메뉴 건너뛰기




Volumn 36, Issue 10, 2011, Pages 501-514

Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; CYCLIN D1; G PROTEIN COUPLED RECEPTOR KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE; MYC PROTEIN; ONCOPROTEIN; PEPTIDYLPROLYL ISOMERASE PIN1; PHOSPHOPROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN MCL 1; RETINOIC ACID RECEPTOR ALPHA; SMAD PROTEIN; STEROID RECEPTOR COACTIVATOR 3; STRESS ACTIVATED PROTEIN KINASE; TELOMERIC REPEAT BINDING FACTOR 1; TRANSCRIPTION FACTOR E2F;

EID: 80053299231     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2011.07.001     Document Type: Review
Times cited : (297)

References (144)
  • 1
    • 0036806311 scopus 로고    scopus 로고
    • Evolution of protein kinase signaling from yeast to man
    • Manning G., et al. Evolution of protein kinase signaling from yeast to man. Trends Biochem. Sci. 2002, 27:514-520.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 514-520
    • Manning, G.1
  • 2
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling-50 years and counting
    • Pawson T., Scott J.D. Protein phosphorylation in signaling-50 years and counting. Trends Biochem. Sci. 2005, 30:286-290.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 3
    • 34548660854 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer
    • Lu K.P., et al. Prolyl cis-trans isomerization as a molecular timer. Nat. Chem. Biol. 2007, 3:619-629.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 619-629
    • Lu, K.P.1
  • 4
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
    • Lu K.P., Zhou X.Z. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling 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
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K.P., et al. 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
  • 6
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu P.J., et al. 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
  • 7
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., et al. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 1997, 89:875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1
  • 8
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism
    • Yaffe M.B. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 1997, 278:1957-1960.
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1
  • 9
    • 79953127123 scopus 로고    scopus 로고
    • 5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72
    • 5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72. J. Biol. Chem. 2011, 286:5717-5726.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5717-5726
    • Werner-Allen, J.W.1
  • 10
    • 0033638180 scopus 로고    scopus 로고
    • Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins
    • Zhou X.Z., et al. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol. Cell 2000, 6:873-883.
    • (2000) Mol. Cell , vol.6 , pp. 873-883
    • Zhou, X.Z.1
  • 11
    • 0037022355 scopus 로고    scopus 로고
    • Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes
    • Liou Y.C. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:1335-1340.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1335-1340
    • Liou, Y.C.1
  • 12
    • 0043069764 scopus 로고    scopus 로고
    • Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration
    • Liou Y.C., et al. Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. Nature 2003, 424:556-561.
    • (2003) Nature , vol.424 , pp. 556-561
    • Liou, Y.C.1
  • 13
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu P.J., et al. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 1999, 399:784-788.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1
  • 14
    • 0034840950 scopus 로고    scopus 로고
    • Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC
    • Ryo A., et al. Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 2001, 3:793-801.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 793-801
    • Ryo, A.1
  • 15
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA
    • Ryo A., et al. Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 2003, 12:1413-1426.
    • (2003) Mol. Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1
  • 16
    • 0037073713 scopus 로고    scopus 로고
    • Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage
    • Wulf G.M. Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage. J. Biol. Chem. 2002, 277:47976-47979.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47976-47979
    • Wulf, G.M.1
  • 17
    • 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., 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. 2001, 20:3459-3472.
    • (2001) EMBO J. , vol.20 , pp. 3459-3472
    • Wulf, G.M.1
  • 18
    • 18644384283 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults
    • Zacchi P., et al. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 2002, 419:853-857.
    • (2002) Nature , vol.419 , pp. 853-857
    • Zacchi, P.1
  • 19
    • 18644384688 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
    • Zheng H., et al. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 2002, 419:849-853.
    • (2002) Nature , vol.419 , pp. 849-853
    • Zheng, H.1
  • 20
    • 79954456974 scopus 로고    scopus 로고
    • Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function
    • Lee T.H., et al. Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function. Mol. Cell 2011, 42:147-159.
    • (2011) Mol. Cell , vol.42 , pp. 147-159
    • Lee, T.H.1
  • 21
    • 0037169479 scopus 로고    scopus 로고
    • Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function
    • Lu P.J., et al. Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function. J. Biol. Chem. 2002, 277:2381-2384.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2381-2384
    • Lu, P.J.1
  • 22
    • 0036315162 scopus 로고    scopus 로고
    • PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells
    • Ryo A., et al. PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol. 2002, 22:5281-5295.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5281-5295
    • Ryo, A.1
  • 23
    • 0035676154 scopus 로고    scopus 로고
    • IGF-1 induces Pin1 expression in promoting cell cycle S-phase entry
    • You H., et al. IGF-1 induces Pin1 expression in promoting cell cycle S-phase entry. J. Cell. Biochem. 2002, 84:211-216.
    • (2002) J. Cell. Biochem. , vol.84 , pp. 211-216
    • You, H.1
  • 24
    • 80053304845 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerase Pin1 in aging, cancer and Alzheimer's disease
    • Lee T.H., et al. Peptidyl-prolyl cis-trans isomerase Pin1 in aging, cancer and Alzheimer's disease. Expert Rev. Mol. Med. 2011, 13:e21.
