Elin Esbjörner Winters
Elin Esbjörner is Associate Professor of Chemical Biology. Her research group studies protein misfolding and amyloid formation phenomena related to neurodegenerative diseases, using a combination of in vitro biophysics methods and cell biological approaches, including fluorescence microscopies and live cell imaging. The group focuses on how amyloid proteins interact with cells and cellular membranes, on their cell uptake and trafficking mechanisms, as well as on how different biological and pharmacological modulators affect the amyloid formation process. Elin is also a Principle Investigation in the for functional RNA delivery, where her group collaborates extensively with chemists and physicists to explore fundamental mechanisms for effective cellular uptake (endocytosis) and cytosolic delivery of nucleic-acid based drugs. Within this consortium, Elin’s group also contributes to the development of new fluorescent probes and bioanalytical methods to explore the interaction of drug delivery vectors with cells.
Showing 60 publications
The inhibition of fibril formation of lysozyme by sucrose and trehalose
CATIONIC NANOPARTICLES MODULATE ELECTROSTATIC INTERACTIONS IN CATABOLIC CARTILAGE
Probing physical properties of single amyloid fibrils using nanofluidic channels
Pore formation by melittin in porous silica-supported lipid membranes
Probing physical properties of single amyloid fibrils using nanofluidic channels
Novel endosomolytic compounds enable highly potent delivery of antisense oligonucleotides
Single-shot self-supervised object detection in microscopy
Stealth Fluorescence Labeling for Live Microscopy Imaging of mRNA Delivery
A Nanofluidic Device for Multiplexed Analysis of Single Exosomes
The Liver and Kidneys mediate clearance of cardiac troponin in the rat
Novel clearance of muscle proteins by muscle cells
Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro
Copper Chaperone Atox1 Interacts with Cell Cycle Proteins
A nano flow cytometer for single lipid vesicle analysis
Time-resolved thioflavin-T fluorescence-expanding the amyloid characterisation toolbox
Assigning Membrane Binding Geometry of Cytochrome c by Polarized Light Spectroscopy
DNA condensation by PAMAM dendrimers: Self-assembly characteristics and effect on transcription
Stimulated endocytosis in penetratin uptake: Effect of arginine and lysine
Tryptophan Orientation in Model Lipid Membranes
Retinoid chromophores as probes of membrane lipid order
Membrane Interactions of Cell-Penetrating Peptides
Membrane interaction properties of cell-penetrating peptides
Membrane binding and translocation of cell-penetrating peptides
Vesicle size-dependent translocation of penetratin analogs across lipid membranes
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Showing 15 research projects
Nanochannel Microscopy for Single Exosome Analysis
An in vitro platform to evaluate nanomedicine performance in blood
Eludicating endosomal escape for the next generation of mRNA delivery vehicles
The Stability of Amyloid Fibrils - a case study on a-synuclein
Crosstalk of Membrane trafficking and Protein aggregation in Neurodegenerative Disease
Differential cellilar uptake of alpha-synuclein monomers, oligomers and short fibrils
The role of lipid droplets in neurodegeneration studied in cells using advanced microscopy
Improved resolution in imaging of amyloid fibrils using non-covalent fluorescent dyes
Funktionell leverans av nukleotid-baserade läkemedel
Vad karaktäriserar en toxisk amyloid oligomer?
Identification of Cellular Targets for Amyloid Beta Toxicity in Alzheimers Disease