참고문헌 (94)

1. Curr. Top. Med. Chem. A Galat 3 1315 2003 10.2174/1568026033451862 Galat, A. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr. Top. Med. Chem. 3, 1315-1347 (2003). 

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2. Mol. Carcinog. KP Lu 45 397 2006 10.1002/mc.20216 Lu, K. P. et al. Targeting carcinogenesis: a role for the prolyl isomerase Pin1? Mol. Carcinog. 45, 397-402 (2006). 

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3. Nature L Pastorino 440 528 2006 10.1038/nature04543 Pastorino, L. et al. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production. Nature 440, 528-534 (2006). 

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4. Nature KP Lu 380 544 1996 10.1038/380544a0 Lu, K. P., Hanes, S. D. & Hunter, T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547 (1996). PIN1 is identified and described for the first time in mammals as a NIMA-interacting protein with a potential role as a negative regulator of mitosis. 

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5. Yeast SD Hanes 5 55 1989 10.1002/yea.320050108 Hanes, S. D., Shank, P. R. & Bostian, K. A. Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5, 55-72 (1989). ESS1P, the yeast PIN1 homologue, is described as an essential protein in yeast, a fact that did not hold true in mammalian systems. 

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6. EMBO J. DG Crenshaw 17 1315 1998 10.1093/emboj/17.5.1315 Crenshaw, D. G., Yang, J., Means, A. R. & Kornbluth, S. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17, 1315-1327 (1998). 

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7. Genes Dev. M Shen 12 706 1998 10.1101/gad.12.5.706 Shen, M., Stukenberg, P. T., Kirschner, M. W. & Lu, K. P. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12, 706-720 (1998). 

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8. Mol. Cell PT Stukenberg 7 1071 2001 10.1016/S1097-2765(01)00245-3 Stukenberg, P. T. & Kirschner, M. W. Pin1 acts catalytically to promote a conformational change in Cdc25. Mol. Cell 7, 1071-1083 (2001). 

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9. Science KE Winkler 287 1644 2000 10.1126/science.287.5458.1644 Winkler, K. E., Swenson, K. I., Kornbluth, S. & Means, A. R. Requirement of the prolyl isomerase Pin1 for the replication checkpoint. Science 287, 1644-1647 (2000). 

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10. Proc. Natl Acad. Sci. USA R Maleszka 93 447 1996 10.1073/pnas.93.1.447 Maleszka, R., Hanes, S. D., Hackett, R. L., de Couet, H. G. & Miklos, G. L. The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 93, 447-451 (1996). 

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11. Biochem. Biophys. Res. Commun. F Fujimori 265 658 1999 10.1006/bbrc.1999.1736 Fujimori, F., Takahashi, K., Uchida, C. & Uchida, T. Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265, 658-663 (1999). The first of several papers to describe the germline deletion of PIN1. The only phenotype described in this publication was that PIN1-null were unable to efficiently re-enter the cell cycle from a quiescent state. Interestingly, no one has yet provided a direct mechanistic explanation for this phenomenon. 

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12. Gene R Maleszka 203 89 1997 10.1016/S0378-1119(97)00522-2 Maleszka, R., Lupas, A., Hanes, S. D. & Miklos, G. L. The dodo gene family encodes a novel protein involved in signal transduction and protein folding. Gene 203, 89-93 (1997). 

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13. Nature Cell Biol. T Hsu 3 538 2001 10.1038/35078508 Hsu, T., McRackan, D., Vincent, T. S. & Gert de Couet, H. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nature Cell Biol. 3, 538-543 (2001). 

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14. Proc. Natl Acad. Sci. USA YC Liou 99 1335 2002 10.1073/pnas.032404099 Liou, Y. C. et al. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Natl Acad. Sci. USA 99, 1335-1340 (2002). Describes notable phenotypes in Pin1 -deficient mice, and contains the first description of a non-mitotic target for PIN1. 

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15. Development FW Atchison 130 3579 2003 10.1242/dev.00584 Atchison, F. W., Capel, B. & Means, A. R. Pin1 regulates the timing of mammalian primordial germ cell proliferation. Development 130, 3579-3586 (2003). Elegantly describes how PIN1 can serve as a molecular 'timer' of G1/S progression, and shows that the lack of this function in the PIN1-null mouse leads to fewer divisions of the primordial germ cells and thus to infertility. 

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16. Biol. Reprod. FW Atchison 69 1989 2003 10.1095/biolreprod.103.020859 Atchison, F. W. & Means, A. R. Spermatogonial depletion in adult Pin1-deficient mice. Biol. Reprod. 69, 1989-1997 (2003). 