    • (2011) Expert Rev. Mol. Med. , vol.13
    • Lee, T.H.1
  • 25
    • 0020022916 scopus 로고
    • Mechanisms of intracellular protein breakdown
    • Hershko A., Ciechanover A. Mechanisms of intracellular protein breakdown. Annu. Rev. Biochem. 1982, 51:335-364.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 335-364
    • Hershko, A.1    Ciechanover, A.2
  • 26
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994, 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1
  • 27
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 2001, 70:503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 28
    • 33745156511 scopus 로고    scopus 로고
    • Ubiquitin and SUMO systems in the regulation of mitotic checkpoints
    • Gutierrez G.J., Ronai Z. Ubiquitin and SUMO systems in the regulation of mitotic checkpoints. Trends Biochem. Sci. 2006, 31:324-332.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 324-332
    • Gutierrez, G.J.1    Ronai, Z.2
  • 29
    • 0037462424 scopus 로고    scopus 로고
    • Cdc4 ubiquitin ligase
    • Cdc4 ubiquitin ligase. Cell 2003, 112:243-256.
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1
  • 30
    • 33947140574 scopus 로고    scopus 로고
    • Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?
    • Balastik M., et al. Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?. Biochim. Biophys. Acta 2007, 1772:422-429.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 422-429
    • Balastik, M.1
  • 31
    • 39349085931 scopus 로고    scopus 로고
    • Pinning down signaling in the immune system: the role of the peptidyl-prolyl isomerase Pin1 in immune cell function
    • Esnault S., et al. Pinning down signaling in the immune system: the role of the peptidyl-prolyl isomerase Pin1 in immune cell function. Crit. Rev. Immunol. 2008, 28:45-60.
    • (2008) Crit. Rev. Immunol. , vol.28 , pp. 45-60
    • Esnault, S.1
  • 32
    • 34848907217 scopus 로고    scopus 로고
    • Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1
    • Lippens G., et al. Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1. FEBS J. 2007, 274:5211-5222.
    • (2007) FEBS J. , vol.274 , pp. 5211-5222
    • Lippens, G.1
  • 33
    • 34247490735 scopus 로고    scopus 로고
    • PIN1, the cell cycle and cancer
    • Yeh E.S., Means A.R. PIN1, the cell cycle and cancer. Nat. Rev. Cancer 2007, 7:381-388.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 381-388
    • Yeh, E.S.1    Means, A.R.2
  • 34
    • 1942533406 scopus 로고    scopus 로고
    • Prevalent overexpression of prolyl isomerase Pin1 in human cancers
    • Bao L., et al. Prevalent overexpression of prolyl isomerase Pin1 in human cancers. Am. J. Pathol. 2004, 164:1727-1737.
    • (2004) Am. J. Pathol. , vol.164 , pp. 1727-1737
    • Bao, L.1
  • 35
    • 0028308702 scopus 로고
    • Cyclin D1 protein expression and function in human breast cancer
    • Bartkova J., et al. Cyclin D1 protein expression and function in human breast cancer. Int. J. Cancer 1994, 57:353-361.
    • (1994) Int. J. Cancer , vol.57 , pp. 353-361
    • Bartkova, J.1
  • 36
    • 0033119801 scopus 로고    scopus 로고
    • β-catenin regulates expression of cyclin D1 in colon carcinoma cells
    • Tetsu O., McCormick F. β-catenin regulates expression of cyclin D1 in colon carcinoma cells. Nature 1999, 398:422-426.
    • (1999) Nature , vol.398 , pp. 422-426
    • Tetsu, O.1    McCormick, F.2
  • 37
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl J.A., et al. Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 1998, 12:3499-3511.
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1
  • 38
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl J.A., et al. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 1997, 11:957-972.
    • (1997) Genes Dev. , vol.11 , pp. 957-972
    • Diehl, J.A.1
  • 39
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
    • Smeal T., et al. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 1991, 354:494-496.
    • (1991) Nature , vol.354 , pp. 494-496
    • Smeal, T.1
  • 40
    • 77952423398 scopus 로고    scopus 로고
    • Elevated PIN1 expression by C/EBPα-p30 blocks C/EBPα-induced granulocytic differentiation through c-Jun in AML
    • Pulikkan J.A., et al. Elevated PIN1 expression by C/EBPα-p30 blocks C/EBPα-induced granulocytic differentiation through c-Jun in AML. Leukemia 2010, 24:914-923.
    • (2010) Leukemia , vol.24 , pp. 914-923
    • Pulikkan, J.A.1
  • 41
    • 0036234124 scopus 로고    scopus 로고
    • MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis
    • Craig R.W. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 2002, 16:444-454.
    • (2002) Leukemia , vol.16 , pp. 444-454
    • Craig, R.W.1
  • 42
    • 34347350211 scopus 로고    scopus 로고
    • Degradation of Mcl-1 by β-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization
    • Ding Q., et al. Degradation of Mcl-1 by β-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization. Mol. Cell. Biol. 2007, 27:4006-4017.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4006-4017
    • Ding, Q.1
  • 43
    • 51049101063 scopus 로고    scopus 로고
    • Down-regulation of myeloid cell leukemia-1 through inhibiting Erk/Pin 1 pathway by sorafenib facilitates chemosensitization in breast cancer
    • Ding Q., et al. Down-regulation of myeloid cell leukemia-1 through inhibiting Erk/Pin 1 pathway by sorafenib facilitates chemosensitization in breast cancer. Cancer Res. 2008, 68:6109-6117.
    • (2008) Cancer Res. , vol.68 , pp. 6109-6117
    • Ding, Q.1
  • 44
    • 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., et al. 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
  • 45
    • 0037351048 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer
    • Ryo A., et al. Prolyl isomerase Pin1: a catalyst for oncogenesis and a potential therapeutic target in cancer. J. Cell Sci. 2003, 116:773-783.
