한빛사논문
- 조회1,226
Abstract
Shin Jung C. Lee,a† Eunju Nam,a† Hyuck Jin Lee,b Masha G. Savelieffcd and Mi Hee Lim*a
a Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea
b School of Life Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea
c Department of Neurosurgery, University of Michigan, Ann Arbor 48109, USA
d SciGency Science Communications, Ann Arbor 48104, USA
* Corresponding author
†These authors contributed equally to this work.
Abstract
Alzheimer's disease (AD) is characterized by an imbalance between production and clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers into β-stranded fibrils via multiple oligomeric states. Among the various Aβ species, structured oligomers are proposed to be more toxic than fibrils; however, the identification of Aβ oligomers has been challenging due to their heterogeneous and metastable nature. Multiple techniques have recently helped us gain a better understanding of oligomers' assembly details and structural properties. Moreover, some progress on elucidating the mechanisms of oligomer-triggered toxicity has been made. Based on the collection of current findings, there is growing consensus that control of toxic Aβ oligomers could be a valid approach to regulate Aβ-associated toxicity, which could advance development of new diagnostics and therapeutics for amyloid-related diseases. In this review, we summarize the recent understanding of Aβ oligomers' assembly, structural properties, and toxicity, along with inhibitors against Aβ aggregation, including oligomerization.
논문정보
- Review Paper
- 2016년 11월 (BRIC 등록일 2016-12-01)
- 국내(교신)+국외 연구진
- 생명과학 > 생화학
댓글 작성 로그인
팝업 닫기관련 링크
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기
