Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2009-4-13
pubmed:abstractText
Overexpression of zinc-dependent metalloproteinase, aminopeptidase N (APN/CD13), is considered to be involved in the process of tumor invasion and metastasis. Herein we describe the synthesis and in vitro enzymatic inhibition assay of antineoplaston AS2-5 scaffold peptidomimetic compounds. The results demonstrated that most of these L-iso-glutamine derivatives displayed selective inhibitory activity against APN as compared with MMP-2, with IC(50) values in the micromole range. The structure-activity relationships were also briefly discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1464-3391
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3053-60
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Novel aminopeptidase N inhibitors derived from antineoplaston AS2-5 (Part I).
pubmed:affiliation
School of Pharmaceutical Sciences, Shandong University, No. 44 WenhuaXi Road, Ji'nan, 250012, Shandong Province, PR China.
pubmed:publicationType
Journal Article