메뉴 건너뛰기




Volumn 68, Issue , 2014, Pages 268-277

The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation

Author keywords

Cysteine oxidation; Free radicals; Mitochondria; PDGF; Protein tyrosine phosphatase

Indexed keywords

P66SHC PROTEIN; PLATELET DERIVED GROWTH FACTOR; PROTEIN; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84892388139     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.12.022     Document Type: Article
Times cited : (38)

References (66)
  • 4
    • 0032554630 scopus 로고    scopus 로고
    • 5R(S/T) in protein-tyrosine phosphatases
    • DOI 10.1021/bi971187i
    • G.H. Peters, T.M. Frimurer, and O.H. Olsen Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases Biochemistry 37 1998 5383 5393 (Pubitemid 28241919)
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5383-5393
    • Peters, G.H.1    Frimurer, T.M.2    Olsen, O.H.3
  • 5
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    • DOI 10.1038/370571a0
    • J.A. Stuckey, H.L. Schubert, E.B. Fauman, Z.Y. Zhang, J.E. Dixon, and M.A. Saper Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate Nature 370 1994 571 575 (Pubitemid 24264925)
    • (1994) Nature , vol.370 , Issue.6490 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.-Y.4    Dixon, J.E.5    Saper, M.A.6
  • 6
    • 0027383705 scopus 로고
    • Active site labeling of the Yersinia protein tyrosine phosphatase: The determination of the pK(a) of the active site cysteine and the function of the conserved histidine 402
    • Z.Y. Zhang, and J.E. Dixon Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402 Biochemistry 32 1993 9340 9345 (Pubitemid 23292052)
    • (1993) Biochemistry , vol.32 , Issue.36 , pp. 9340-9345
    • Zhang, Z.-Y.1    Dixon, J.E.2
  • 7
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286 (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 8
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • DOI 10.1021/bi973035t
    • J.M. Denu, and K.G. Tanner Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation Biochemistry 37 1998 5633 5642 (Pubitemid 28241948)
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 9
    • 33750620971 scopus 로고    scopus 로고
    • Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine
    • DOI 10.1515/BC.2006.175, PII BCHM38710111399
    • C. von Montfort, V.S. Sharov, S. Metzger, C. Schoneich, H. Sies, and L.O. Klotz Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine Biol. Chem. 387 2006 1399 1404 (Pubitemid 44691420)
    • (2006) Biological Chemistry , vol.387 , Issue.10-11 , pp. 1399-1404
    • Von Montfort, C.1    Sharov, V.S.2    Metzger, S.3    Schoneich, C.4    Sies, H.5    Klotz, L.-O.6
  • 13
    • 84880275000 scopus 로고    scopus 로고
    • Thiol-dependent recovery of catalytic activity from oxidized protein tyrosine phosphatases
    • Z.D. Parsons, and K.S. Gates Thiol-dependent recovery of catalytic activity from oxidized protein tyrosine phosphatases Biochemistry 52 2013 6412 6423
    • (2013) Biochemistry , vol.52 , pp. 6412-6423
    • Parsons, Z.D.1    Gates, K.S.2
  • 14
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • DOI 10.1074/jbc.273.25.15366
    • S.R. Lee, K.S. Kwon, S.R. Kim, and S.G. Rhee Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor J. Biol. Chem. 273 1998 15366 15372 (Pubitemid 28298140)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15366-15372
    • Lee, S.-R.1    Kwont, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 17
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • DOI 10.1016/S1097-2765(02)00445-8
    • T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo Mol. Cell 9 2002 387 399 (Pubitemid 34195563)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 387-399
    • Meng, T.-C.1    Fukada, T.2    Tonks, N.K.3
  • 18
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • P. Chiarugi, T. Fiaschi, M.L. Taddei, D. Talini, E. Giannoni, G. Raugei, and G. Ramponi Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation J. Biol. Chem. 276 2001 33478 33487
