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Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin

Authors
 Young-Sik Kim  ;  Daekyun Lee  ;  Eun-Kyung Lee  ;  Jee Young Sung  ;  Kwang Chul Chung  ;  Jongsun Kim  ;  Seung R Paik 
Citation
 Brain Research, Vol.908(1) : 93-98, 2001 
Journal Title
 Brain Research 
ISSN
 0006-8993 
Issue Date
2001
Abstract
Various protein aggregates of α-synuclein developed by way of the common protein self-oligomerization in the presence of Aβ25-35, copper, and eosin were examined. All the aggregates exhibited congo red birefringence although the actual amounts of the aggregates were varied as determined by thioflavin T binding fluorescence. When their morphologies were analyzed in relation to in vitro cytotoxicity, the smallest granular aggregates obtained with copper exhibited the highest cytotoxicity, while the fibrous structures by eosin did not affect the cell.
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/142563
DOI
10.1016/S0006-8993(01)02575-6
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실)
Yonsei Authors
김종선(Kim, Jong Sun)
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Full Text
http://www.sciencedirect.com/science/article/pii/S0006899301025756
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