Correction To: Α-Synuclein’s Uniquely Long Amphipathic Helix Enhances Its Membrane Binding and Remodeling Capacity

Journal of Membrane Biology- United States

doi 10.1007/s00232-018-0042-y

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July 27, 2018

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Springer Science and Business Media LLC

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Correction To: Α-Synuclein’s Uniquely Long Amphipathic Helix Enhances Its Membrane Binding and Remodeling Capacity

Journal of Membrane Biology- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

An N-Terminal Amphipathic Helix Binds Phosphoinositides and Enhances Kalirin Sec14 Domain-Mediated Membrane Interactions

Structural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-Binding Amphipathic Helix

A Predicted Amphipathic Helix Mediates Plasma Membrane Localization of GRK5

Tau Binds to Lipid Membrane Surfaces via Short Amphipathic Helices Located in Its Microtubule-Binding Repeats

Α-Synuclein-Induced Membrane Remodeling Is Driven by Binding Affinity, Partition Depth, and Interleaflet Order Asymmetry

Membrane Binding, Bending and Remodeling by Calcium Sensor Proteins

Protein-Drug Interactions in the Membrane: The Small Molecule Anle138b and Its Binding to Α-Synuclein Oligomers

Photoregulated Binding of Amphipathic Proteins to Azoaromatic Polymer

Intracellular Receptor-Type Transcription Factor, LasR, Contains a Highly Conserved Amphipathic Region Which Precedes the Putative Helix—turn—helix DNA Binding Motif