    • (2001) J. Biol. Chem. , vol.276 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5    Raugei, G.6    Ramponi, G.7
  • 19
    • 4444233558 scopus 로고    scopus 로고
    • Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B
    • DOI 10.1074/jbc.M404606200
    • T.C. Meng, D.A. Buckley, S. Galic, T. Tiganis, and N.K. Tonks Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B J. Biol. Chem. 279 2004 37716 37725 (Pubitemid 39195485)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37716-37725
    • Meng, T.-C.1    Buckley, D.A.2    Galic, S.3    Tiganis, T.4    Tonks, N.K.5
  • 20
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • K. Mahadev, A. Zilbering, L. Zhu, and B.J. Goldstein Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade J. Biol. Chem. 276 2001 21938 21942
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 23
    • 84898416421 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase oxidation in cell adhesion and migration
    • Epub ahead of print
    • Frijhoff, J.; Dagnell, M.; Godfrey R.; Ostman, A. Regulation of protein tyrosine phosphatase oxidation in cell adhesion and migration, Antioxid Redox Signaling, Epub ahead of print, http://dx.doi.org/10.1089/ars.2013.5643
    • Antioxid Redox Signaling
    • Frijhoff, J.1    Dagnell, M.2    Godfrey, R.3    Ostman, A.4
  • 26
    • 84872188607 scopus 로고    scopus 로고
    • S-glutathionylation of LMW-PTP regulates VEGF-mediated FAK activation and endothelial cell migration
    • M.A. Abdelsaid, and A.B. El-Remessy S-glutathionylation of LMW-PTP regulates VEGF-mediated FAK activation and endothelial cell migration J. Cell Sci 125 Pt 20 2012 4751 4760
    • (2012) J. Cell Sci , vol.125 , Issue.PART 20 , pp. 4751-4760
    • Abdelsaid, M.A.1    El-Remessy, A.B.2
  • 29
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • DOI 10.1083/jcb.200709049
    • K. Chen, M.T. Kirber, H. Xiao, Y. Yang, and J.F. Keaney Jr. Regulation of ROS signal transduction by NADPH oxidase 4 localization J. Cell Biol. 181 2008 1129 1139 (Pubitemid 351915488)
    • (2008) Journal of Cell Biology , vol.181 , Issue.7 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney Jr., J.F.5
  • 30
    • 79953881843 scopus 로고    scopus 로고
    • J.D. Lambeth; A.M. Shah; F. Morel; R.P. Brandes, the E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4
    • I. Takac, K. Schroder, L. Zhang, B. Lardy, and N. Anilkumar J.D. Lambeth; A.M. Shah; F. Morel; R.P. Brandes, The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4 J. Biol. Chem. 286 2011 13304 13313
    • (2011) J. Biol. Chem. , vol.286 , pp. 13304-13313
    • Takac, I.1    Schroder, K.2    Zhang, L.3    Lardy, B.4    Anilkumar, N.5
  • 31
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • J.D. Lambeth NOX enzymes and the biology of reactive oxygen Nat. Rev. Immunol. 4 2004 181 189 (Pubitemid 38339084)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.3 , pp. 181-189
    • Lambeth, J.D.1
  • 37
    • 67649243697 scopus 로고    scopus 로고
    • The cardioprotective effects elicited by p66(Shc) ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury
    • Carpi, A.; R. Menabo; N. Kaludercic; P. Pelicci; F. Di Lisa; M. Giorgio, The cardioprotective effects elicited by p66(Shc) ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury. Biochim. Biophys. Acta1787774-7802009.
    • Biochim. Biophys. Acta1787774-7802009
    • Carpi, A.1    Menabo, R.2    Kaludercic, N.3    Pelicci, P.4    Di Lisa, F.5    Giorgio, M.6
  • 40
    • 84861608177 scopus 로고    scopus 로고
    • Reactive oxygen species induced by p66Shc longevity protein mediate nongenomic androgen action via tyrosine phosphorylation signaling to enhance tumorigenicity of prostate cancer cells
    • S. Veeramani, Y.W. Chou, F.C. Lin, S. Muniyan, F.F. Lin, S. Kumar, Y. Xie, S.M. Lele, Y. Tu, and M.F. Lin Reactive oxygen species induced by p66Shc longevity protein mediate nongenomic androgen action via tyrosine phosphorylation signaling to enhance tumorigenicity of prostate cancer cells Free Radic. Biol. Med. 53 2012 95 108
