rdf:type |
|
lifeskim:mentions |
umls-concept:C0007428,
umls-concept:C0012512,
umls-concept:C0013089,
umls-concept:C0026336,
umls-concept:C0030685,
umls-concept:C0033262,
umls-concept:C0391871,
umls-concept:C0678594,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1514873,
umls-concept:C1963578,
umls-concept:C2603343
|
pubmed:issue |
23
|
pubmed:dateCreated |
1999-1-21
|
pubmed:abstractText |
A series of lysosomal protease-sensitive peptides attached to doxorubicin (DOX) was prepared as model substrates for internalizing anticancer immunoconjugates and potential antimetastasis prodrugs. Rates of cathepsin B-mediated release of free drug was measured for each, and human plasma stabilities for representative examples.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0960-894X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
8
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3341-6
|
pubmed:dateRevised |
2004-11-17
|
pubmed:meshHeading |
|
pubmed:year |
1998
|
pubmed:articleTitle |
Cathepsin B-sensitive dipeptide prodrugs. 1. A model study of structural requirements for efficient release of doxorubicin.
|
pubmed:affiliation |
Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492-7660, USA.
|
pubmed:publicationType |
Journal Article
|