메뉴 건너뛰기




Volumn 53, Issue 6, 2010, Pages 2494-2501

Membrane permeable cyclic peptidyl inhibitors against human peptidylprolyl isomer ase pin1

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; ARGININE; BETA ACTIN; CYCLIC PEPTIDYL INHIBITOR; PEPTIDE LIBRARY; PEPTIDYLPROLYL ISOMERASE PIN1; PROMYELOCYTIC LEUKEMIA PROTEIN; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; UNCLASSIFIED DRUG;

EID: 77949860245     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm901778v     Document Type: Article
Times cited : (63)

References (47)
  • 1
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
    • Fischer, G.; Aumuller, T. Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 2003, 148, 105-150.
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.148 , pp. 105-150
    • Fischer, G.1    Aumuller, T.2
  • 2
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- Or phosphothreonine-binding modules
    • Lu, P. J.; Zhou, X. Z.; Shen, M. H.; Lu, K. P. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 1999, 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.H.3    Lu, K.P.4
  • 4
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase Pinl: A pivotal new twist in phosphorylation signaling and disease
    • Lu, K. P.; Zhou, X. Z. The prolyl isomerase Pinl: a pivotal new twist in phosphorylation signaling and disease. Nat. Rev. Mol. Cell Biol. 2007, 8, 904-916.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 5
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pinl, interacts with Cdc25 and Plx1
    • Crenshaw, D. G.; Yang, J.; Means, A. R.; Kornbluth, S. The mitotic peptidyl-prolyl isomerase, Pinl, interacts with Cdc25 and Plx1. EMBO J. 1998, 17, 1315-1327.
    • (1998) EMBO J. , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 6
    • 0035947078 scopus 로고    scopus 로고
    • Pin1 acts catalytically to promote a conformational change in Cdc25
    • Stukenberg, P. T.; Kirschner, M. W. Pin1 acts catalytically to promote a conformational change in Cdc25. Mol. Cell 2001, 7, 1071-1083.
    • (2001) Mol. Cell , vol.7 , pp. 1071-1083
    • Stukenberg, P.T.1    Kirschner, M.W.2
  • 8
    • 34247282654 scopus 로고    scopus 로고
    • Mechanism for inactivation of the mitotic inhibitory kinase Weel at M phase
    • Okamoto, K.; Sagata, N. Mechanism for inactivation of the mitotic inhibitory kinase Weel at M phase. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 3753-3758.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3753-3758
    • Okamoto, K.1    Sagata, N.2
  • 9
    • 0032771752 scopus 로고    scopus 로고
    • A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pinl
    • Albert, A. L.; Lavoie, S.; Vincent, M. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pinl. J. Cell Sci. 1999, 112, 2493-2500.
    • (1999) J. Cell Sci. , vol.112 , pp. 2493-2500
    • Albert, A.L.1    Lavoie, S.2    Vincent, M.3
  • 10
    • 34247196176 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 functions in mitotic chromosome condensation
    • Xu, Y. X.; Manley, J. L. The prolyl isomerase Pin1 functions in mitotic chromosome condensation. Mol. Cell 2007, 26, 287-300.
    • (2007) Mol. Cell , vol.26 , pp. 287-300
    • Xu, Y.X.1    Manley, J.L.2
  • 11
    • 0035796405 scopus 로고    scopus 로고
    • Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1
    • Wulf, G. M.; Ryo, A.; Wulf, G. G.; Lee, S. W.; Niu, T. H.; Petkova, V.; Lu, K. P. Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. EMBO J. 2001, 20, 3459-3472.
    • (2001) EMBO J. , vol.20 , pp. 3459-3472
    • Wulf, G.M.1    Ryo, A.2    Wulf, G.G.3    Lee, S.W.4    Niu, T.H.5    Petkova, V.6    Lu, K.P.7
  • 13
    • 33644850537 scopus 로고    scopus 로고
    • The loss of PIN1 deregulates cyclin e and sensitizes mouse embryo fibroblasts to genomic instability
    • Yeh, E. S.; Lew, B. O.; Means, A. R. The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability. J. Biol. Chem. 2006, 281, 241-251.
    • (2006) J. Biol. Chem. , vol.281 , pp. 241-251
    • Yeh, E.S.1    Lew, B.O.2    Means, A.R.3
  • 17
    • 20744432450 scopus 로고    scopus 로고
    • Mutations in proline 82 of p53 impair its activation by Pinl and Chk2 in response to DNA damage
