subramaniam, Vinod

2013

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Hunting the Chameleon: Structural Conformations of the Intrinsically Disordered Protein Alpha-Synuclein

Chembiochem : a European journal of chemical biology, 2012-04, Vol.13 (6), p.761-768

2012

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Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore

FEBS letters, 2002-08, Vol.525 (1), p.13-19

2002

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How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?

Evaluation of Fluorophores to Label SNAP-Tag Fused Proteins for Multicolor Single-Molecule Tracking Microscopy in Live Cells

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

Solubilization of lipids and lipid phases by the styrene–maleic acid copolymer

Classification of Dynamical Diffusion States in Single Molecule Tracking Microscopy

Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells

Lipid-Conjugated Rigidochromic Probe Discloses Membrane Alteration in Model Cells of Krabbe Disease

Refractive Index Sensing of Green Fluorescent Proteins in Living Cells Using Fluorescence Lifetime Imaging Microscopy

Parkinson's Protein α-Synuclein Binds Efficiently and with a Novel Conformation to Two Natural Membrane Mimics

Integrin-dependent activation of the JNK signaling pathway by mechanical stress

p53 Specifically Binds Triplex DNA In Vitro and in Cells

Micromechanical bending of single collagen fibrils using atomic force microscopy

Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates

Spatiotemporal proliferation of human stromal cells adjusts to nutrient availability and leads to stanniocalcin-1 expression in vitro and in vivo

EGFP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy

One- and Two-Photon Excited Fluorescence Lifetimes and Anisotropy Decays of Green Fluorescent Proteins

Membrane interactions of oligomeric alpha-synuclein: potential role in Parkinson's disease

Solution conditions define morphological homogeneity of α-synuclein fibrils

Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy

Repeats in the α-Synuclein Sequence Determine its Conformation on Membranes and Influence Aggregation Properties

Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils

Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cellElectronic supplementary information (ESI) available: Experimental details, sample preparation, raw data, and analysis. See DOI: 10.1039/c7cp03432f

150 Getting a grip on alpha-synuclein amyloid oligomers

Hunting the Chameleon: Structural Conformations of the Intrinsically Disordered Protein Alpha-Synuclein

Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore

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