Earticle

초록

영어

Amyloid oligomers are believed to play important causal roles in many types of amyloid-related degenerative diseases. Many different laboratories have reported amyloid oligomers that differ in size, morphology, toxicity, and method of preparation or purification, raising the question of the structural relationships among these oligomer preparations. The structural plasticity that has been reported to occur in amyloid formed from the same protein sequence indicates that it is quite possible that different oligomer preparations may represent distinct structural variants. In view of the difficulty in determining the precise structure of amyloids, conformation- and epitope-specific antibodies may provide a facile means of classifying amyloid oligomer structures. Conformation-dependent antibodies that recognize generic epitopes that are specifically associated with distinct aggregation states of many different amyloid-forming sequences indicate that there are at least two fundamentally distinct types of amyloid oligomers: fibrillar and prefibrillar oligomers. Classification of amyloid oligomers according to their underlying structures may be a more useful and rational approach than relying on differences in size and morphology.

목차

Abstract
 1. Introduction
 2. Different Classes of Amyloid Oligomers
 3. Is There any Common Epitopes, and Do They Have Different Forms of Prefibrillar and Fibrillar Oligomers?
 4. So is the Size is Important?
 5. Dose the Amyloid Aggregates Have Structural Polymorphisms within a Class?
 6. Amyloid Oligomers and its Structural Basis
 References

키워드

저자

• Pham Thi Dieu Tuyet [ Department of Biotechnology, Hanoi University of Science and Technology, University of Hanoi, Vietnam. ] Corresponding author

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  통합자연과학논문집(구 조선자연과학논문집) [Journal of Integrative Natural Science]

• 간기

  계간

• pISSN

  2005-1042

• 수록기간

  2008~2025

• 등재여부

  KCI 등재

• 십진분류

  KDC 405 DDC 505