    • Berger, M.; Stahl, N.; Del Sal, G.; Haupt, Y. Mutations in proline 82 of p53 impair its activation by Pinl and Chk2 in response to DNA damage. Mol. Cell. Biol. 2005, 25, 5380-5388.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5380-5388
    • Berger, M.1    Stahl, N.2    Del Sal, G.3    Haupt, Y.4
  • 19
    • 27444440554 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of c-Fos by ERK: A novel role for the prolyl isomerase Pinl
    • Monje, P.; Hernandez-Losa, J.; Lyons, R. J.; Castellone, M. D.; Gutkind, J. S. Regulation of the transcriptional activity of c-Fos by ERK: a novel role for the prolyl isomerase Pinl. J. Biol. Chem. 2005, 250, 35081-35084.
    • (2005) J. Biol. Chem. , vol.250 , pp. 35081-35084
    • Monje, P.1    Hernandez-Losa, J.2    Lyons, R.J.3    Castellone, M.D.4    Gutkind, J.S.5
  • 20
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-kB signaling by Pin1-dependent proly1 isomerization and ubiquitinmediated proteolysis of p65/RelA
    • Ryo, A.; Suizu, F.; Yoshida, Y.; Perrem, K; Liou, Y. C.; Wulf, G.; Rottapel, R.; Yamaoka, S.; Lu, K. P. Regulation of NF-kB signaling by Pin1-dependent proly1 isomerization and ubiquitinmediated proteolysis of p65/RelA. Mo0I. Cell 2003, 12, 1413-1426.
    • (2003) Mo0I. Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1    Suizu, F.2    Yoshida, Y.3    Perrem, K.4    Liou, Y.C.5    Wulf, G.6    Rottapel, R.7    Yamaoka, S.8    Lu, K.P.9
  • 21
    • 0034840950 scopus 로고    scopus 로고
    • Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC
    • Ryo, A.; Nakamura, N.; Wulf, G.; Liou, Y. C.; Lu, K. P. Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC Nat. Cell Biol. 2001, 5, 793-801.
    • (2001) Nat. Cell Biol. , vol.5 , pp. 793-801
    • Ryo, A.1    Nakamura, N.2    Wulf, G.3    Liou, Y.C.4    Lu, K.P.5
  • 22
    • 31344433667 scopus 로고    scopus 로고
    • Activation of β-catenin signaling in prostate cancer by peptidylprolyl isomerase Pinl-mediated abrogation of the androgen receptor-β-catenin interaction
    • Chen, S. Y.; Wulf, G.; Zhou, X. Z.; Rubin, M. A.; Lu, K. P.; Balk, S. P. Activation of β-catenin signaling in prostate cancer by peptidylprolyl isomerase Pinl-mediated abrogation of the androgen receptor-β-catenin interaction. Mol. Cell. Biol. 2006, 26, 929-939.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 929-939
    • Chen, S.Y.1    Wulf, G.2    Zhou, X.Z.3    Rubin, M.A.4    Lu, K.P.5    Balk, S.P.6
  • 23
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K. P.; Hanes, S. D.; Hunter, T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 1996, 380, 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 24
    • 0034050649 scopus 로고    scopus 로고
    • Requirement of the prolyl isomerase Pinl for the replication checkpoint
    • Winkler, K. E.; Swenson, K. I.; Kornbluth, S.; Means, A. R. Requirement of the prolyl isomerase Pinl for the replication checkpoint. Science 2000, 287, 1644-1647.
    • (2000) Science , vol.287 , pp. 1644-1647
    • Winkler, K.E.1    Swenson, K.I.2    Kornbluth, S.3    Means, A.R.4
  • 29
    • 43049124394 scopus 로고    scopus 로고
    • Novel spiroannulated 3-benzofuranones. Synthesis and inhibition of the human peptidyl prolyl isomerase Pin1
    • Braun, M.; Hessamian-Alinejad, A.; Feaux de Lacroix, B.; Alvarez, B. H.; Fischer, G. Novel spiroannulated 3-benzofuranones. Synthesis and inhibition of the human peptidyl prolyl isomerase Pin1. Molecules 2008, 13, 995-1003.
    • (2008) Molecules , vol.13 , pp. 995-1003
    • Braun, M.1    Hessamian-Alinejad, A.2    De Feaux Lacroix, B.3    Alvarez, B.H.4    Fischer, G.5
  • 33
    • 9644302270 scopus 로고    scopus 로고
    • Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere
    • Wang, X. J.; Xu, B. L.; Mullins, A. B.; Neiler, F. K.; Etzkorn, F. A. Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere. J. Am. Chem. Soc. 2004, 126, 15533-15542.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15533-15542
    • Wang, X.J.1    Xu, B.L.2    Mullins, A.B.3    Neiler, F.K.4    Etzkorn, F.A.5
  • 37
    • 42449142364 scopus 로고    scopus 로고
