Journal
BIOCHEMISTRY
Volume 53, Issue 51, Pages 8001-8004Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi501333q
Keywords
-
Categories
Funding
- IIT Jodhpur
- BRNS
Ask authors/readers for more resources
The question of how an aggregating protein can influence aggregation of other proteins located in its vicinity is particularly significant because many proteins coexist in cells. We demonstrate in vitro coaggregation and cross-seeding of lysozyme, bovine serum albumin, insulin, and cytochrome c during their amyloid formation. The coaggregation process seems to be more dependent on the temperature-induced intermediate species of these proteins and less dependent on their sequence identities. Because amyloid-linked inclusions and plaques are recognized as multicomponent entities originating from aggregation of the associated protein, these findings may add new insights into the mechanistic understanding of amyloid-related pathologies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available