Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2003-10-31
pubmed:abstractText
We have studied the model peptides that undergo self-initiated structural transition from alpha-helix to beta-sheet and self-assembling into amyloid fibrils. We here constructed an inhibition system of amyloid formation utilizing homologous recognition and assembly of peptides with increased solubility. Among 20 peptides with homologous sequences examined here, cationic peptides showed the stronger inhibition ability against the amyloid formation of a model peptide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4051-4
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Inhibition of peptide amyloid formation by cationic peptides with homologous sequences.
pubmed:affiliation
Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
pubmed:publicationType
Journal Article