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 95-108
    • Veeramani, S.1    Chou, Y.W.2    Lin, F.C.3    Muniyan, S.4    Lin, F.F.5    Kumar, S.6    Xie, Y.7    Lele, S.M.8    Tu, Y.9    Lin, M.F.10
  • 41
    • 10644221359 scopus 로고    scopus 로고
    • Investigation of protein-tyrosine phosphatases by in-gel assays
    • DOI 10.1016/j.ymeth.2004.07.004, PII S1046202304001677
    • B. Markova, P. Gulati, P.A. Herrlich, and F.D. Bohmer Investigation of protein-tyrosine phosphatases by in-gel assays Methods 35 2005 22 27 (Pubitemid 39647575)
    • (2005) Methods , vol.35 , Issue.1 , pp. 22-27
    • Markova, B.1    Gulati, P.2    Herrlich, P.A.3    Bohmer, F.D.4
  • 43
    • 48249149472 scopus 로고    scopus 로고
    • A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells
    • B. Boivin, S. Zhang, J.L. Arbiser, Z.Y. Zhang, and N.K. Tonks A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells Proc. Natl. Acad. Sci. USA 105 2008 9959 9964
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9959-9964
    • Boivin, B.1    Zhang, S.2    Arbiser, J.L.3    Zhang, Z.Y.4    Tonks, N.K.5
  • 45
    • 0027179869 scopus 로고
    • The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp
    • A. Kazlauskas, G.S. Feng, T. Pawson, and M. Valius The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp Proc. Natl. Acad. Sci. USA 90 1993 6939 6943 (Pubitemid 23222363)
    • (1993) Proceedings of the National Academy of Sciences of the United States of America , vol.90 , Issue.15 , pp. 6939-6943
    • Kazlauskas, A.1    Feng, G.-S.2    Pawson, T.3    Valius, M.4
  • 46
    • 0032476646 scopus 로고    scopus 로고
    • Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant, negative mutant PTP1B
    • DOI 10.1083/jcb.143.3.861
    • C.O. Arregui, J. Balsamo, and J. Lilien Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B J. Cell Biol. 143 1998 861 873 (Pubitemid 28512577)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 861-873
    • Arregui, C.O.1    Balsamo, J.2    Lilien, J.3
  • 47
    • 84883696390 scopus 로고    scopus 로고
    • Regulation of the Src kinase-associated phosphoprotein 55 homologue by the protein tyrosine phosphatase PTP-PEST in the control of cell motility
    • E. Ayoub, A. Hall, A.M. Scott, M.M. Chagnon, G. Miquel, M. Halle, M. Noda, A. Bikflavi, and M.L. Tremblay Regulation of the Src kinase-associated phosphoprotein 55 homologue by the protein tyrosine phosphatase PTP-PEST in the control of cell motility J. Biol. Chem. 288 2013 25739 25748
    • (2013) J. Biol. Chem. , vol.288 , pp. 25739-25748
    • Ayoub, E.1    Hall, A.2    Scott, A.M.3    Chagnon, M.M.4    Miquel, G.5    Halle, M.6    Noda, M.7    Bikflavi, A.8    Tremblay, M.L.9
  • 48
    • 84878001153 scopus 로고    scopus 로고
    • PTP1B promotes focal complex maturation, lamellar persistence and directional migration
    • J.E. Burdisso, A. Gonzalez, and C.O. Arregui PTP1B promotes focal complex maturation, lamellar persistence and directional migration J. Cell Sci. 126 Pt 8 2013 1820 1831
    • (2013) J. Cell Sci. , vol.126 , Issue.PARTT 8 , pp. 1820-1831
    • Burdisso, J.E.1    Gonzalez, A.2    Arregui, C.O.3
  • 49
    • 0141865507 scopus 로고    scopus 로고
    • Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • DOI 10.1093/emboj/cdg492
    • G. von Wichert, B. Haimovich, G.S. Feng, and M.P. Sheetz Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2 EMBO J. 22 2003 5023 5035 (Pubitemid 37222023)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 5023-5035
    • Von Wichert, G.1    Haimovich, B.2    Feng, G.-S.3    Sheetz, M.P.4
  • 50
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • DOI 10.1074/jbc.273.33.21125
    • D.H. Yu, C.K. Qu, O. Henegariu, X. Lu, and G.S. Feng Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion J. Biol. Chem. 273 1998 21125 21131 (Pubitemid 28385400)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 21125-21131
