Linked Life Data

17996987

Source:http://linkedlifedata.com/resource/pubmed/id/17996987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-7-1
pubmed:abstractText
Here we report the synthesis and biological properties of peptide-based molecules bearing constrained analogues of phenylalanine at the C-terminal. Compounds were tested as proteasome subunits' inhibitors. Dehydro-peptides showed good inhibition, in particular against trypsin-like (T-L) proteasome activity while some C-terminal Tic-derivatives inhibit only caspase-like activity in enzymatic beta1 subunits with a certain degree of efficacy. The best analogues of the series demonstrated good resistance to proteolysis and a capacity to permeate the cell membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0223-5234
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1403-11
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
C-terminal constrained phenylalanine as a pharmacophoric unit in peptide-based proteasome inhibitors.
pubmed:affiliation
Department of Pharmaceutical Sciences and Biotechnology Center, University of Ferrara, Ferrara, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't