Structural disorder of monomeric α-synuclein persists in mammalian cells
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structural disorder of monomeric α-synuclein persists in mammalian cells
Authors
Keywords
-
Journal
NATURE
Volume 530, Issue 7588, Pages 45-50
Publisher
Springer Nature
Online
2016-01-23
DOI
10.1038/nature16531
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- New insights into cellular α-synuclein homeostasis in health and disease
- (2016) Ulf Dettmer et al. CURRENT OPINION IN NEUROBIOLOGY
- Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
- (2015) Céline Galvagnion et al. Nature Chemical Biology
- Thermodynamics of protein destabilization in live cells
- (2015) Jens Danielsson et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Quinary structure modulates protein stability in cells
- (2015) William B. Monteith et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation
- (2015) Ulf Dettmer et al. Nature Communications
- Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders
- (2015) Vladimir N. Uversky Frontiers in Aging Neuroscience
- Purification of α-Synuclein from Human Brain Reveals an Instability of Endogenous Multimers as the Protein Approaches Purity
- (2014) Eric S. Luth et al. BIOCHEMISTRY
- Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
- (2014) Francois-Xavier Theillet et al. CHEMICAL REVIEWS
- Probing Protein Conformation in Cells by EPR Distance Measurements using Gd3+ Spin Labeling
- (2014) Andrea Martorana et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
- (2014) B. G. Wilhelm et al. SCIENCE
- Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour
- (2014) Giuliana Fusco et al. Nature Communications
- In VivoCross-linking Reveals Principally Oligomeric Forms of α-Synuclein and β-Synuclein in Neurons and Non-neural Cells
- (2013) Ulf Dettmer et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- N-terminal Acetylation Stabilizes N-terminal Helicity in Lipid- and Micelle-bound α-Synuclein and Increases Its Affinity for Physiological Membranes
- (2013) Igor Dikiy et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Properties of native brain α-synuclein
- (2013) Jacqueline Burré et al. NATURE
- Defining the Native State of α-Synuclein
- (2013) Dennis Selkoe et al. Neurodegenerative Diseases
- Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?: Figure 1
- (2012) Andres Binolfi et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Impact of N-Terminal Acetylation of α-Synuclein on Its Random Coil and Lipid Binding Properties
- (2012) Alexander S. Maltsev et al. BIOCHEMISTRY
- Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
- (2012) Nunilo Cremades et al. CELL
- α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, andEscherichia coliExists Predominantly as Disordered Monomer
- (2012) Bruno Fauvet et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Characterization of Semisynthetic and NaturallyNα-Acetylated α-Synucleinin Vitroand in Intact Cells
- (2012) Bruno Fauvet et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- 100 years of Lewy pathology
- (2012) Michel Goedert et al. Nature Reviews Neurology
- The many faces of α-synuclein: from structure and toxicity to therapeutic target
- (2012) Hilal A. Lashuel et al. NATURE REVIEWS NEUROSCIENCE
- N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
- (2012) Lijuan Kang et al. PROTEIN SCIENCE
- Protein N-terminal acetyltransferases: when the start matters
- (2012) Kristian K. Starheim et al. TRENDS IN BIOCHEMICAL SCIENCES
- α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
- (2011) Tim Bartels et al. NATURE
- A soluble -synuclein construct forms a dynamic tetramer
- (2011) W. Wang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Detection of Transient Interchain Interactions in the Intrinsically Disordered Protein α-Synuclein by NMR Paramagnetic Relaxation Enhancement
- (2010) Kuen-Phon Wu et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- The catecholaminergic RCSN-3 cell line: A model to study dopamine metabolism
- (2009) Irmgard Paris et al. NEUROTOXICITY RESEARCH
- Structural and mechanistic basis behind the inhibitory interaction of PcTS on α-synuclein amyloid fibril formation
- (2009) Gonzalo R. Lamberto et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Single Particle Characterization of Iron-induced Pore-forming α-Synuclein Oligomers
- (2008) Marcus Kostka et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Differential Dynamical Effects of Macromolecular Crowding on an Intrinsically Disordered Protein and a Globular Protein: Implications for In-Cell NMR Spectroscopy
- (2008) Conggang Li et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started