    • Yu, D.-H.1    Qu, C.-K.2    Henegariu, O.3    Lu, X.4    Feng, G.-S.5
  • 52
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • S.G. Rhee, H.A. Woo, I.S. Kil, and S.H. Bae Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides J. Biol. Chem. 287 2012 4403 4410
    • (2012) J. Biol. Chem. , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 53
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • J. Nunnari, and A. Suomalainen Mitochondria: in sickness and in health Cell 148 2012 1145 1159
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 54
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 55
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • DOI 10.1016/j.cmet.2005.05.001, PII S1550413105001397
    • R.D. Guzy, B. Hoyos, E. Robin, H. Chen, L. Liu, K.D. Mansfield, M.C. Simon, U. Hammerling, and P.T. Schumacker Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing Cell Metab. 1 2005 401 408 (Pubitemid 43960623)
    • (2005) Cell Metabolism , vol.1 , Issue.6 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3    Chen, H.4    Liu, L.5    Mansfield, K.D.6    Simon, M.C.7    Hammerling, U.8    Schumacker, P.T.9
  • 58
    • 0027506762 scopus 로고
    • Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively
    • M. Valius, C. Bazenet, and A. Kazlauskas Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectively Mol. Cell. Biol 13 1993 133 143 (Pubitemid 23006891)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.1 , pp. 133-143
    • Valius, M.1    Bazenet, C.2    Kazlauskas, A.3
  • 59
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • DOI 10.1038/361315a0
    • M.J. Berridge Inositol trisphosphate and calcium signalling Nature 361 1993 315 325 (Pubitemid 23041621)
    • (1993) Nature , vol.361 , Issue.6410 , pp. 315-325
    • Berridge, M.J.1
  • 60
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor β
    • R.J. Lechleider, S. Sugimoto, A.M. Bennett, A.S. Kashishian, J.A. Cooper, S.E. Shoelson, C.T. Walsh, and B.G. Neel Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor J. Biol. Chem. 268 1993 21478 21481 (Pubitemid 23320630)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.29 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 61
    • 0033600129 scopus 로고    scopus 로고
    • SHP-2 binds to Tyr763 and Tyr1009 in the PDGF β-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis
    • DOI 10.1038/sj.onc.1202705
    • L. Ronnstrand, A.K. Arvidsson, A. Kallin, C. Rorsman, U. Hellman, U. Engstrom, C. Wernstedt, and C.H. Heldin SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis Oncogene 18 1999 3696 3702 (Pubitemid 29338502)
    • (1999) Oncogene , vol.18 , Issue.25 , pp. 3696-3702
    • Ronnstrand, L.1    Arvidsson, A.-K.2    Kallin, A.3    Rorsman, C.4    Hellman, U.5    Engstrom, U.6    Wernstedt, C.7    Heldin, C.-H.8
  • 63
    • 50649099634 scopus 로고    scopus 로고
    • P66shc negatively regulates insulin-like growth factor i signal transduction via inhibition of p52shc binding to Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 leading to impaired growth factor receptor-bound protein-2 membrane recruitment
    • G. Xi, X. Shen, and D.R. Clemmons p66shc negatively regulates insulin-like growth factor I signal transduction via inhibition of p52shc binding to Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 leading to impaired growth factor receptor-bound protein-2 membrane recruitment Mol. Endocrinol 22 2008 2162 2175
    • (2008) Mol. Endocrinol , vol.22 , pp. 2162-2175
    • Xi, G.1    Shen, X.2    Clemmons, D.R.3
  • 64
    • 84877290780 scopus 로고    scopus 로고
    • Mitochondrial localization and the persistent migration of epithelial cancer cells
    • S.P. Desai, S.N. Bhatia, M. Toner, and D. Irimia Mitochondrial localization and the persistent migration of epithelial cancer cells Biophys. J. 104 2013 2077 2088
    • (2013) Biophys. J. , vol.104 , pp. 2077-2088
    • Desai, S.P.1    Bhatia, S.N.2    Toner, M.3    Irimia, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.