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17. J. Cell. Biochem. H You 84 211 2002 10.1002/jcb.10037 You, H. et al. IGF-1 induces Pin1 expression in promoting cell cycle S-phase entry. J. Cell. Biochem. 84, 211-216 (2002). 

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18. J. Biol. Chem. JD Joseph 279 32373 2004 10.1074/jbc.M405415200 Joseph, J. D., Daigle, S. N. & Means, A. R. PINA is essential for growth and positively influences NIMA function in Aspergillus nidulans. J. Biol. Chem. 279, 32373-32384 (2004). 

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19. Mol. Cell Biol. A Ryo 22 5281 2002 10.1128/MCB.22.15.5281-5295.2002 Ryo, A. et al. PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell Biol. 22, 5281-5295 (2002). 

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20. J. Biol. Chem. ES Yeh 281 241 2006 10.1074/jbc.M505770200 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. 281, 241-251 (2006). 

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21. Nature Cell Biol. A Ryo 3 793 2001 10.1038/ncb0901-793 Ryo, A., Nakamura, M., Wulf, G., Liou, Y. C. & Lu, K. P. Pin1 regulates turnover and subcellular localization of b-catenin by inhibiting its interaction with APC. Nature Cell Biol. 3, 793-801 (2001). 

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22. EMBO J. GM Wulf 20 3459 2001 10.1093/emboj/20.13.3459 Wulf, G. M. et al. Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1. EMBO J. 20, 3459-3472 (2001). The first paper to suggest that PIN1 might act as a tumour-promoting factor. The authors provide data that shows that PIN1 is upregulated in human tumour samples. 

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23. Nature Cell Biol. E Yeh 6 308 2004 10.1038/ncb1110 Yeh, E. et al. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nature Cell Biol. 6, 308-318 (2004). This paper provides a detailed molecular mechanism of how PIN1 regulates the stability of one of its important G1 targets, MYC, as well as the first data suggesting the possibility that PIN1 may act as a tumour suppressor. 

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24. Mol. Cell F Mantovani 14 625 2004 10.1016/j.molcel.2004.05.007 Mantovani, F. et al. Pin1 links the activities of c-Abl and p300 in regulating p73 function. Mol. Cell 14, 625-636 (2004). 

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25. Nature P Zacchi 419 853 2002 10.1038/nature01120 Zacchi, P. et al. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419, 853-857 (2002). 

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26. Nature H Zheng 419 849 2002 10.1038/nature01116 Zheng, H. et al. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 419, 849-853 (2002). An important set of publications that identify p53 as a target of PIN1 and demonstrate that p53 is regulated by PIN1 in response to cell stress. PIN1 is shown to be required for p53 stabilization, which is necessary for its activity as a transcription factor. 

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27. Mol. Cell MK Dougherty 17 215 2005 10.1016/j.molcel.2004.11.055 Dougherty, M. K. et al. Regulation of Raf-1 by direct feedback phosphorylation. Mol. Cell 17, 215-224 (2005). 

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28. Mol. Cell. Biol. P Yi 25 9687 2005 10.1128/MCB.25.21.9687-9699.2005 Yi, P. et al. Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1). Mol. Cell. Biol. 25, 9687-9699 (2005). 

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29. Cancer Res. G Ayala 63 6244 2003 Ayala, G. et al. The prolyl isomerase Pin1 is a novel prognostic marker in human prostate cancer. Cancer Res. 63, 6244-6251 (2003). 

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30. Am. J. Pathol. L Bao 164 1727 2004 10.1016/S0002-9440(10)63731-5 Bao, L. et al. Prevalent overexpression of prolyl isomerase Pin1 in human cancers. Am. J. Pathol. 164, 1727-1737 (2004). 

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31. Mol. Cell. Biol. SY Chen 26 929 2006 10.1128/MCB.26.3.929-939.2006 Chen, S. Y. et al. Activation of β-catenin signaling in prostate cancer by peptidyl-prolyl isomerase Pin1-mediated abrogation of the androgen receptor-β-catenin interaction. Mol. Cell. Biol. 26, 929-939 (2006). 

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32. Int. J. Oncol. M Fukuchi 29 329 2006 Fukuchi, M. et al. Prolyl isomerase Pin1 expression predicts prognosis in patients with esophageal squamous cell carcinoma and correlates with cyclinD1 expression. Int. J. Oncol. 29, 329-334 (2006). 

