Structure-guided design of alpha-amino acid-derived Pin1 inhibitors.

[1]  Samantha Greasley,et al.  Structure-based design of novel human Pin1 inhibitors (I). , 2009, Bioorganic & medicinal chemistry letters.

[2]  Z. Dong,et al.  The prolyl isomerase Pin1 interacts with a ribosomal protein S6 kinase to enhance insulin-induced AP-1 activity and cellular transformation. , 2009, Carcinogenesis.

[3]  P. van der Sluijs,et al.  Juglone Inactivates Cysteine-rich Proteins Required for Progression through Mitosis* , 2008, Journal of Biological Chemistry.

[4]  Roderick E Hubbard,et al.  The SeeDs approach: integrating fragments into drug discovery. , 2007, Current topics in medicinal chemistry.

[5]  M. Bowman,et al.  Structural basis for high-affinity peptide inhibition of human Pin1. , 2007, ACS chemical biology.

[6]  W. Frank,et al.  Aryl indanyl ketones: efficient inhibitors of the human peptidyl prolyl cis/trans isomerase Pin1. , 2006, Angewandte Chemie.

[7]  H. Akiyama,et al.  Comparative analysis of enzyme activities and mRNA levels of peptidyl prolyl cis/trans isomerases in various organs of wild type and Pin1 −/− mice , 2006, FEBS letters.

[8]  Xiao Zhen Zhou,et al.  Nanomolar inhibitors of the peptidyl prolyl cis/trans isomerase Pin1 from combinatorial peptide libraries. , 2006, Journal of medicinal chemistry.

[9]  Akira Yamaguchi,et al.  Stable Suppression of Tumorigenicity by Pin1-Targeted RNA Interference in Prostate Cancer , 2005, Clinical Cancer Research.

[10]  Brian Dymock,et al.  Design and Characterization of Libraries of Molecular Fragments for Use in NMR Screening against Protein Targets , 2004, J. Chem. Inf. Model..

[11]  Priti Garg,et al.  Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis , 2004, The EMBO journal.

[12]  A. Hopkins,et al.  Ligand efficiency: a useful metric for lead selection. , 2004, Drug discovery today.

[13]  Xiao Zhen Zhou,et al.  Pin1 modulates the structure and function of human RNA polymerase II. , 2003, Genes & development.

[14]  Sam W. Lee,et al.  PIN1 Is an E2F Target Gene Essential for Neu/Ras-Induced Transformation of Mammary Epithelial Cells , 2002, Molecular and Cellular Biology.

[15]  T. Hunter,et al.  Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[16]  Tianhua Niu,et al.  Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c‐Jun towards cyclin D1 , 2001, The EMBO journal.

[17]  A. Schnapp,et al.  Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis. , 2000, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.

[18]  G. Fischer,et al.  Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. , 1998, Biochemistry.

[19]  M. Kirschner,et al.  Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. , 1997, Science.

[20]  Y. Matsuo,et al.  Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation. , 2003, Chemistry & biology.

[21]  Masafumi Nakamura,et al.  Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC , 2001, Nature Cell Biology.