Amyloid polymorphs and pathological diversities

Ronald Melki

doi:10.1016/j.neuint.2022.105335

Amyloid polymorphs and pathological diversities

Neurochem Int. 2022 Jun:156:105335. doi: 10.1016/j.neuint.2022.105335. Epub 2022 Apr 5.

Author

Ronald Melki¹

Affiliation

¹ Institut Francois Jacob (MIRCen), CEA and Laboratory of Neurodegenerative Diseases, CNRS, 18 Route du Panorama, 92265, Fontenay-Aux-Roses cedex, France. Electronic address: ronald.melki@cnrs.fr.

PMID: 35395342
DOI: 10.1016/j.neuint.2022.105335

Abstract

The presence of protein aggregates within the central nervous system is intimately associated to debilitating neurodegenerative diseases. While the aggregation of proteins, that share no primary structure identity, is understandable in different diseases, that of a given protein yielding distinct pathologies is counterintuitive. This short review relates molecular and mechanistic processes to the observed pathological diversity.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid / chemistry
Humans
Neurodegenerative Diseases* / metabolism
Protein Aggregation, Pathological* / metabolism

Substances

Amyloid