Steve Friedman

Conversion of an MMP-potent scaffold to an MMP-selective HER-2 sheddase inhibitor via scaffold hybridization and subtle <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si3.gif" overflow="scroll"><mml:mrow><mml:msubsup><mml:mrow><mml:mtext>P</mml:mtext></mml:mrow><mml:mrow><mml:mn>1</mml:mn></mml:mrow><mml:mrow><mml:mo>′</mml:mo></mml:mrow></mml:msubsup></mml:mrow></mml:math> permutations

Design and identification of selective HER-2 sheddase inhibitors via P1′ manipulation and unconventional P2′ perturbations to induce a molecular metamorphosis

Discovery of novel selective HER-2 sheddase inhibitors through optimization of P1 moiety

Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition

Corrigendum to “Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition” [Bioorg. Med. Chem. Lett. 19 (2009) 3525]

HER2/EGFR in Cancer Research

Peptidase Inhibition and Analysis

Ethics in Clinical Research

Protease and Inhibitor Mechanisms

Monoclonal and Polyclonal Antibodies Research