    • Cyclic peptidyl inhibitors of Grb2 and tensin SH2 domains identified from combinatorial libraries
    • Zhang, Y.; Zhou, S. G.; Wavreille, A. S.; DeWille, J.; Pei, D. Cyclic peptidyl inhibitors of Grb2 and tensin SH2 domains identified from combinatorial libraries. J. Comb. Chem. 2008, 10, 247-255.
    • (2008) J. Comb. Chem. , vol.10 , pp. 247-255
    • Zhang, Y.1    Zhou, S.G.2    Wavreille, A.S.3    Dewille, J.4    Pei, D.5
  • 38
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidyl-prolyl isomerase Pin 1 binds and regulates mitosis-specific phosphoproteins
    • Shen, M.; Stukenberg, P. T.; Kirschner, M. W.; Lu, K. P. The essential mitotic peptidyl-prolyl isomerase Pin 1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 1998, 12, 706-720.
    • (1998) Genes Dev. , vol.12 , pp. 706-720
    • Shen, M.1    Stukenberg, P.T.2    Kirschner, M.W.3    Lu, K.P.4
  • 39
    • 33747621649 scopus 로고    scopus 로고
    • Traceless capping agent for peptide sequencing by partial Edman degradation and mass spectrometry
    • Thakkar, A.; Wavreille, A.-S.; Pei, D. Traceless capping agent for peptide sequencing by partial Edman degradation and mass spectrometry. Anal. Chem. 2006, 78, 5935-5939.
    • (2006) Anal. Chem. , vol.78 , pp. 5935-5939
    • Thakkar, A.1    Wavreille, A.-S.2    Pei, D.3
  • 40
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron, J. L.; Kuzmic, P.; Kishore, V.; Colonbonilla, E.; Rich, D. H. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 1991, 30, 6112-6134.
    • (1991) Biochemistry , vol.30 , pp. 6112-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colonbonilla, E.4    Rich, D.H.5
  • 41
    • 33847735051 scopus 로고    scopus 로고
    • A chemical approach to the identification of tensin-binding proteins
    • Wavreille, A. S.; Pei, D. A chemical approach to the identification of tensin-binding proteins. ACS Chem. Biol. 2007, 2, 109-118.
    • (2007) ACS Chem. Biol. , vol.2 , pp. 109-118
    • Wavreille, A.S.1    Pei, D.2
  • 42
    • 38549132438 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells
    • Reineke, E. L.; Lam, M.; Liu, O.; Liu, Y.; Stanya, K. J.; Chang, K. S.; Means, A. R.; Kao, H. Y. Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells. Mol. Cell. Biol. 2008, 28, 997-1006.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 997-1006
    • Reineke, E.L.1    Lam, M.2    Liu, O.3    Liu, Y.4    Stanya, K.J.5    Chang, K.S.6    Means, A.R.7    Kao, H.Y.8
  • 43
    • 53749085961 scopus 로고    scopus 로고
    • Cdk2 and Pin1 negatively regulate the transcriptional corepressor SMRT
    • Stanya, K. J.; Liu, Y.; Means, A. R.; Kao, H. Y. Cdk2 and Pin1 negatively regulate the transcriptional corepressor SMRT. J. Cell Biol. 2008, 183, 49-61.
    • (2008) J. Cell Biol. , vol.183 , pp. 49-61
    • Stanya, K.J.1    Liu, Y.2    Means, A.R.3    Kao, H.Y.4
  • 45
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives, E.; Brodin, P.; Lebleu, B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 1997, 272, 16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 46
    • 33749532845 scopus 로고    scopus 로고
    • High-throughput sequence determination of cyclic peptide library members by partial Edman degradation/mass spectrometry
    • Joo, S. H.; Xiao, Q.; Ling, Y.; Gopishetty, B.; Pei, D. High-throughput sequence determination of cyclic peptide library members by partial Edman degradation/mass spectrometry. J. Am. Chem. Soc. 2006, 128, 13000-13009.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13000-13009
    • Joo, S.H.1    Xiao, Q.2    Ling, Y.3    Gopishetty, B.4    Pei, D.5
  • 47
    • 58949090838 scopus 로고    scopus 로고
    • Synthesis and screening of a cyclic peptide library: Discovery of small-molecule ligands against human prolactin receptor
    • Liu, T.; Joo, S. H.; Voorhees, J. L.; Brooks, C. L.; Pei, D. Synthesis and screening of a cyclic peptide library: discovery of small-molecule ligands against human prolactin receptor. Bioorg. Med. Chem. 2009, 17, 1026-1033.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1026-1033
    • Liu, T.1    Joo, S.H.2    Voorhees, J.L.3    Brooks, C.L.4    Pei, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.