    • (2003) J. Cell Sci. , vol.116 , pp. 773-783
    • Ryo, A.1
  • 46
    • 2342526543 scopus 로고    scopus 로고
    • A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells
    • Yeh E., et al. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nat. Cell Biol. 2004, 6:308-318.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 308-318
    • Yeh, E.1
  • 47
    • 62049085035 scopus 로고    scopus 로고
    • The Axin1 scaffold protein promotes formation of a degradation complex for c-Myc
    • Arnold H.K., et al. The Axin1 scaffold protein promotes formation of a degradation complex for c-Myc. EMBO J. 2009, 28:500-512.
    • (2009) EMBO J. , vol.28 , pp. 500-512
    • Arnold, H.K.1
  • 48
    • 33644850537 scopus 로고    scopus 로고
    • The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability
    • Yeh E.S., et al. 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
  • 49
    • 33144488245 scopus 로고    scopus 로고
    • Function of retinoid nuclear receptors: lessons from genetic and pharmacological dissections of the retinoic acid signaling pathway during mouse embryogenesis
    • Mark M., et al. Function of retinoid nuclear receptors: lessons from genetic and pharmacological dissections of the retinoic acid signaling pathway during mouse embryogenesis. Annu. Rev. Pharmacol. Toxicol. 2006, 46:451-480.
    • (2006) Annu. Rev. Pharmacol. Toxicol. , vol.46 , pp. 451-480
    • Mark, M.1
  • 50
    • 59149091122 scopus 로고    scopus 로고
    • Inhibition of the peptidyl-prolyl-isomerase Pin1 enhances the responses of acute myeloid leukemia cells to retinoic acid via stabilization of RARα and PML-RARα
    • Gianni M., et al. Inhibition of the peptidyl-prolyl-isomerase Pin1 enhances the responses of acute myeloid leukemia cells to retinoic acid via stabilization of RARα and PML-RARα. Cancer Res. 2009, 69:1016-1026.
    • (2009) Cancer Res. , vol.69 , pp. 1016-1026
    • Gianni, M.1
  • 51
    • 12844275363 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates phospho-Ser retinoic acid receptor α stability
    • Brondani V., et al. The peptidyl-prolyl isomerase Pin1 regulates phospho-Ser retinoic acid receptor α stability. Biochem. Biophys. Res. Commun. 2005, 328:6-13.
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 6-13
    • Brondani, V.1
  • 52
    • 77951227828 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein controls cell migration in response to hydrogen peroxide and insulin-like growth factor-1
    • Reineke E.L., et al. Promyelocytic leukemia protein controls cell migration in response to hydrogen peroxide and insulin-like growth factor-1. J. Biol. Chem. 2010, 285:9485-9492.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9485-9492
    • Reineke, E.L.1
  • 53
    • 27144480681 scopus 로고    scopus 로고
    • 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)
    • 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. 2005, 25:9687-9699.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9687-9699
    • Yi, P.1
  • 54
    • 0242499448 scopus 로고    scopus 로고
    • Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
    • Siegel P.M., Massague J. Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer. Nat. Rev. Cancer 2003, 3:807-821.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 807-821
    • Siegel, P.M.1    Massague, J.2
  • 55
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation
    • Ebisawa T., et al. Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 2001, 276:12477-12480.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12477-12480
    • Ebisawa, T.1
  • 56
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation
    • Kavsak P., et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation. Mol. Cell 2000, 6:1365-1375.
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1
  • 57
    • 33846688094 scopus 로고    scopus 로고
    • Balancing BMP signaling through integrated inputs into the Smad1 linker
    • Sapkota G., et al. Balancing BMP signaling through integrated inputs into the Smad1 linker. Mol. Cell 2007, 25:441-454.
    • (2007) Mol. Cell , vol.25 , pp. 441-454
    • Sapkota, G.1
  • 58
    • 65249175171 scopus 로고    scopus 로고
    • Pin1 down-regulates transforming growth factor-β (TGF-β) signaling by inducing degradation of Smad proteins
    • Nakano A., et al. Pin1 down-regulates transforming growth factor-β (TGF-β) signaling by inducing degradation of Smad proteins. J. Biol. Chem. 2009, 284:6109-6115.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6109-6115
    • Nakano, A.1
  • 59
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg E.A. Mitotic kinases as regulators of cell division and its checkpoints. Nat. Rev. Mol. Cell Biol. 2001, 2:21-32.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 60
    • 19344363250 scopus 로고    scopus 로고
    • Pathophysiological roles of G-protein-coupled receptor kinases
    • Metaye T., et al. Pathophysiological roles of G-protein-coupled receptor kinases. Cell. Signal. 2005, 17:917-928.
    • (2005) Cell. Signal. , vol.17 , pp. 917-928
    • Metaye, T.1
  • 61
    • 47849125977 scopus 로고    scopus 로고
    • Immunohistochemical detection, regulation and antiproliferative function of G-protein-coupled receptor kinase 2 in thyroid carcinomas
    • Metaye T., et al. Immunohistochemical detection, regulation and antiproliferative function of G-protein-coupled receptor kinase 2 in thyroid carcinomas. J. Endocrinol. 2008, 198:101-110.
    • (2008) J. Endocrinol. , vol.198 , pp. 101-110
    • Metaye, T.1
  • 62
    • 0033869812 scopus 로고    scopus 로고
    • Overexpression of G protein-coupled receptor kinase-2 in smooth muscle cells attenuates mitogenic signaling via G protein-coupled and platelet-derived growth factor receptors
    • Peppel K., et al. Overexpression of G protein-coupled receptor kinase-2 in smooth muscle cells attenuates mitogenic signaling via G protein-coupled and platelet-derived growth factor receptors. Circulation 2000, 102:793-799.
    • (2000) Circulation , vol.102 , pp. 793-799
    • Peppel, K.1
  • 63
    • 75749118972 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 2 (GRK2) modulation and cell cycle progression
    • Penela P., et al. G protein-coupled receptor kinase 2 (GRK2) modulation and cell cycle progression. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:1118-1123.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1118-1123
    • Penela, P.1
  • 64
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 65
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 66
    • 0034940160 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies
    • Lee V.M., et al. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 2001, 24:1121-1159.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1121-1159
    • Lee, V.M.1
  • 67
    • 0345602771 scopus 로고    scopus 로고
    • Amyloid β protein toxicity mediated by the formation of amyloid-β protein precursor complexes
    • Lu D.C., et al. Amyloid β protein toxicity mediated by the formation of amyloid-β protein precursor complexes. Ann. Neurol. 2003, 54:781-789.
    • (2003) Ann. Neurol. , vol.54 , pp. 781-789
    • Lu, D.C.1
  • 68
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
    • Pastorino L., et al. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production. Nature 2006, 440:528-534.
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1
  • 69
    • 33646511135 scopus 로고    scopus 로고
    • Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: a redox proteomics analysis
    • Sultana R., et al. Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: a redox proteomics analysis. Neurobiol. Aging 2006, 27:918-925.
    • (2006) Neurobiol. Aging , vol.27 , pp. 918-925
    • Sultana, R.1
  • 70
    • 43049143027 scopus 로고    scopus 로고
    • Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy
    • Lim J., et al. Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy. J. Clin. Invest. 2008, 118:1877-1889.
    • (2008) J. Clin. Invest. , vol.118 , pp. 1877-1889
    • Lim, J.1
  • 71
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein
    • Lotharius J., Brundin P. Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein. Nat. Rev. Neurosci. 2002, 3:932-942.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 72
    • 33645238274 scopus 로고    scopus 로고
    • Prolyl-isomerase Pin1 accumulates in lewy bodies of parkinson disease and facilitates formation of α-synuclein inclusions
    • Ryo A. Prolyl-isomerase Pin1 accumulates in lewy bodies of parkinson disease and facilitates formation of α-synuclein inclusions. J. Biol. Chem. 2006, 281:4117-4125.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4117-4125
    • Ryo, A.1
  • 73
    • 0035929353 scopus 로고    scopus 로고
    • Switching and signaling at the telomere
    • Blackburn E.H. Switching and signaling at the telomere. Cell 2001, 106:661-673.
    • (2001) Cell , vol.106 , pp. 661-673
    • Blackburn, E.H.1
  • 74
    • 34548667973 scopus 로고    scopus 로고
    • Telomere length, stem cells and aging
    • Blasco M.A. Telomere length, stem cells and aging. Nat. Chem. Biol. 2007, 3:640-649.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 640-649
    • Blasco, M.A.1
  • 75
    • 0029586089 scopus 로고
    • A human telomeric protein
    • Chong L., et al. A human telomeric protein. Science 1995, 270:1663-1667.
    • (1995) Science , vol.270 , pp. 1663-1667
    • Chong, L.1
  • 76
    • 0033961281 scopus 로고    scopus 로고
    • Control of human telomere length by TRF1 and TRF2
    • Smogorzewska A., et al. Control of human telomere length by TRF1 and TRF2. Mol. Cell. Biol. 2000, 20:1659-1668.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1659-1668
    • Smogorzewska, A.1
  • 77
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel B., de Lange T. Control of telomere length by the human telomeric protein TRF1. Nature 1997, 385:740-743.
    • (1997) Nature , vol.385 , pp. 740-743
    • van Steensel, B.1    de Lange, T.2
  • 78
    • 0031443638 scopus 로고    scopus 로고
    • Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis
    • Shen M., et al. Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:13618-13623.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13618-13623
    • Shen, M.1
  • 79
    • 58149351370 scopus 로고    scopus 로고
    • Essential role of Pin1 in the regulation of TRF1 stability and telomere maintenance
    • Lee T.H., et al. Essential role of Pin1 in the regulation of TRF1 stability and telomere maintenance. Nat. Cell Biol. 2009, 11:97-105.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 97-105
    • Lee, T.H.1
  • 80
    • 0037213048 scopus 로고    scopus 로고
    • Telomere shortening in T cells correlates with Alzheimer's disease status
    • Panossian L.A., et al. Telomere shortening in T cells correlates with Alzheimer's disease status. Neurobiol. Aging 2003, 24:77-84.
    • (2003) Neurobiol. Aging , vol.24 , pp. 77-84
    • Panossian, L.A.1
  • 81
    • 34547132819 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 affects Che-1 stability in response to apoptotic DNA damage
    • De Nicola F., et al. The prolyl isomerase Pin1 affects Che-1 stability in response to apoptotic DNA damage. J. Biol. Chem. 2007, 282:19685-19691.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19685-19691
    • De Nicola, F.1
  • 82
    • 2942547565 scopus 로고    scopus 로고
    • Pin1 links the activities of c-Abl and p300 in regulating p73 function
    • Mantovani F., et al. Pin1 links the activities of c-Abl and p300 in regulating p73 function. Mol. Cell 2004, 14:625-636.
    • (2004) Mol. Cell , vol.14 , pp. 625-636
    • Mantovani, F.1
  • 83
    • 63149174264 scopus 로고    scopus 로고
    • Peptidylproline cis-trans-isomerase Pin1 interacts with human T-cell leukemia virus type 1 tax and modulates its activation of NF-κB
    • Peloponese J.M., et al. Peptidylproline cis-trans-isomerase Pin1 interacts with human T-cell leukemia virus type 1 tax and modulates its activation of NF-κB. J. Virol. 2009, 83:3238-3248.
    • (2009) J. Virol. , vol.83 , pp. 3238-3248
    • Peloponese, J.M.1
  • 84
    • 25844441096 scopus 로고    scopus 로고
    • Skp2 ubiquitin ligase
    • Skp2 ubiquitin ligase. Mol. Cell 2005, 20:9-19.
    • (2005) Mol. Cell , vol.20 , pp. 9-19
    • Hao, B.1
  • 85
    • 69949134410 scopus 로고    scopus 로고
    • Pin1 catalyzes conformational changes of Thr-187 in p27Kip1 and mediates its stability through a polyubiquitination process
    • Zhou W., et al. Pin1 catalyzes conformational changes of Thr-187 in p27Kip1 and mediates its stability through a polyubiquitination process. J. Biol. Chem. 2009, 284:23980-23988.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23980-23988
    • Zhou, W.1
  • 86
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T., Karin M. The regulation of transcription by phosphorylation. Cell 1992, 70:375-387.
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 87
    • 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
  • 88
    • 0029983519 scopus 로고    scopus 로고
    • Cellular signaling pathways and cytoskeletal organization
    • Kosik K.S., et al. Cellular signaling pathways and cytoskeletal organization. Ann. N. Y. Acad. Sci. 1996, 777:114-120.
    • (1996) Ann. N. Y. Acad. Sci. , vol.777 , pp. 114-120
    • Kosik, K.S.1
  • 89
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini M.G., Goedert M. Tau protein pathology in neurodegenerative diseases. Trends Neurosci. 1998, 21:428-433.
    • (1998) Trends Neurosci. , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 90
    • 0344625369 scopus 로고    scopus 로고
    • Characterization of the phosphorylation sites of human high molecular weight neurofilament protein by electrospray ionization tandem mass spectrometry and database searching
    • Jaffe H., et al. Characterization of the phosphorylation sites of human high molecular weight neurofilament protein by electrospray ionization tandem mass spectrometry and database searching. Biochemistry 1998, 37:3931-3940.
    • (1998) Biochemistry , vol.37 , pp. 3931-3940
    • Jaffe, H.1
  • 91
    • 0029022205 scopus 로고
    • Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A
    • Veeranna K.T., et al. Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A. J. Neurochem. 1995, 64:2681-2690.
    • (1995) J. Neurochem. , vol.64 , pp. 2681-2690
    • Veeranna, K.T.1
  • 92
    • 72449200109 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins
    • Rudrabhatla P., et al. Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins. J. Neurosci. 2009, 29:14869-14880.
    • (2009) J. Neurosci. , vol.29 , pp. 14869-14880
    • Rudrabhatla, P.1
  • 93
    • 19944430124 scopus 로고    scopus 로고
    • Regulation of Raf-1 by direct feedback phosphorylation
    • Dougherty M.K., et al. Regulation of Raf-1 by direct feedback phosphorylation. Mol. Cell 2005, 17:215-224.
    • (2005) Mol. Cell , vol.17 , pp. 215-224
    • Dougherty, M.K.1
  • 94
    • 0344011538 scopus 로고    scopus 로고
    • Pin1 modulates the structure and function of human RNA polymerase II
    • Xu Y.X., et al. Pin1 modulates the structure and function of human RNA polymerase II. Genes Dev. 2003, 17:2765-2776.
    • (2003) Genes Dev. , vol.17 , pp. 2765-2776
    • Xu, Y.X.1
  • 95
    • 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
  • 96
    • 70350028604 scopus 로고    scopus 로고
    • A novel functional variant (-842G>C) in the PIN1 promoter contributes to decreased risk of squamous cell carcinoma of the head and neck by diminishing the promoter activity
    • Lu J., et al. A novel functional variant (-842G>C) in the PIN1 promoter contributes to decreased risk of squamous cell carcinoma of the head and neck by diminishing the promoter activity. Carcinogenesis 2009, 30:1717-1721.
    • (2009) Carcinogenesis , vol.30 , pp. 1717-1721
    • Lu, J.1
  • 97
    • 33751327516 scopus 로고    scopus 로고
    • PIN1 promoter polymorphisms are associated with Alzheimer's disease
    • Segat L., et al. PIN1 promoter polymorphisms are associated with Alzheimer's disease. Neurobiol. Aging 2007, 28:69-74.
    • (2007) Neurobiol. Aging , vol.28 , pp. 69-74
    • Segat, L.1
  • 98
    • 80053292119 scopus 로고    scopus 로고
    • A PIN1 polymorphism that prevents its suppression by AP4 associates with delayed onset of Alzheimer's disease
    • Ma S.L., et al. A PIN1 polymorphism that prevents its suppression by AP4 associates with delayed onset of Alzheimer's disease. Neurobiol. Aging 2010, 10.1016/j.physletb.2003.10.071.
    • (2010) Neurobiol. Aging
    • Ma, S.L.1
  • 99
    • 1842763560 scopus 로고    scopus 로고
    • Pinning down cell signaling, cancer and Alzheimer's disease
    • Lu K.P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 2004, 29:200-209.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 200-209
    • Lu, K.P.1
  • 100
    • 27744536481 scopus 로고    scopus 로고
    • Polo-like kinase 1-mediated phosphorylation stabilizes Pin1 by inhibiting its ubiquitination in human cells
    • Eckerdt F. Polo-like kinase 1-mediated phosphorylation stabilizes Pin1 by inhibiting its ubiquitination in human cells. J. Biol. Chem. 2005, 280:36575-36583.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36575-36583
    • Eckerdt, F.1
  • 101
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: structure, function, and beyond
    • Bialik S., Kimchi A. The death-associated protein kinases: structure, function, and beyond. Annu. Rev. Biochem. 2006, 75:189-210.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 102
    • 0035141040 scopus 로고    scopus 로고
    • ARF/p53-mediated apoptotic checkpoint to suppress oncogenic transformation
    • ARF/p53-mediated apoptotic checkpoint to suppress oncogenic transformation. Nat. Cell Biol. 2001, 3:1-7.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1-7
    • Raveh, T.1
  • 103
    • 77951184824 scopus 로고    scopus 로고
    • Active Mek2 as a regulatory scaffold that promotes Pin1 binding to BPGAP1 to suppress BPGAP1-induced acute Erk activation and cell migration
    • Pan C.Q., et al. Active Mek2 as a regulatory scaffold that promotes Pin1 binding to BPGAP1 to suppress BPGAP1-induced acute Erk activation and cell migration. J. Cell Sci. 2010, 123:903-916.
    • (2010) J. Cell Sci. , vol.123 , pp. 903-916
    • Pan, C.Q.1
  • 104
    • 44449109478 scopus 로고    scopus 로고
    • Trophoblastic p53 is stabilised by a cis-trans isomerisation necessary for the formation of high molecular weight complexes involving the N-terminus of p53
    • Cohen M., et al. Trophoblastic p53 is stabilised by a cis-trans isomerisation necessary for the formation of high molecular weight complexes involving the N-terminus of p53. Biochimie 2008, 90:855-862.
    • (2008) Biochimie , vol.90 , pp. 855-862
    • Cohen, M.1
  • 105
    • 68249119759 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation
    • Siepe D., Jentsch S. Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Nat. Cell Biol. 2009, 11:967-972.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 967-972
    • Siepe, D.1    Jentsch, S.2
  • 106
    • 34547700604 scopus 로고    scopus 로고
    • Opposite regulation of oligodendrocyte apoptosis by JNK3 and Pin1 after spinal cord injury
    • Li Q.M., et al. Opposite regulation of oligodendrocyte apoptosis by JNK3 and Pin1 after spinal cord injury. J. Neurosci. 2007, 27:8395-8404.
    • (2007) J. Neurosci. , vol.27 , pp. 8395-8404
    • Li, Q.M.1
  • 107
    • 77955834772 scopus 로고    scopus 로고
    • Phosphorylation stabilizes Nanog by promoting its interaction with Pin1
    • Moretto-Zita M., et al. Phosphorylation stabilizes Nanog by promoting its interaction with Pin1. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:13312-13317.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13312-13317
    • Moretto-Zita, M.1
  • 108
    • 79953193459 scopus 로고    scopus 로고
    • A distinct role for Pin1 in the induction and maintenance of pluripotency
    • Nishi M., et al. A distinct role for Pin1 in the induction and maintenance of pluripotency. J. Biol. Chem. 2011, 286:11593-11603.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11593-11603
    • Nishi, M.1
  • 109
    • 61849086777 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 stabilizes the human T-cell leukemia virus type 1 (HTLV-1) Tax oncoprotein and promotes malignant transformation
    • Jeong S.J., et al. The prolyl isomerase Pin1 stabilizes the human T-cell leukemia virus type 1 (HTLV-1) Tax oncoprotein and promotes malignant transformation. Biochem. Biophys. Res. Commun. 2009, 381:294-299.
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 294-299
    • Jeong, S.J.1
  • 110
    • 77949264933 scopus 로고    scopus 로고
    • Concerted action of cellular JNK and Pin1 restricts HIV-1 genome integration to activated CD4+ T lymphocytes
    • Manganaro L., et al. Concerted action of cellular JNK and Pin1 restricts HIV-1 genome integration to activated CD4+ T lymphocytes. Nat. Med. 2010, 16:329-333.
    • (2010) Nat. Med. , vol.16 , pp. 329-333
    • Manganaro, L.1
  • 111
    • 33947303068 scopus 로고    scopus 로고
    • Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis
    • Pang R., et al. Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis. Gastroenterology 2007, 132:1088-1103.
    • (2007) Gastroenterology , vol.132 , pp. 1088-1103
    • Pang, R.1
  • 112
    • 27444440554 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1
    • Monje P., et al. Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1. J. Biol. Chem. 2005, 280:35081-35084.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35081-35084
    • Monje, P.1
  • 113
    • 22544461011 scopus 로고    scopus 로고
    • Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint
    • Campaner S., et al. Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint. Mol. Cell. Biol. 2005, 25:6660-6672.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6660-6672
    • Campaner, S.1
  • 114
    • 13444259420 scopus 로고    scopus 로고
    • The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1
    • Proteau A., et al. The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. J. Mol. Biol. 2005, 346:1163-1172.
    • (2005) J. Mol. Biol. , vol.346 , pp. 1163-1172
    • Proteau, A.1
  • 115
    • 33750801024 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes
    • Esnault S., et al. The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes. J. Immunol. 2006, 177:6999-7006.
    • (2006) J. Immunol. , vol.177 , pp. 6999-7006
    • Esnault, S.1
  • 116
    • 5444234359 scopus 로고    scopus 로고
    • EL signaling pathway in neuronal apoptosis
    • EL signaling pathway in neuronal apoptosis. J. Neurosci. 2004, 24:8762-8770.
    • (2004) J. Neurosci. , vol.24 , pp. 8762-8770
    • Becker, E.B.1
  • 117
    • 41649088278 scopus 로고    scopus 로고
    • A topoisomerase II-dependent mechanism for resetting replicons at the S-M-phase transition
    • Cuvier O., et al. A topoisomerase II-dependent mechanism for resetting replicons at the S-M-phase transition. Genes Dev. 2008, 22:860-865.
    • (2008) Genes Dev. , vol.22 , pp. 860-865
    • Cuvier, O.1
  • 118
    • 0036097027 scopus 로고    scopus 로고
    • Proteasomal degradation of human peptidyl prolyl isomerase pin1-pointing phospho Bcl2 toward dephosphorylation
    • Basu A., et al. Proteasomal degradation of human peptidyl prolyl isomerase pin1-pointing phospho Bcl2 toward dephosphorylation. Neoplasia 2002, 4:218-227.
    • (2002) Neoplasia , vol.4 , pp. 218-227
    • Basu, A.1
  • 119
    • 0035524625 scopus 로고    scopus 로고
    • Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1
    • Pathan N., et al. Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1. Neoplasia 2001, 3:550-559.
    • (2001) Neoplasia , vol.3 , pp. 550-559
    • Pathan, N.1
  • 120
    • 61349151785 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 is highly expressed in Her2-positive breast cancer and regulates erbB2 protein stability
    • Lam P.B., et al. Prolyl isomerase Pin1 is highly expressed in Her2-positive breast cancer and regulates erbB2 protein stability. Mol. Cancer 2008, 7:91.
    • (2008) Mol. Cancer , vol.7 , pp. 91
    • Lam, P.B.1
  • 121
    • 77449115522 scopus 로고    scopus 로고
    • Proline cis/trans-isomerase Pin1 regulates peroxisome proliferator-activated receptor γ activity through the direct binding to the activation function-1 domain
    • Fujimoto Y., et al. Proline cis/trans-isomerase Pin1 regulates peroxisome proliferator-activated receptor γ activity through the direct binding to the activation function-1 domain. J. Biol. Chem. 2010, 285:3126-3132.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3126-3132
    • Fujimoto, Y.1
  • 122
    • 69249087271 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55
    • van der Horst A., Khanna K.K. The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55. Cancer Res. 2009, 69:6651-6659.
    • (2009) Cancer Res. , vol.69 , pp. 6651-6659
    • van der Horst, A.1    Khanna, K.K.2
  • 123
    • 67650092976 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation
    • Liao Y., et al. Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation. Oncogene 2009, 28:2436-2445.
    • (2009) Oncogene , vol.28 , pp. 2436-2445
    • Liao, Y.1
  • 124
    • 74049131292 scopus 로고    scopus 로고
    • Pin1At encoding a peptidyl-prolyl cis/trans isomerase regulates flowering time in Arabidopsis
    • Wang Y., et al. Pin1At encoding a peptidyl-prolyl cis/trans isomerase regulates flowering time in Arabidopsis. Mol. Cell 2010, 37:112-122.
    • (2010) Mol. Cell , vol.37 , pp. 112-122
    • Wang, Y.1
  • 125
    • 33745830461 scopus 로고    scopus 로고
    • Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1
    • Yu L., et al. Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1. J. Biol. Chem. 2006, 281:18201-18207.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18201-18207
    • Yu, L.1
  • 126
    • 33744499683 scopus 로고    scopus 로고
    • Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1
    • Saitoh T., et al. Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1. Nat. Immunol. 2006, 7:598-605.
    • (2006) Nat. Immunol. , vol.7 , pp. 598-605
    • Saitoh, T.1
  • 127
    • 53749085961 scopus 로고    scopus 로고
    • Cdk2 and Pin1 negatively regulate the transcriptional corepressor SMRT
    • Stanya K.J., et al. 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
  • 128
    • 34547642807 scopus 로고    scopus 로고
    • Negative regulation of Pim-1 protein kinase levels by the B56β subunit of PP2A
    • Ma J., et al. Negative regulation of Pim-1 protein kinase levels by the B56β subunit of PP2A. Oncogene 2007, 26:5145-5153.
    • (2007) Oncogene , vol.26 , pp. 5145-5153
    • Ma, J.1
  • 129
    • 54749134224 scopus 로고    scopus 로고
    • kip1 expression through inhibition of Forkhead box O tumor suppressors
    • kip1 expression through inhibition of Forkhead box O tumor suppressors. Cancer Res. 2008, 68:7597-7605.
    • (2008) Cancer Res. , vol.68 , pp. 7597-7605
    • Brenkman, A.B.1
  • 130
    • 75149185157 scopus 로고    scopus 로고
    • Pin1 facilitates the phosphorylation-dependent ubiquitination of SF-1 to regulate gonadotropin β-subunit gene transcription
    • Luo Z., et al. Pin1 facilitates the phosphorylation-dependent ubiquitination of SF-1 to regulate gonadotropin β-subunit gene transcription. Mol. Cell. Biol. 2010, 30:745-763.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 745-763
    • Luo, Z.1
  • 131
    • 78650743362 scopus 로고    scopus 로고
    • Phosphorylation/dephosphorylation of human SULT4A1: role of Erk1 and PP2A
    • Mitchell D.J., et al. Phosphorylation/dephosphorylation of human SULT4A1: role of Erk1 and PP2A. Biochim. Biophys. Acta 2011, 1813:231-237.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 231-237
    • Mitchell, D.J.1
  • 132
    • 67650824974 scopus 로고    scopus 로고
    • Cytosolic aryl sulfotransferase 4A1 interacts with the peptidyl prolyl cis-trans isomerase Pin1
    • Mitchell D.J., Minchin R.F. Cytosolic aryl sulfotransferase 4A1 interacts with the peptidyl prolyl cis-trans isomerase Pin1. Mol. Pharmacol. 2009, 76:388-395.
    • (2009) Mol. Pharmacol. , vol.76 , pp. 388-395
    • Mitchell, D.J.1    Minchin, R.F.2
  • 133
    • 78049397634 scopus 로고    scopus 로고
    • Proline isomerase Pin1 represses terminal differentiation and myocyte enhancer factor 2C function in skeletal muscle cells
    • Magli A., et al. Proline isomerase Pin1 represses terminal differentiation and myocyte enhancer factor 2C function in skeletal muscle cells. J. Biol. Chem. 2010, 285:34518-34527.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34518-34527
    • Magli, A.1
  • 134
    • 37549031354 scopus 로고    scopus 로고
    • A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx
    • Ryo A., et al. A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx. J. Biol. Chem. 2007, 282:36671-36681.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36671-36681
    • Ryo, A.1
  • 135
    • 33745095542 scopus 로고    scopus 로고
    • Pin1 allows for differential Tau dephosphorylation in neuronal cells
    • Hamdane M., et al. Pin1 allows for differential Tau dephosphorylation in neuronal cells. Mol. Cell. Neurosci. 2006, 32:155-160.
    • (2006) Mol. Cell. Neurosci. , vol.32 , pp. 155-160
    • Hamdane, M.1
  • 136
    • 37849032065 scopus 로고    scopus 로고
    • Binding of phosphatase inhibitor-2 to prolyl isomerase Pin1 modifies specificity for mitotic phosphoproteins
    • Li M., et al. Binding of phosphatase inhibitor-2 to prolyl isomerase Pin1 modifies specificity for mitotic phosphoproteins. Biochemistry 2008, 47:292-300.
    • (2008) Biochemistry , vol.47 , pp. 292-300
    • Li, M.1
  • 137
    • 38849085399 scopus 로고    scopus 로고
    • Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis
    • Shen Z.J., et al. Pin1 regulates TGF-β1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis. J. Clin. Invest. 2008, 118:479-490.
    • (2008) J. Clin. Invest. , vol.118 , pp. 479-490
    • Shen, Z.J.1
  • 138
    • 70349673290 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 determines parathyroid hormone mRNA levels and stability in rat models of secondary hyperparathyroidism
    • Nechama M., et al. The peptidyl-prolyl isomerase Pin1 determines parathyroid hormone mRNA levels and stability in rat models of secondary hyperparathyroidism. J. Clin. Invest. 2009, 119:3102-3114.
    • (2009) J. Clin. Invest. , vol.119 , pp. 3102-3114
    • Nechama, M.1
  • 139
    • 20744432450 scopus 로고    scopus 로고
    • Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage
    • Berger M., et al. Mutations in proline 82 of p53 impair its activation by Pin1 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
  • 140
    • 34249948703 scopus 로고    scopus 로고
    • Ablation of a peptidyl prolyl isomerase Pin1 from p53-null mice accelerated thymic hyperplasia by increasing the level of the intracellular form of Notch1
    • Takahashi K., et al. Ablation of a peptidyl prolyl isomerase Pin1 from p53-null mice accelerated thymic hyperplasia by increasing the level of the intracellular form of Notch1. Oncogene 2007, 26:3835-3845.
    • (2007) Oncogene , vol.26 , pp. 3835-3845
    • Takahashi, K.1
  • 141
    • 33846925252 scopus 로고    scopus 로고
    • Mouse mutants reveal that putative protein interaction sites in the p53 proline-rich domain are dispensable for tumor suppression
    • Toledo F., et al. Mouse mutants reveal that putative protein interaction sites in the p53 proline-rich domain are dispensable for tumor suppression. Mol. Cell. Biol. 2007, 27:1425-1432.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1425-1432
    • Toledo, F.1
  • 142
    • 36248966518 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from adult human fibroblasts by defined factors
    • Takahashi K., et al. Induction of pluripotent stem cells from adult human fibroblasts by defined factors. Cell 2007, 131:861-872.
    • (2007) Cell , vol.131 , pp. 861-872
    • Takahashi, K.1
  • 143
    • 33747195353 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors
    • Takahashi K., Yamanaka S. Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell 2006, 126:663-676.
    • (2006) Cell , vol.126 , pp. 663-676
    • Takahashi, K.1    Yamanaka, S.2
  • 144
    • 0038143611 scopus 로고    scopus 로고
    • Functional expression cloning of Nanog, a pluripotency sustaining factor in embryonic stem cells
    • Chambers I., et al. Functional expression cloning of Nanog, a pluripotency sustaining factor in embryonic stem cells. Cell 2003, 113:643-655.
    • (2003) Cell , vol.113 , pp. 643-655
    • Chambers, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.