Identification of a novel class of small-molecule antiangiogenic agents through the screening of combinatorial libraries which function by inhibiting the binding and localization of proteinase MMP2 to integrin alpha(V)beta(3).
Boger, D L
Identification of a novel class of small-molecule antiangiogenic agents through the screening of combinatorial libraries which function by inhibiting the binding and localization of proteinase MMP2 to integrin alpha(V)beta(3). [electronic resource] - Journal of the American Chemical Society Feb 2001 - 1280-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0002-7863
10.1021/ja003579+ doi
Angiogenesis Inhibitors--analysis
Animals
Combinatorial Chemistry Techniques
Humans
Matrix Metalloproteinase 2--metabolism
Matrix Metalloproteinase Inhibitors
Models, Chemical
Neovascularization, Pathologic--physiopathology
Neovascularization, Physiologic--physiology
Peptide Library
Protein Binding
Receptors, Vitronectin--metabolism
Solubility
Vitronectin--metabolism
Identification of a novel class of small-molecule antiangiogenic agents through the screening of combinatorial libraries which function by inhibiting the binding and localization of proteinase MMP2 to integrin alpha(V)beta(3). [electronic resource] - Journal of the American Chemical Society Feb 2001 - 1280-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0002-7863
10.1021/ja003579+ doi
Angiogenesis Inhibitors--analysis
Animals
Combinatorial Chemistry Techniques
Humans
Matrix Metalloproteinase 2--metabolism
Matrix Metalloproteinase Inhibitors
Models, Chemical
Neovascularization, Pathologic--physiopathology
Neovascularization, Physiologic--physiology
Peptide Library
Protein Binding
Receptors, Vitronectin--metabolism
Solubility
Vitronectin--metabolism