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33. World J. Gastroenterol. CJ Kim 11 5006 2005 10.3748/wjg.v11.i32.5006 Kim, C. J. et al. Pin1 overexpression in colorectal cancer and its correlation with aberrant beta-catenin expression. World J. Gastroenterol. 11, 5006-5009 (2005). 

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34. Apmis CJ Kim 114 518 2006 10.1111/j.1600-0463.2006.apm_379.x Kim, C. J. et al. Pin1 gene mutation is a rare event in gastric cancer. Apmis 114, 518-522 (2006). 

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35. Mol. Cancer Ther. DM Kokkinakis 4 1338 2005 10.1158/1535-7163.MCT-05-0141 Kokkinakis, D. M., Liu, X. & Neuner, R. D. Modulation of cell cycle and gene expression in pancreatic tumor cell lines by methionine deprivation (methionine stress): implications to the therapy of pancreatic adenocarcinoma. Mol. Cancer Ther. 4, 1338-1348 (2005). 

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36. J. Surg. Oncol. J Kuramochi 94 155 2006 10.1002/jso.20510 Kuramochi, J. et al. High Pin1 expression is associated with tumor progression in colorectal cancer. J. Surg. Oncol. 94, 155-160 (2006). 

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37. J. Huazhong Univ. Sci. Technolog. Med. Sci. H Li 26 120 2006 10.1007/BF02828056 Li, H. et al. Expression of Pin1 and Ki67 in cervical cancer and their significance. J. Huazhong Univ. Sci. Technolog. Med. Sci. 26, 120-122 (2006). 

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38. Ai Zheng HY Li 25 367 2006 Li, H. Y. et al. Expression and clinical significance of Pin1 and Cyclin D1 in cervical cancer cell lines and cervical epithelial tissues]. Ai Zheng 25, 367-372 (2006). 

39. Zhonghua Fu Chan Ke Za Zhi HY Li 41 417 2006 Li, H. Y. et al. Short hairpin RNA silences Pin1 and affects proliferation and apoptosis in HeLa cell line. Zhonghua Fu Chan Ke Za Zhi 41, 417-421 (2006). 

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40. Trends Biochem. Sci. KP Lu 29 200 2004 10.1016/j.tibs.2004.02.002 Lu, K. P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 29, 200-209 (2004). 

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41. Cancer Cell KP Lu 4 175 2003 10.1016/S1535-6108(03)00218-6 Lu, K. P. Prolyl isomerase Pin1 as a molecular target for cancer diagnostics and therapeutics. Cancer Cell 4, 175-180 (2003). 

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42. Oncol. Rep. H Miyashita 10 455 2003 Miyashita, H., Mori, S., Motegi, K., Fukumoto, M. & Uchida, T. Pin1 is overexpressed in oral squamous cell carcinoma and its levels correlate with cyclin D1 overexpression. Oncol. Rep. 10, 455-461 (2003). 

43. Oncol. Rep. H Miyashita 10 1045 2003 Miyashita, H., Uchida, T., Mori, S., Echigo, S. & Motegi, K. Expression status of Pin1 and cyclins in oral squamous cell carcinoma: Pin1 correlates with Cyclin D1 mRNA expression and clinical significance of cyclins. Oncol. Rep. 10, 1045-1048 (2003). 

44. J. Pathol. M Nakashima 202 446 2004 10.1002/path.1534 Nakashima, M. et al. Cyclin D1 overexpression in thyroid tumours from a radio-contaminated area and its correlation with Pin1 and aberrant β-catenin expression. J. Pathol. 202, 446-455 (2004). 

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45. J. Cell Sci. A Ryo 116 773 2003 10.1242/jcs.00276 Ryo, A., Liou, Y. C., Lu, K. P. & Wulf, G. Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer. J. Cell Sci. 116, 773-783 (2003). 

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46. Clin. Cancer Res. A Ryo 11 7523 2005 10.1158/1078-0432.CCR-05-0457 Ryo, A. et al. Stable suppression of tumorigenicity by Pin1-targeted RNA interference in prostate cancer. Clin. Cancer Res. 11, 7523-7531 (2005). 

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47. Pathol. Res. Pract. T Sasaki 202 357 2006 10.1016/j.prp.2005.12.007 Sasaki, T. et al. An immunohistochemical scoring system of prolyl isomerase Pin1 for predicting relapse of prostate carcinoma after radical prostatectomy. Pathol. Res. Pract. 202, 357-364 (2006). 

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56. Mol. Cell XZ Zhou 6 873 2000 10.1016/S1097-2765(05)00083-3 Zhou, X. Z. et al. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol. Cell 6, 873-883 (2000). 

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