Title : Cellular membrane disruption by amyloid fibrils involved intermolecular disulfide cross-linking.

Pub. Date : 2009 Jun 30

PMID : 19449893






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes. Disulfides lysozyme Homo sapiens
2 LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes. Disulfides lysozyme Homo sapiens
3 The exposure of interior hydrophobic residues and the increased level of solvent-accessible disulfides in the lysozyme fibrils are thought to be involved in membrane disruption. Disulfides lysozyme Homo sapiens