Work

Heterotypic amyloid interactions: Clues to polymorphic bias and selective cellular vulnerability?

Year: 2021

Type: review

Source: Current Opinion in Structural Biology

DOI: 10.1016/j.sbi.2021.11.007

Authors: Nikolaos Louros, Joost Schymkowitz, Frederic Rousseau

Institutions: VIB-KU Leuven Center for Brain & Disease Research, KU Leuven

Language: English

Topic: Prion Diseases and Protein Misfolding

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Fonds Wetenschappelijk Onderzoek, KU Leuven, Vlaams Instituut voor Biotechnologie, Vlaamse regering

Awards: G2475798000, Mapping the impact of post-translational modifications on protein aggregation., Atomic Force Microscopy Enhanced Spectroscopy to Study Strains and Seeding of Amyloids In Situ, A high-throughput platform for screening amyloid strains and their seeding capacity at single-particle resolution, Principles of specificity in cross-aggregation interactions, Cellular handling of protein aggregation gatekeepers, G8248501640, Towards understanding the specificity of protein aggregation, G8524111995

OpenAlex ID: W4200102773

FWCI: 0.262

Cites: 99

Cited by: 21

Related to: 10