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Updated: Mar 30, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Amyloids: from Pathogenesis to Function
A A Nizhnikov1, K S Antonets, S G Inge-Vechtomov
1Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, 199034, Russia. ant.nizhnikov@gmail.com.
Amyloids are protein aggregates linked to diseases but also play vital cellular roles. Recent research redefines their function, revealing their importance across all life forms and leading to the new field of amyloidomics.
Area of Science:
- Biochemistry and Molecular Biology
- Cell Biology
- Structural Biology
Background:
- Amyloids are protein aggregates characterized by a cross-β structure.
- Historically linked to incurable human diseases (amyloidoses).
- Recent discoveries highlight their essential roles in cellular functions across all domains of life.
Purpose of the Study:
- To provide a retrospective analysis of amyloid biology.
- To highlight the reinterpretation of amyloids' biological roles.
- To introduce the development of systems biology of amyloids (amyloidomics).
Main Methods:
- Literature review and retrospective analysis.
- Examination of historical and recent research on amyloid structure and function.
- Synthesis of findings to establish the field of amyloidomics.
Main Results:
- Amyloids are not solely pathogenic; they are crucial for cellular processes.
- Functional amyloids are involved in diverse roles, from bacterial biofilms to memory in eukaryotes.
- Prions, a class of infectious proteins, often exhibit amyloid features.
- The field of amyloidomics has emerged, integrating systems biology approaches.
Conclusions:
- The understanding of amyloids has shifted from pathogens to essential biological components.
- Amyloid research has evolved significantly, revealing their widespread functional importance.
- Amyloidomics represents a new frontier in understanding protein structure and function.
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