Publication

Cryo-EM structure of alpha-synuclein fibrils

Related publications (46)

About
Privacy
Disclaimer

Graph Chatbot

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

Cryo-EM structure of alpha-synuclein fibrils

Graph Chatbot

Chat with Graph Search

Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease

New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy

Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports

Gold nanoparticles as a new tool in amyloid studies

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

Molecular dissection of amyloid disaggregation by human HSP70

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy