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Volumn 29, Issue 1, 2010, Pages 207-222

P66Shc- A longevity redox protein in human prostate cancer progression and metastasis: P66Shc in cancer progression and metastasis

Author keywords

Apoptosis; Cell proliferation; Metastasis; P66Shc; Prostate cancer; Redox

Indexed keywords

ADAPTOR PROTEIN; ANDROGEN; BIOLOGICAL MARKER; INTEGRIN; P66SHC PROTEIN; PROTEIN P53; SERINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 77349100142     PISSN: 01677659     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10555-010-9213-8     Document Type: Review
Times cited : (41)

References (156)
  • 2
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • 11357141
    • GI Evan KH Vousden 2001 Proliferation, cell cycle and apoptosis in cancer Nature 411 342 348 11357141
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.I.1    Vousden, K.H.2
  • 3
    • 0033009890 scopus 로고    scopus 로고
    • The central effectors of cell death in the immune system
    • 10358774
    • JC Rathmell CB Thompson 1999 The central effectors of cell death in the immune system Annual Review of Immunology 17 781 828 10358774
    • (1999) Annual Review of Immunology , vol.17 , pp. 781-828
    • Rathmell, J.C.1    Thompson, C.B.2
  • 5
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • 10444588
    • A Gross JM McDonnell SJ Korsmeyer 1999 BCL-2 family members and the mitochondria in apoptosis Genes and Development 13 1899 1911 10444588
    • (1999) Genes and Development , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 6
    • 0036179645 scopus 로고    scopus 로고
    • Death receptors couple to both cell proliferation and apoptosis
    • 11854313
    • RC Budd 2002 Death receptors couple to both cell proliferation and apoptosis Journal of Clinical Investigation 109 437 441 11854313
    • (2002) Journal of Clinical Investigation , vol.109 , pp. 437-441
    • Budd, R.C.1
  • 7
    • 0026777369 scopus 로고
    • A novel transforming protein [SHC] with an SH2 domain is implicated in mitogenic signal transduction
    • 1623525
    • G Pelicci L Lanfrancone F Grignani J McGlade F Cavallo G Forni, et al. 1992 A novel transforming protein [SHC] with an SH2 domain is implicated in mitogenic signal transduction Cell 70 93 104 1623525
    • (1992) Cell , vol.70 , pp. 93-104
    • Pelicci, G.1    Lanfrancone, L.2    Grignani, F.3    McGlade, J.4    Cavallo, F.5    Forni, G.6
  • 8
    • 0031056755 scopus 로고    scopus 로고
    • Opposite effects of the p52Shc/p46Shc and p66Shc splicing isoforms on the EGF receptor- MAP kinase-fos signaling pathway
    • 9049300
    • E Migliaccio S Mele AE Salcini G Pelicci KM Lai G Superti-Furga, et al. 1997 Opposite effects of the p52Shc/p46Shc and p66Shc splicing isoforms on the EGF receptor- MAP kinase-fos signaling pathway The EMBO Journal 16 706 716 9049300
    • (1997) The EMBO Journal , vol.16 , pp. 706-716
    • Migliaccio, E.1    Mele, S.2    Salcini, A.E.3    Pelicci, G.4    Lai, K.M.5    Superti-Furga, G.6
  • 9
    • 0035474473 scopus 로고    scopus 로고
    • Signaling via Shc family adapter proteins
    • 11607835
    • KS Ravichandran 2001 Signaling via Shc family adapter proteins Oncogene 20 6322 6330 11607835
    • (2001) Oncogene , vol.20 , pp. 6322-6330
    • Ravichandran, K.S.1
  • 10
    • 0346024127 scopus 로고    scopus 로고
    • P66Shc protein is upregulated by steroid hormones in hormone-sensitive cancer cells and in primary prostate carcinomas
    • MS Lee T Igawa SJ Chen D Van Bemmel JS Lin FF Lin, et al. 2004 p66Shc protein is upregulated by steroid hormones in hormone-sensitive cancer cells and in primary prostate carcinomas International Journal of Cancer 108 672 678
    • (2004) International Journal of Cancer , vol.108 , pp. 672-678
    • Lee, M.S.1    Igawa, T.2    Chen, S.J.3    Van Bemmel, D.4    Lin, J.S.5    Lin, F.F.6
  • 13
    • 0034682240 scopus 로고    scopus 로고
    • Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells
    • 10851066
    • TC Meng MS Lee MF Lin 2000 Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells Oncogene 19 2664 2677 10851066
    • (2000) Oncogene , vol.19 , pp. 2664-2677
    • Meng, T.C.1    Lee, M.S.2    Lin, M.F.3
  • 15
    • 33845298019 scopus 로고    scopus 로고
    • Receptor for activated C kinase 1 [RACK1] and Src regulate the tyrosine phosphorylation and function of the androgen receptor
    • 17108144
    • S Kraus D Gioeli T Vomastek V Gordon MJ Weber 2006 Receptor for activated C kinase 1 [RACK1] and Src regulate the tyrosine phosphorylation and function of the androgen receptor Cancer Research 66 11047 11054 17108144
    • (2006) Cancer Research , vol.66 , pp. 11047-11054
    • Kraus, S.1    Gioeli, D.2    Vomastek, T.3    Gordon, V.4    Weber, M.J.5
  • 16
    • 33749445413 scopus 로고    scopus 로고
    • Regulation of androgen receptor activity by tyrosine Phosphorylation
    • 17045208
    • Z Guo B Dai T Jiang K Xu Y Xie O Kim 2006 Regulation of androgen receptor activity by tyrosine Phosphorylation Cancer Cell 10 309 319 17045208
    • (2006) Cancer Cell , vol.10 , pp. 309-319
    • Guo, Z.1    Dai, B.2    Jiang, T.3    Xu, K.4    Xie, Y.5    Kim, O.6
  • 17
    • 34250690433 scopus 로고    scopus 로고
    • Kinases and protein phosphorylation as regulators of steroid hormone action
    • 17525795
    • NL Weigel NL Moore 2007 Kinases and protein phosphorylation as regulators of steroid hormone action Nuclear Receptor Signaling 5 e005 17525795
    • (2007) Nuclear Receptor Signaling , vol.5 , pp. 005
    • Weigel, N.L.1    Moore, N.L.2
  • 18
    • 0023284318 scopus 로고
    • Estrogenic regulation of growth and polypeptide growth factor secretion in human breast carcinoma
    • 3549276
    • RB Dickson ME Lippman 1987 Estrogenic regulation of growth and polypeptide growth factor secretion in human breast carcinoma Endocrine Reviews 8 29 43 3549276
    • (1987) Endocrine Reviews , vol.8 , pp. 29-43
    • Dickson, R.B.1    Lippman, M.E.2
  • 19
    • 0031006005 scopus 로고    scopus 로고
    • Variability of glutathione levels in normal breast tissue and subcutaneous fat during the menstrual cycle: An in vivo study with microdialysis technique
    • 9141520
    • C Dabrosin K Ollinger U Ungerstedt M Hammar 1997 Variability of glutathione levels in normal breast tissue and subcutaneous fat during the menstrual cycle: an in vivo study with microdialysis technique Journal of Clinical Endocrinology and Metabolism 82 1382 1384 9141520
    • (1997) Journal of Clinical Endocrinology and Metabolism , vol.82 , pp. 1382-1384
    • Dabrosin, C.1    Ollinger, K.2    Ungerstedt, U.3    Hammar, M.4
  • 20
    • 0034811660 scopus 로고    scopus 로고
    • Catechol estrogen metabolites and conjugates in mammary tumors and hyperplastic tissue from estrogen receptor-alpha knock-out [ERKO]/Wnt-1 mice: Implications for initiation of mammary tumors
    • 11532882
    • P Devanesan RJ Santen WP Bocchinfuso KS Korach EG Rogan E Cavalieri 2001 Catechol estrogen metabolites and conjugates in mammary tumors and hyperplastic tissue from estrogen receptor-alpha knock-out [ERKO]/Wnt-1 mice: Implications for initiation of mammary tumors Carcinogenesis 22 1573 1576 11532882
    • (2001) Carcinogenesis , vol.22 , pp. 1573-1576
    • Devanesan, P.1    Santen, R.J.2    Bocchinfuso, W.P.3    Korach, K.S.4    Rogan, E.G.5    Cavalieri, E.6
  • 21
    • 0027530832 scopus 로고
    • Effects of EGF, bFGF, NGF, and PDGF [bb] on cell proliferative, migratory, and invasive capacities of human brain-tumour biopsies in vitro
    • O Engebraaten R Bjerkvig PH Pedersen OD Laerum 1993 Effects of EGF, bFGF, NGF, and PDGF [bb] on cell proliferative, migratory, and invasive capacities of human brain-tumour biopsies in vitro International Journal of Cancer 53 209 214
    • (1993) International Journal of Cancer , vol.53 , pp. 209-214
    • Engebraaten, O.1    Bjerkvig, R.2    Pedersen, P.H.3    Laerum, O.D.4
  • 22
    • 0028965013 scopus 로고
    • Enhanced effect of epidermal growth factor on pulmonary metastasis and in vitro invasion of rat mammary carcinoma cells
    • 7889524
    • J Hamada H Nagayasu M Takayama T Kawano M Hosokawa N Takeichi 1995 Enhanced effect of epidermal growth factor on pulmonary metastasis and in vitro invasion of rat mammary carcinoma cells Cancer Letters 89 161 167 7889524
    • (1995) Cancer Letters , vol.89 , pp. 161-167
    • Hamada, J.1    Nagayasu, H.2    Takayama, M.3    Kawano, T.4    Hosokawa, M.5    Takeichi, N.6
  • 23
    • 0026351399 scopus 로고
    • Basic fibroblast growth factor released by single, isolated cells stimulates their migration in an autocrine manner
    • P Mignatti T Morimoto DB Rifkin 1991 Basic fibroblast growth factor released by single, isolated cells stimulates their migration in an autocrine manner Proceedings of National Academy of Sciences 88 11007 11011
    • (1991) Proceedings of National Academy of Sciences , vol.88 , pp. 11007-11011
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 24
    • 0027196857 scopus 로고
    • Cell motility, invasion, and malignancy induced by overexpression of K-FGF or bFGF
    • 8440326
    • WR Taylor AH Greenberg EA Turley JA Wright 1993 Cell motility, invasion, and malignancy induced by overexpression of K-FGF or bFGF Experimental cell research 204 295 301 8440326
    • (1993) Experimental Cell Research , vol.204 , pp. 295-301
    • Taylor, W.R.1    Greenberg, A.H.2    Turley, E.A.3    Wright, J.A.4
  • 28
    • 0029007694 scopus 로고
    • The motogenic and mitogenic responses to HGF are amplified by the Shc adaptor protein
    • 7731718
    • G Pelicci S Giordano Z Zhen AE Salcini L Lanfrancone A Bardelli, et al. 1995 The motogenic and mitogenic responses to HGF are amplified by the Shc adaptor protein Oncogene 10 1631 1638 7731718
    • (1995) Oncogene , vol.10 , pp. 1631-1638
    • Pelicci, G.1    Giordano, S.2    Zhen, Z.3    Salcini, A.E.4    Lanfrancone, L.5    Bardelli, A.6
  • 29
    • 0026777104 scopus 로고
    • Lymphocyte development of adherence and motility in extracellular matrix during IL-2 stimulation
    • 1385607
    • S Ratner P Patrick G Bora 1992 Lymphocyte development of adherence and motility in extracellular matrix during IL-2 stimulation The Journal of Immunology 149 681 688 1385607
    • (1992) The Journal of Immunology , vol.149 , pp. 681-688
    • Ratner, S.1    Patrick, P.2    Bora, G.3
  • 30
    • 0033581704 scopus 로고    scopus 로고
    • The p66shc adaptor protein controls oxidative stress response and life span in mammals
    • 10580504
    • E Migliaccio M Giorgio S Mele G Pelicci P Reboldi PP Pandolfi, et al. 1999 The p66shc adaptor protein controls oxidative stress response and life span in mammals Nature 402 309 313 10580504
    • (1999) Nature , vol.402 , pp. 309-313
    • Migliaccio, E.1    Giorgio, M.2    Mele, S.3    Pelicci, G.4    Reboldi, P.5    Pandolfi, P.P.6
  • 31
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • 8108730
    • WC Orr RS Sohal 1994 Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster Science 263 1128 1130 8108730
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 32
    • 0033551325 scopus 로고    scopus 로고
    • A cytosolic catalase is needed to extend adult lifespan in C. elegans daf-C and clk-1 mutants
    • 10335847
    • J Taub JF Lau C Ma JH Hahn R Hoque J Rothblatt, et al. 1999 A cytosolic catalase is needed to extend adult lifespan in C. elegans daf-C and clk-1 mutants Nature 399 162 166 10335847
    • (1999) Nature , vol.399 , pp. 162-166
    • Taub, J.1    Lau, J.F.2    Ma, C.3    Hahn, J.H.4    Hoque, R.5    Rothblatt, J.6
  • 34
    • 0034099236 scopus 로고    scopus 로고
    • Elevated levels of p66 Shc are found in breast cancer cell lines and primary tumors with high metastatic potential
    • 10741744
    • JG Jackson T Yoneda GM Clark D Yee 2000 Elevated levels of p66 Shc are found in breast cancer cell lines and primary tumors with high metastatic potential Clinical Cancer Research 6 1135 1139 10741744
    • (2000) Clinical Cancer Research , vol.6 , pp. 1135-1139
    • Jackson, J.G.1    Yoneda, T.2    Clark, G.M.3    Yee, D.4
  • 36
    • 0142219884 scopus 로고    scopus 로고
    • Shc proteins are strong, independent prognostic markers for both node negative and node positive primary breast cancer
    • 14583473
    • PA Davol R Bagdasaryan GJ Elfenbein AL Maizel AR Frackelton Jr 2003 Shc proteins are strong, independent prognostic markers for both node negative and node positive primary breast cancer Cancer Research 63 6772 6783 14583473
    • (2003) Cancer Research , vol.63 , pp. 6772-6783
    • Davol, P.A.1    Bagdasaryan, R.2    Elfenbein, G.J.3    Maizel, A.L.4    Frackelton Jr, A.R.5
  • 38
    • 35348820034 scopus 로고    scopus 로고
    • P66 Shc tumor levels show a strong prognostic correlation with disease outcome in stage IIA colon cancer
    • 17908971
    • SR Grossman S Lyle MB Resnick E Sabo RT Lis E Rosinha, et al. 2007 p66 Shc tumor levels show a strong prognostic correlation with disease outcome in stage IIA colon cancer Clinical Cancer Research 13 5798 5804 17908971
    • (2007) Clinical Cancer Research , vol.13 , pp. 5798-5804
    • Grossman, S.R.1    Lyle, S.2    Resnick, M.B.3    Sabo, E.4    Lis, R.T.5    Rosinha, E.6
  • 39
    • 0031979414 scopus 로고    scopus 로고
    • Characterization of human epidermal growth factor receptor and c-Src interactions in human breast tumor cells
    • JS Biscardi AP Belsches SJ Parsons 1998 Characterization of human epidermal growth factor receptor and c-Src interactions in human breast tumor cells Molecular Carcinoenesis 21 261 272
    • (1998) Molecular Carcinoenesis , vol.21 , pp. 261-272
    • Biscardi, J.S.1    Belsches, A.P.2    Parsons, S.J.3
  • 40
    • 0031812342 scopus 로고    scopus 로고
    • Constitutively tyrosine phosphorylated p52 Shc in breast cancer cells: Correlation with ErbB2 and p66 Shc expression
    • 9696394
    • LE Stevenson AR Frackelton Jr 1998 Constitutively tyrosine phosphorylated p52 Shc in breast cancer cells: correlation with ErbB2 and p66 Shc expression Breast Cancer Research and Treatment 49 119 128 9696394
    • (1998) Breast Cancer Research and Treatment , vol.49 , pp. 119-128
    • Stevenson, L.E.1    Frackelton Jr, A.R.2
  • 41
    • 27944483366 scopus 로고    scopus 로고
    • Expression of p66 [Shc] protein correlates with proliferation of human prostate cancer cells
    • 16170380
    • S Veeramani T Igawa TC Yuan FF Lin MS Lee JS Lin, et al. 2005 Expression of p66 [Shc] protein correlates with proliferation of human prostate cancer cells Oncogene 24 7203 7212 16170380
    • (2005) Oncogene , vol.24 , pp. 7203-7212
    • Veeramani, S.1    Igawa, T.2    Yuan, T.C.3    Lin, F.F.4    Lee, M.S.5    Lin, J.S.6
  • 42
    • 50649122731 scopus 로고    scopus 로고
    • Mitochondrial redox signaling by p66 Shc is involved in regulating androgenic growth stimulation of human prostate cancer cells
    • 18504439
    • S Veeramani TC Yuan FF Lin MF Lin 2008 Mitochondrial redox signaling by p66 Shc is involved in regulating androgenic growth stimulation of human prostate cancer cells Oncogene 27 5057 5068 18504439
    • (2008) Oncogene , vol.27 , pp. 5057-5068
    • Veeramani, S.1    Yuan, T.C.2    Lin, F.F.3    Lin, M.F.4
  • 43
    • 0037151066 scopus 로고    scopus 로고
    • The p66 Shc longevity gene is silenced through epigenetic modifications of an alternative promoter
    • 11948181
    • A Ventura L Luzi S Pacini CT Baldari PG Pelicci 2002 The p66 Shc longevity gene is silenced through epigenetic modifications of an alternative promoter Journal of Biological Chemistry 277 22370 22376 11948181
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 22370-22376
    • Ventura, A.1    Luzi, L.2    Pacini, S.3    Baldari, C.T.4    Pelicci, P.G.5
  • 44
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • 9405336
    • T Pawson JD Scott 1997 Signaling through scaffold, anchoring, and adaptor proteins Science 278 2075 2080 9405336
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 45
    • 16544395966 scopus 로고    scopus 로고
    • Enhanced expression of adaptor molecule p46 Shc in nuclei of hepatocellular carcinoma cells: Study of LEC rats
    • 15375560
    • S Yoshida T Masaki H Feng J Yuji Y Miyauchi T Funaki, et al. 2004 Enhanced expression of adaptor molecule p46 Shc in nuclei of hepatocellular carcinoma cells: study of LEC rats International Journal of Oncology 25 1089 1096 15375560
    • (2004) International Journal of Oncology , vol.25 , pp. 1089-1096
    • Yoshida, S.1    Masaki, T.2    Feng, H.3    Yuji, J.4    Miyauchi, Y.5    Funaki, T.6
  • 46
    • 22744447211 scopus 로고    scopus 로고
    • Electron transfer between cytochrome c and p66 Shc generates reactive oxygen species that trigger mitochondrial apoptosis
    • 16051147
    • M Giorgio E Migliaccio F Orsini D Paolucci M Moroni C Contursi, et al. 2005 Electron transfer between cytochrome c and p66 Shc generates reactive oxygen species that trigger mitochondrial apoptosis Cell 122 221 233 16051147
    • (2005) Cell , vol.122 , pp. 221-233
    • Giorgio, M.1    Migliaccio, E.2    Orsini, F.3    Paolucci, D.4    Moroni, M.5    Contursi, C.6
  • 47
    • 17644391695 scopus 로고    scopus 로고
    • P66SHC: The apoptotic side of Shc proteins
    • 15711918
    • M Pellegrini S Pacini CT Baldari 2005 p66SHC: the apoptotic side of Shc proteins Apoptosis 10 13 18 15711918
    • (2005) Apoptosis , vol.10 , pp. 13-18
    • Pellegrini, M.1    Pacini, S.2    Baldari, C.T.3
  • 48
    • 0029664527 scopus 로고    scopus 로고
    • P66Shc isoform down-regulated and not required for HER-2/neu signaling pathway in human breast cancer cell lines with HER-2/neu overexpression
    • 8660324
    • Y Xie MC Hung 1996 p66Shc isoform down-regulated and not required for HER-2/neu signaling pathway in human breast cancer cell lines with HER-2/neu overexpression Biochemical and Biophysical Research Communications 221 140 145 8660324
    • (1996) Biochemical and Biophysical Research Communications , vol.221 , pp. 140-145
    • Xie, Y.1    Hung, M.C.2
  • 50
    • 0035930534 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase specifically phosphorylates p66ShcA at serine 36 in response to ultraviolet irradiation
    • 11602589
    • S Le TJ Connors AC Maroney 2001 c-Jun N-terminal kinase specifically phosphorylates p66ShcA at serine 36 in response to ultraviolet irradiation Journal of Biological Chemistry 276 48332 48336 11602589
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 48332-48336
    • Le, S.1    Connors, T.J.2    Maroney, A.C.3
  • 51
    • 0030998473 scopus 로고    scopus 로고
    • Insulin stimulates the phosphorylation of the 66- and 52-kilodalton Shc isoforms by distinct pathways
    • 9165038
    • AW Kao SB Waters S Okada JE Pessin 1997 Insulin stimulates the phosphorylation of the 66- and 52-kilodalton Shc isoforms by distinct pathways Endocrinology 138 2474 2480 9165038
    • (1997) Endocrinology , vol.138 , pp. 2474-2480
    • Kao, A.W.1    Waters, S.B.2    Okada, S.3    Pessin, J.E.4
  • 52
    • 0034665140 scopus 로고    scopus 로고
    • Taxol mediates serine phosphorylation of the 66-kDa Shc isoform
    • 11016645
    • CP Yang SB Horwitz 2000 Taxol mediates serine phosphorylation of the 66-kDa Shc isoform Cancer Research 60 5171 5178 11016645
    • (2000) Cancer Research , vol.60 , pp. 5171-5178
    • Yang, C.P.1    Horwitz, S.B.2
  • 53
    • 0030783255 scopus 로고    scopus 로고
    • The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen- activated protein kinase pathway
    • 9346957
    • N Okada K Wada BA Goldsmith S Koizumi 1997 The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen- activated protein kinase pathway Journal of Biological Chemistry 272 28042 28049 9346957
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 28042-28049
    • Okada, N.1    Wada, K.2    Goldsmith, B.A.3    Koizumi, S.4
  • 54
    • 30044449425 scopus 로고    scopus 로고
    • Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: Role in Rac1-induced oxidative stress
    • 16251354
    • FA Khanday T Yamamori I Mattagajasingh Z Zhang A Bugayenko A Naqvi, et al. 2006 Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: role in Rac1-induced oxidative stress Molecular Biology of the Cell 17 122 129 16251354
    • (2006) Molecular Biology of the Cell , vol.17 , pp. 122-129
    • Khanday, F.A.1    Yamamori, T.2    Mattagajasingh, I.3    Zhang, Z.4    Bugayenko, A.5    Naqvi, A.6
  • 55
    • 33846817351 scopus 로고    scopus 로고
    • Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc
    • 17272725
    • P Pinton A Rimessi S Marchi F Orsini E Migliaccio M Giorgio, et al. 2007 Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc Science 315 659 663 17272725
    • (2007) Science , vol.315 , pp. 659-663
    • Pinton, P.1    Rimessi, A.2    Marchi, S.3    Orsini, F.4    Migliaccio, E.5    Giorgio, M.6
  • 57
    • 0036328026 scopus 로고    scopus 로고
    • Role of DNA methylation in the regulation of cell function: Autoimmunity, aging and cancer
    • 12163700
    • BC Richardson 2002 Role of DNA methylation in the regulation of cell function: autoimmunity, aging and cancer The Journal of Nutrition 132 2401S 2405S 12163700
    • (2002) The Journal of Nutrition , vol.132
    • Richardson, B.C.1
  • 60
    • 0032401808 scopus 로고    scopus 로고
    • Aging and DNA methylation in colorectal mucosa and cancer
    • 9850084
    • N Ahuja Q Li AL Mohan SB Baylin JP Issa 1998 Aging and DNA methylation in colorectal mucosa and cancer Cancer Research 58 5489 5494 9850084
    • (1998) Cancer Research , vol.58 , pp. 5489-5494
    • Ahuja, N.1    Li, Q.2    Mohan, A.L.3    Baylin, S.B.4    Issa, J.P.5
  • 64
    • 6344287822 scopus 로고    scopus 로고
    • Role of the p66Shc isoform in insulin-like growth factor i receptor signaling through MEK/Erk and regulation of actin cytoskeleton in rat myoblasts
    • 15262993
    • A Natalicchio L Laviola C De Tullio LA Renna C Montrone S Perrini, et al. 2004 Role of the p66Shc isoform in insulin-like growth factor I receptor signaling through MEK/Erk and regulation of actin cytoskeleton in rat myoblasts Journal of Biological Chemistry 279 43900 43909 15262993
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 43900-43909
    • Natalicchio, A.1    Laviola, L.2    De Tullio, C.3    Renna, L.A.4    Montrone, C.5    Perrini, S.6
  • 65
    • 0035854682 scopus 로고    scopus 로고
    • Endothelin-1 induces serine phosphorylation of the adaptor protein p66Shc and its association with 14-3-3 protein in glomerular mesangial cells
    • 11342545
    • M Foschi F Franchi J Han G La Villa A Sorokin 2001 Endothelin-1 induces serine phosphorylation of the adaptor protein p66Shc and its association with 14-3-3 protein in glomerular mesangial cells Journal of Biological Chemistry 276 26640 26647 11342545
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 26640-26647
    • Foschi, M.1    Franchi, F.2    Han, J.3    La Villa, G.4    Sorokin, A.5
  • 66
    • 0037119469 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation of ShcA. Regulation of protein-tyrosine phosphatase-pest binding and involvement in insulin signaling
    • 12052829
    • A Faisal M el-Shemerly D Hess Y Nagamine 2002 Serine/threonine phosphorylation of ShcA. Regulation of protein-tyrosine phosphatase-pest binding and involvement in insulin signaling Journal of Biological Chemistry 277 30144 30152 12052829
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 30144-30152
    • Faisal, A.1    El-Shemerly, M.2    Hess, D.3    Nagamine, Y.4
  • 67
    • 0037067132 scopus 로고    scopus 로고
    • Distinct mechanisms of taxol-induced serine phosphorylation of the 66-kDa Shc isoform in A549 and RAW 264.7 cells
    • 12063170
    • CP Yang SB Horwitz 2002 Distinct mechanisms of taxol-induced serine phosphorylation of the 66-kDa Shc isoform in A549 and RAW 264.7 cells Biochimica et Biophysica Acta 1590 76 83 12063170
    • (2002) Biochimica et Biophysica Acta , vol.1590 , pp. 76-83
    • Yang, C.P.1    Horwitz, S.B.2
  • 68
    • 44449146636 scopus 로고    scopus 로고
    • P66shc inhibits pro-survival epidermal growth factor receptor/ERK signaling during severe oxidative stress in mouse renal proximal tubule cells
    • 18174162
    • I Arany A Faisal Y Nagamine RL Safirstein 2008 p66shc inhibits pro-survival epidermal growth factor receptor/ERK signaling during severe oxidative stress in mouse renal proximal tubule cells Journal of Biological Chemistry 283 6110 6117 18174162
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 6110-6117
    • Arany, I.1    Faisal, A.2    Nagamine, Y.3    Safirstein, R.L.4
  • 69
    • 0030662196 scopus 로고    scopus 로고
    • 12-O- Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase [ERK] signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells
    • 9388190
    • MY El-Shemerly D Besser M Nagasawa Y Nagamine 1997 12-O- Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase [ERK] signaling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells Journal of Biological Chemistry 272 30599 30602 9388190
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30599-30602
    • El-Shemerly, M.Y.1    Besser, D.2    Nagasawa, M.3    Nagamine, Y.4
  • 70
    • 0030030357 scopus 로고    scopus 로고
    • Insulin stimulation of a MEK- dependent but ERK-independent SOS protein kinase
    • 8552085
    • KH Holt BG Kasson JE Pessin 1996 Insulin stimulation of a MEK- dependent but ERK-independent SOS protein kinase Molecular and Cellular Biology 16 577 583 8552085
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 577-583
    • Holt, K.H.1    Kasson, B.G.2    Pessin, J.E.3
  • 71
    • 0038509964 scopus 로고    scopus 로고
    • P66[Shc]: At the crossroad of oxidative stress and the genetics of aging
    • 12763525
    • S Purdom QM Chen 2003 p66[Shc]: at the crossroad of oxidative stress and the genetics of aging Trends in Molecular Medicine 9 206 210 12763525
    • (2003) Trends in Molecular Medicine , vol.9 , pp. 206-210
    • Purdom, S.1    Chen, Q.M.2
  • 73
    • 0034031776 scopus 로고    scopus 로고
    • Endothelin-1 inhibits apoptosis of vascular smooth muscle cells induced by nitric oxide and serum deprivation via MAP kinase pathway
    • 10764663
    • M Shichiri M Yokokura F Marumo Y Hirata 2000 Endothelin-1 inhibits apoptosis of vascular smooth muscle cells induced by nitric oxide and serum deprivation via MAP kinase pathway Arteriosclerosis, Thrombosis, and Vascular Biology 20 989 997 10764663
    • (2000) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.20 , pp. 989-997
    • Shichiri, M.1    Yokokura, M.2    Marumo, F.3    Hirata, Y.4
  • 74
    • 0028032399 scopus 로고
    • Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase
    • 7929214
    • T Habib R Herrera SJ Decker 1994 Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase Journal of Biological Chemistry 269 25243 25246 7929214
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 25243-25246
    • Habib, T.1    Herrera, R.2    Decker, S.J.3
  • 75
    • 0029988340 scopus 로고    scopus 로고
    • Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity
    • 8626541
    • A Charest J Wagner S Jacob CJ McGlade ML Tremblay 1996 Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity Journal of Biological Chemistry 271 8424 8429 8626541
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 8424-8429
    • Charest, A.1    Wagner, J.2    Jacob, S.3    McGlade, C.J.4    Tremblay, M.L.5
  • 76
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-depedent signaling pathway
    • 11884717
    • S Nemoto T Finkel 2002 Redox regulation of forkhead proteins through a p66shc-depedent signaling pathway Science 295 2450 2452 11884717
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 77
    • 85047695800 scopus 로고    scopus 로고
    • A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis
    • 12032825
    • M Trinei M Giorgio A Cicalese S Barozzi A Ventura E Migliaccio, et al. 2002 A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis Oncogene 21 3872 3878 12032825
    • (2002) Oncogene , vol.21 , pp. 3872-3878
    • Trinei, M.1    Giorgio, M.2    Cicalese, A.3    Barozzi, S.4    Ventura, A.5    Migliaccio, E.6
  • 81
    • 23244434000 scopus 로고    scopus 로고
    • Genetic deletion of the p66Shc adaptor protein protects from angiotensin II-induced myocardial damage
    • 15998704
    • G Graiani C Lagrasta E Migliaccio F Spillmann M Meloni P Madeddu, et al. 2005 Genetic deletion of the p66Shc adaptor protein protects from angiotensin II-induced myocardial damage Hypertension 46 433 440 15998704
    • (2005) Hypertension , vol.46 , pp. 433-440
    • Graiani, G.1    Lagrasta, C.2    Migliaccio, E.3    Spillmann, F.4    Meloni, M.5    Madeddu, P.6
  • 83
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • 8635688
    • CK Sen L Packer 1996 Antioxidant and redox regulation of gene transcription The FASEB Journal 10 709 720 8635688
    • (1996) The FASEB Journal , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 84
    • 2942584910 scopus 로고    scopus 로고
    • The life span determinant p66Shc localizes to mitochondria where it associates with mitochondrial heat shock protein 70 and regulates trans-membrane potential
    • 15078873
    • F Orsini E Migliaccio M Moroni C Contursi VA Raker D Piccini, et al. 2004 The life span determinant p66Shc localizes to mitochondria where it associates with mitochondrial heat shock protein 70 and regulates trans-membrane potential Journal of Biological Chemistry 279 25689 25695 15078873
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 25689-25695
    • Orsini, F.1    Migliaccio, E.2    Moroni, M.3    Contursi, C.4    Raker, V.A.5    Piccini, D.6
  • 86
    • 0028115871 scopus 로고
    • X- irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates
    • 8261431
    • MA Stevenson SS Pollock CN Coleman SK Calderwood 1994 X- irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates Cancer Research 54 12 15 8261431
    • (1994) Cancer Research , vol.54 , pp. 12-15
    • Stevenson, M.A.1    Pollock, S.S.2    Coleman, C.N.3    Calderwood, S.K.4
  • 88
    • 0033229866 scopus 로고    scopus 로고
    • P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2
    • 10545114
    • PF Li R Dietz R von Harsdorf 1999 p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2 The EMBO Journal 18 6027 6036 10545114
    • (1999) The EMBO Journal , vol.18 , pp. 6027-6036
    • Li, P.F.1    Dietz, R.2    Von Harsdorf, R.3
  • 89
    • 0034629291 scopus 로고    scopus 로고
    • P53 induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • DOI 10.1074/jbc.275.10.7337
    • M Schuler E Bossy-Wetzel JC Goldstein P Fitzgerald DR Green 2000 p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release Journal of Biological Chemistry 275 7337 7342 10702305 (Pubitemid 30146286)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 7337-7342
    • Schuler, M.1    Bossy-Wetzel, E.2    Goldstein, J.C.3    Fitzgerald, P.4    Green, D.R.5
  • 93
    • 0034136548 scopus 로고    scopus 로고
    • Apoptosis in the early bovine embryo
    • 10840875
    • C Matwee DH Betts WA King 2000 Apoptosis in the early bovine embryo Zygote 8 57 68 10840875
    • (2000) Zygote , vol.8 , pp. 57-68
    • Matwee, C.1    Betts, D.H.2    King, W.A.3
  • 94
    • 33947727705 scopus 로고    scopus 로고
    • Endogenously generated hydrogen peroxide induces apoptosis via mitochondrial damage independent of NF-kappaB and p53 activation in bovine embryos
    • 17353043
    • C Velez-Pardo AT Morales MJ Del Rio M Olivera-Angel 2007 Endogenously generated hydrogen peroxide induces apoptosis via mitochondrial damage independent of NF-kappaB and p53 activation in bovine embryos Theriogenology 67 1285 1296 17353043
    • (2007) Theriogenology , vol.67 , pp. 1285-1296
    • Velez-Pardo, C.1    Morales, A.T.2    Del Rio, M.J.3    Olivera-Angel, M.4
  • 95
    • 49649117536 scopus 로고    scopus 로고
    • Permanent embryo arrest: Molecular and cellular concepts
    • 18511487
    • DH Betts P Madan 2008 Permanent embryo arrest: molecular and cellular concepts Molecular Human Reproduction 14 445 453 18511487
    • (2008) Molecular Human Reproduction , vol.14 , pp. 445-453
    • Betts, D.H.1    Madan, P.2
  • 96
    • 0039425278 scopus 로고    scopus 로고
    • Negative regulation of the forkhead transcription factor FKHR by Akt
    • 10358014
    • ED Tang G Nuñez FG Barr KL Guan 1999 Negative regulation of the forkhead transcription factor FKHR by Akt Journal of Biological Chemistry 274 16741 16746 10358014
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 16741-16746
    • Tang, E.D.1    Nuñez, G.2    Barr, F.G.3    Guan, K.L.4
  • 97
    • 0035019007 scopus 로고    scopus 로고
    • Identification and characterization of members of the FKHR [FOX O] subclass of winged-helix transcription factors in the mouse
    • 11353388
    • WH Biggs 3rd WK Cavenee KC Arden 2001 Identification and characterization of members of the FKHR [FOX O] subclass of winged-helix transcription factors in the mouse Mammalian Genome 12 416 425 11353388
    • (2001) Mammalian Genome , vol.12 , pp. 416-425
    • Biggs III, W.H.1    Cavenee, W.K.2    Arden, K.C.3
  • 98
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • 10102273
    • A Brunet A Bonni MJ Zigmond MZ Lin P Juo LS Hu, et al. 1999 Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor Cell 96 857 868 10102273
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1    Bonni, A.2    Zigmond, M.J.3    Lin, M.Z.4    Juo, P.5    Hu, L.S.6
  • 99
    • 0037136563 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
    • 12239572
    • GJ Kops TB Dansen PE Polderman I Saarloos KW Wirtz PJ Coffer, et al. 2002 Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress Nature 419 316 321 12239572
    • (2002) Nature , vol.419 , pp. 316-321
    • Kops, G.J.1    Dansen, T.B.2    Polderman, P.E.3    Saarloos, I.4    Wirtz, K.W.5    Coffer, P.J.6
  • 100
    • 0034609737 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1
    • 11050388
    • PF Dijkers RH Medema JW Lammers L Koenderman PJ Coffer 2000 Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1 Current Biology 10 1201 1204 11050388
    • (2000) Current Biology , vol.10 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3    Koenderman, L.4    Coffer, P.J.5
  • 101
    • 0347087425 scopus 로고    scopus 로고
    • A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria
    • 14573619
    • A Ventura M Maccarana VA Raker PG Pelicci 2004 A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria Journal of Biological Chemistry 279 2299 2306 14573619
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 2299-2306
    • Ventura, A.1    MacCarana, M.2    Raker, V.A.3    Pelicci, P.G.4
  • 103
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • 9624056
    • R Rizzuto P Pinton W Carrington FS Fay KE Fogarty LM Lifshitz, et al. 1998 Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses Science 280 1763 1766 9624056
    • (1998) Science , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3    Fay, F.S.4    Fogarty, K.E.5    Lifshitz, L.M.6
  • 107
    • 18344387559 scopus 로고    scopus 로고
    • Phosphorylation-specific prolyl isomerization: Is there an underlying theme?
    • 15867923
    • G Wulf G Finn F Suizu KP Lu 2005 Phosphorylation-specific prolyl isomerization: is there an underlying theme? Nature Cell Biology 7 435 441 15867923
    • (2005) Nature Cell Biology , vol.7 , pp. 435-441
    • Wulf, G.1    Finn, G.2    Suizu, F.3    Lu, K.P.4
  • 108
    • 33750618076 scopus 로고    scopus 로고
    • Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc
    • 17081113
    • F Orsini M Moroni C Contursi M Yano P Pelicci M Giorgio, et al. 2006 Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc Biological Chemistry 387 1405 1410 17081113
    • (2006) Biological Chemistry , vol.387 , pp. 1405-1410
    • Orsini, F.1    Moroni, M.2    Contursi, C.3    Yano, M.4    Pelicci, P.5    Giorgio, M.6
  • 112
    • 0030057982 scopus 로고    scopus 로고
    • Mechanisms and evolution of aging
    • 8658201
    • GJ Lithgow TB Kirkwood 1996 Mechanisms and evolution of aging Science 273 80 8658201
    • (1996) Science , vol.273 , pp. 80
    • Lithgow, G.J.1    Kirkwood, T.B.2
  • 113
    • 0031796052 scopus 로고    scopus 로고
    • 8-Hydroxydeoxyguanosine and 8-hydroxyguanine as biomarkers of oxidative DNA damage
    • 9919519
    • HJ Helbock KB Beckman BN Ames 1999 8-Hydroxydeoxyguanosine and 8-hydroxyguanine as biomarkers of oxidative DNA damage Methods in Enzymology 300 156 166 9919519
    • (1999) Methods in Enzymology , vol.300 , pp. 156-166
    • Helbock, H.J.1    Beckman, K.B.2    Ames, B.N.3
  • 114
    • 4043176258 scopus 로고    scopus 로고
    • Expression profiles of p53 and p66shc during oxidative stress-induced senescence in fetal bovine fibroblasts
    • 15302571
    • LA Favetta C Robert WA King DH Betts 2004 Expression profiles of p53 and p66shc during oxidative stress-induced senescence in fetal bovine fibroblasts Experimental Cell Research 299 36 48 15302571
    • (2004) Experimental Cell Research , vol.299 , pp. 36-48
    • Favetta, L.A.1    Robert, C.2    King, W.A.3    Betts, D.H.4
  • 115
    • 0041383870 scopus 로고    scopus 로고
    • Differential regulation of Shc adaptor proteins in skeletal muscle, spinal cord and forebrain of aged rats with sensorimotor impairment
    • 12882334
    • X Jiang E Edstrom M Altun B Ulfhake 2003 Differential regulation of Shc adaptor proteins in skeletal muscle, spinal cord and forebrain of aged rats with sensorimotor impairment Aging Cell 2 47 57 12882334
    • (2003) Aging Cell , vol.2 , pp. 47-57
    • Jiang, X.1    Edstrom, E.2    Altun, M.3    Ulfhake, B.4
  • 116
    • 21744449331 scopus 로고    scopus 로고
    • The microtubule stabilizing agent discodermolide is a potent inducer of accelerated cell senescence
    • 15711127
    • LE Klein BS Freeze AB Smith 3rd SB Horwitz 2005 The microtubule stabilizing agent discodermolide is a potent inducer of accelerated cell senescence Cell Cycle 4 501 507 15711127
    • (2005) Cell Cycle , vol.4 , pp. 501-507
    • Klein, L.E.1    Freeze, B.S.2    Smith III, A.B.3    Horwitz, S.B.4
  • 117
    • 33745586024 scopus 로고    scopus 로고
    • Mitochondrial DNA copy number is regulated by cellular proliferation: A role for Ras and p66[Shc]
    • M Trinei I Berniakovich PG Pelicci M Giorgio 2006 Mitochondrial DNA copy number is regulated by cellular proliferation: a role for Ras and p66[Shc] Biochim Biophysics Acta 1757 624 630
    • (2006) Biochim Biophysics Acta , vol.1757 , pp. 624-630
    • Trinei, M.1    Berniakovich, I.2    Pelicci, P.G.3    Giorgio, M.4
  • 118
    • 17844366538 scopus 로고    scopus 로고
    • The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion
    • 15650019
    • M Masuyama R Iida H Takatsuka T Yasuda T Matsuki 2005 The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion Molecular Endocrinology 19 1170 1180 15650019
    • (2005) Molecular Endocrinology , vol.19 , pp. 1170-1180
    • Masuyama, M.1    Iida, R.2    Takatsuka, H.3    Yasuda, T.4    Matsuki, T.5
  • 120
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • 7652575
    • MF Olson A Ashworth A Hall 1995 An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1 Science 269 1270 1272 7652575
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 121
    • 0030723163 scopus 로고    scopus 로고
    • Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways
    • 9388204
    • B Anand-Apte BR Zetter A Viswanathan RG Qiu J Chen R Ruggieri, et al. 1997 Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways Journal of Biological Chemistry 272 30688 30692 9388204
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30688-30692
    • Anand-Apte, B.1    Zetter, B.R.2    Viswanathan, A.3    Qiu, R.G.4    Chen, J.5    Ruggieri, R.6
  • 123
    • 0028043735 scopus 로고
    • Receptor tyrosine kinase signaling required for integrin alpha v beta 5-directed cell motility but not adhesion on vitronectin
    • 7525598
    • RL Klemke M Yebra EM Bayna DA Cheresh 1994 Receptor tyrosine kinase signaling required for integrin alpha v beta 5-directed cell motility but not adhesion on vitronectin The Journal of Cell Biology 127 859 866 7525598
    • (1994) The Journal of Cell Biology , vol.127 , pp. 859-866
    • Klemke, R.L.1    Yebra, M.2    Bayna, E.M.3    Cheresh, D.A.4
  • 125
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • 8608589
    • DA Lauffenburger AF Horwitz 1996 Cell migration: a physically integrated molecular process Cell 84 359 369 8608589
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 127
    • 17744365016 scopus 로고    scopus 로고
    • P66shc expression in proliferating thyroid cells is regulated by thyrotropin receptor signaling
    • 15705774
    • YJ Park TY Kim SH Lee H Kim SW Kim M Shong, et al. 2005 p66shc expression in proliferating thyroid cells is regulated by thyrotropin receptor signaling Endocrinology 146 2473 2480 15705774
    • (2005) Endocrinology , vol.146 , pp. 2473-2480
    • Park, Y.J.1    Kim, T.Y.2    Lee, S.H.3    Kim, H.4    Kim, S.W.5    Shong, M.6
  • 128
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • 8187171
    • E Ruoslahti JC Reed 1994 Anchorage dependence, integrins, and apoptosis Cell 77 477 478 8187171
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 130
    • 0036091414 scopus 로고    scopus 로고
    • The role of alpha[v]beta[3] in prostate cancer progression
    • 11988838
    • CR Cooper CH Chay KJ Pienta 2002 The role of alpha[v]beta[3] in prostate cancer progression Neoplasia 4 191 194 11988838
    • (2002) Neoplasia , vol.4 , pp. 191-194
    • Cooper, C.R.1    Chay, C.H.2    Pienta, K.J.3
  • 131
    • 0033118450 scopus 로고    scopus 로고
    • Prostatic carcinoma cell migration via alpha[v]beta3 integrin is modulated by a focal adhesion kinase pathway
    • 10197643
    • DQ Zheng AS Woodard M Fornaro G Tallini LR Languino 1999 Prostatic carcinoma cell migration via alpha[v]beta3 integrin is modulated by a focal adhesion kinase pathway Cancer Research 59 1655 1664 10197643
    • (1999) Cancer Research , vol.59 , pp. 1655-1664
    • Zheng, D.Q.1    Woodard, A.S.2    Fornaro, M.3    Tallini, G.4    Languino, L.R.5
  • 132
    • 43249109660 scopus 로고    scopus 로고
    • Signaling through ShcA is required for transforming growth factor beta- and Neu/ErbB-2-induced breast cancer cell motility and invasion
    • 18332126
    • JJ Northey J Chmielecki E Ngan C Russo MG Annis WJ Muller, et al. 2008 Signaling through ShcA is required for transforming growth factor beta- and Neu/ErbB-2-induced breast cancer cell motility and invasion Molecular and Cellular Biology 28 3162 3176 18332126
    • (2008) Molecular and Cellular Biology , vol.28 , pp. 3162-3176
    • Northey, J.J.1    Chmielecki, J.2    Ngan, E.3    Russo, C.4    Annis, M.G.5    Muller, W.J.6
  • 133
    • 47749101253 scopus 로고    scopus 로고
    • The ShcA adaptor protein is a critical regulator of breast cancer progression
    • 18604176
    • J Ursini-Siegel WJ Muller 2008 The ShcA adaptor protein is a critical regulator of breast cancer progression Cell Cycle 7 1936 1943 18604176
    • (2008) Cell Cycle , vol.7 , pp. 1936-1943
    • Ursini-Siegel, J.1    Muller, W.J.2
  • 135
    • 0036402136 scopus 로고    scopus 로고
    • Reactive oxygen species stimulated human hepatoma cell proliferation via cross-talk between PI3-K/PKB and JNK signaling pathways
    • 12361705
    • SL Liu X Lin DY Shi J Cheng CQ Wu YD Zhang 2002 Reactive oxygen species stimulated human hepatoma cell proliferation via cross-talk between PI3-K/PKB and JNK signaling pathways Archives of Biochemistry and Biophysics 406 173 182 12361705
    • (2002) Archives of Biochemistry and Biophysics , vol.406 , pp. 173-182
    • Liu, S.L.1    Lin, X.2    Shi, D.Y.3    Cheng, J.4    Wu, C.Q.5    Zhang, Y.D.6
  • 136
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • T Finkel NJ Holbrook 2000 Oxidants, oxidative stress and the biology of ageing Nature 9 239 247
    • (2000) Nature , vol.9 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 137
    • 37349012503 scopus 로고    scopus 로고
    • Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells
    • 18067579
    • YW Lou YY Chen SF Hsu RK Chen CL Lee KH Khoo, et al. 2008 Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells FEBS Journal 275 69 88 18067579
    • (2008) FEBS Journal , vol.275 , pp. 69-88
    • Lou, Y.W.1    Chen, Y.Y.2    Hsu, S.F.3    Chen, R.K.4    Lee, C.L.5    Khoo, K.H.6
  • 138
    • 0030568824 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of a 185 kDa phosphoprotein [pp 185] inversely correlates with the cellular activity of human prostatic acid phosphatase
    • 8806615
    • MF Lin TC Meng 1996 Tyrosine phosphorylation of a 185 kDa phosphoprotein [pp 185] inversely correlates with the cellular activity of human prostatic acid phosphatase Biochemical and Biophysical Research Communications 226 206 213 8806615
    • (1996) Biochemical and Biophysical Research Communications , vol.226 , pp. 206-213
    • Lin, M.F.1    Meng, T.C.2
  • 139
    • 0034785826 scopus 로고    scopus 로고
    • Decreased expression of cellular prostatic acid phosphatase increases umorigenicity of human prostate cancer cells
    • 11586265
    • MF Lin MS Lee XW Zhou JC Andressen TC Meng SL Johansson 2001 Decreased expression of cellular prostatic acid phosphatase increases umorigenicity of human prostate cancer cells The Journal of Urology 166 1943 1950 11586265
    • (2001) The Journal of Urology , vol.166 , pp. 1943-1950
    • Lin, M.F.1    Lee, M.S.2    Zhou, X.W.3    Andressen, J.C.4    Meng, T.C.5    Johansson, S.L.6
  • 140
    • 29144502951 scopus 로고    scopus 로고
    • Cellular prostatic acid phosphatase: A protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer
    • S Veeramani TC Yuan SJ Chen FF Lin JE Petersen S Shaheduzzaman, et al. 2005 Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer Endocr-Related Cancer 12 805 822
    • (2005) Endocr-Related Cancer , vol.12 , pp. 805-822
    • Veeramani, S.1    Yuan, T.C.2    Chen, S.J.3    Lin, F.F.4    Petersen, J.E.5    Shaheduzzaman, S.6
  • 141
  • 143
    • 3843074330 scopus 로고    scopus 로고
    • Deregulation of the Rho GTPase, Rac1, suppresses cyclin-dependent kinase inhibitor p21[CIP1] levels in androgen-independent human prostate cancer cells
    • 15077174
    • S Knight-Krajewski CF Welsh Y Liu LS Lyons JM Faysal ES Yang, et al. 2004 Deregulation of the Rho GTPase, Rac1, suppresses cyclin-dependent kinase inhibitor p21[CIP1] levels in androgen-independent human prostate cancer cells Oncogene 23 5513 5522 15077174
    • (2004) Oncogene , vol.23 , pp. 5513-5522
    • Knight-Krajewski, S.1    Welsh, C.F.2    Liu, Y.3    Lyons, L.S.4    Faysal, J.M.5    Yang, E.S.6
  • 144
    • 66249105451 scopus 로고    scopus 로고
    • Role of reactive oxygen species in carcinogenesis
    • R. Banarjee (eds). Wiley New Jersey
    • Veeramani, S., & Lin, M. F. (2007). Role of reactive oxygen species in carcinogenesis. In R. Banarjee (Ed.), Redox biochemistry (pp. 212-218). New Jersey: Wiley.
    • (2007) Redox Biochemistry , pp. 212-218
    • Veeramani, S.1    Lin, M.F.2
  • 147
    • 0031923726 scopus 로고    scopus 로고
    • PSA and acid phosphatase in the diagnosis of prostate cancer
    • TM Chu MF Lin 1998 PSA and acid phosphatase in the diagnosis of prostate cancer Journal of Clinical Ligand Assay 21 24 34
    • (1998) Journal of Clinical Ligand Assay , vol.21 , pp. 24-34
    • Chu, T.M.1    Lin, M.F.2
  • 148
  • 149
    • 0017567185 scopus 로고
    • Detection of prostatic cancer by solid-phase radioimmunoassay of serum prostatic acid phosphatase
    • AG Foti JF Cooper H Herschman RR Malvaez 1977 Detection of prostatic cancer by solid-phase radioimmunoassay of serum prostatic acid phosphatase New England Journal of Medicine 297 1357 1361 73133 (Pubitemid 8256292)
    • (1977) New England Journal of Medicine , vol.297 , Issue.25 , pp. 1357-1361
    • Foti, A.G.1    Cooper, J.F.2    Herschman, H.3    Malvaez, R.R.4
  • 150
    • 0019826108 scopus 로고
    • Expression of prostatic acid phosphatase in human prostate cancer
    • 7296542
    • R Loor MC Wang L Valenzuela TM Chu 1981 Expression of prostatic acid phosphatase in human prostate cancer Cancer Letters 14 63 69 7296542
    • (1981) Cancer Letters , vol.14 , pp. 63-69
    • Loor, R.1    Wang, M.C.2    Valenzuela, L.3    Chu, T.M.4
  • 151
    • 0019416718 scopus 로고
    • Immunofluorescence for prostatic acid phosphatase: Clinical applications
    • 7021879
    • JE Pontes NR Rose C Ercole JM Pierce Jr 1981 Immunofluorescence for prostatic acid phosphatase: clinical applications The Journal of Urology 126 187 189 7021879
    • (1981) The Journal of Urology , vol.126 , pp. 187-189
    • Pontes, J.E.1    Rose, N.R.2    Ercole, C.3    Pierce Jr, J.M.4
  • 152
    • 0025141718 scopus 로고
    • Gene expression and prostate specificity of human prostatic acid phosphatase [PAP]: Evaluation by RNA blot analyses
    • 1688712
    • T Solin M Kontturi R Pohlmann P Vihko 1990 Gene expression and prostate specificity of human prostatic acid phosphatase [PAP]: evaluation by RNA blot analyses Biochimica et Biophysica Acta 1048 72 77 1688712
    • (1990) Biochimica et Biophysica Acta , vol.1048 , pp. 72-77
    • Solin, T.1    Kontturi, M.2    Pohlmann, R.3    Vihko, P.4
  • 153
    • 0027252549 scopus 로고
    • Prostate specific antigen and prostatic acid phosphatase immunoreactivity as prognostic indicators of advanced prostatic carcinoma
    • 7683340
    • H Sakai Y Yogi Y Minami Y Yushita H Kanetake Y Saito 1993 Prostate specific antigen and prostatic acid phosphatase immunoreactivity as prognostic indicators of advanced prostatic carcinoma The Journal of Urology 149 1020 1023 7683340
    • (1993) The Journal of Urology , vol.149 , pp. 1020-1023
    • Sakai, H.1    Yogi, Y.2    Minami, Y.3    Yushita, Y.4    Kanetake, H.5    Saito, Y.6
  • 154
    • 0033555967 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase associated with prostate cancer progression
    • 9927031
    • D Gioeli JW Mandell GR Petroni HF Frierson Jr MJ Weber 1999 Activation of mitogen-activated protein kinase associated with prostate cancer progression Cancer Research 59 279 284 9927031
    • (1999) Cancer Research , vol.59 , pp. 279-284
    • Gioeli, D.1    Mandell, J.W.2    Petroni, G.R.3    Frierson Jr, H.F.4    Weber, M.J.5
  • 156
    • 0037421969 scopus 로고    scopus 로고
    • ErbB2 signaling is involved in regulating PSA secretion in androgen-independent human prostate cancer LNCaP C-81 cells
    • 12569372
    • MS Lee T Igawa TC Yuan XQ Zhang FF Lin MF Lin 2003 ErbB2 signaling is involved in regulating PSA secretion in androgen-independent human prostate cancer LNCaP C-81 cells Oncogene 22 781 796 12569372
    • (2003) Oncogene , vol.22 , pp. 781-796
    • Lee, M.S.1    Igawa, T.2    Yuan, T.C.3    Zhang, X.Q.4    Lin, F.F.5    Lin, M.F.6


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