메뉴 건너뛰기




Volumn 31, Issue 6, 2012, Pages 716-727

A novel nuclear role for the Vav3 nucleotide exchange factor in androgen receptor coactivation in prostate cancer

Author keywords

androgen receptor; castration resistant prostate cancer; coactivator; guanine nucleotide exchange factor; pleckstrin homology; Vav3

Indexed keywords

ANDROGEN RECEPTOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PLECKSTRIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN VAV3; UNCLASSIFIED DRUG;

EID: 84856955553     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2011.273     Document Type: Article
Times cited : (43)

References (56)
  • 1
    • 0036755404 scopus 로고    scopus 로고
    • Androgen receptor as a target in androgen-independent prostate cancer
    • discussion 138-139
    • Balk SP. (2002). Androgen receptor as a target in androgen-independent prostate cancer. Urology 60: 132-138; discussion 138-139.
    • (2002) Urology , vol.60 , pp. 132-138
    • Balk, S.P.1
  • 2
    • 35148851505 scopus 로고    scopus 로고
    • Prolonged exposure to reduced levels of androgen accelerates prostate cancer progression in Nkx3.1; Pten mutant mice
    • DOI 10.1158/0008-5472.CAN-07-2887
    • Banach-Petrosky W, Jessen WJ, Ouyang X, Gao H, Rao J, Quinn J et al. (2007). Prolonged exposure to reduced levels of androgen accelerates prostate cancer progression in Nkx3.1; Pten mutant mice. Cancer Res 67: 9089-9096. (Pubitemid 47535894)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9089-9096
    • Banach-Petrosky, W.1    Jessen, W.J.2    Ouyang, X.3    Gao, H.4    Rao, J.5    Quinn, J.6    Aronow, B.J.7    Abate-Shen, C.8
  • 3
    • 0035966019 scopus 로고    scopus 로고
    • Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth
    • Bourguignon LY, Zhu H, Zhou B, Diedrich F, Singleton PA, Hung MC. (2001). Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth. J Biol Chem 276: 48679-48692.
    • (2001) J Biol Chem , vol.276 , pp. 48679-48692
    • Bourguignon, L.Y.1    Zhu, H.2    Zhou, B.3    Diedrich, F.4    Singleton, P.A.5    Hung, M.C.6
  • 4
    • 66349098157 scopus 로고    scopus 로고
    • Host deficiency in Vav2/3 guanine nucleotide exchange factors impairs tumor growth, survival, and angiogenesis in vivo
    • Brantley-Sieders DM, Zhuang G, Vaught D, Freeman T, Hwang Y, Hicks D et al. (2009). Host deficiency in Vav2/3 guanine nucleotide exchange factors impairs tumor growth, survival, and angiogenesis in vivo. Mol Cancer Res 7: 615-623.
    • (2009) Mol Cancer Res , vol.7 , pp. 615-623
    • Brantley-Sieders, D.M.1    Zhuang, G.2    Vaught, D.3    Freeman, T.4    Hwang, Y.5    Hicks, D.6
  • 5
    • 0035473464 scopus 로고    scopus 로고
    • Vav proteins, adaptors and cell signaling
    • DOI 10.1038/sj.onc.1204780
    • Bustelo XR. (2001). Vav proteins, adaptors and cell signaling. Oncogene 20: 6372-6381. (Pubitemid 32977845)
    • (2001) Oncogene , vol.20 , Issue.REV. ISS. 5 , pp. 6372-6381
    • Bustelo, X.R.1
  • 6
  • 8
    • 33749345249 scopus 로고    scopus 로고
    • Vav3 oncogene is overexpressed and regulates cell growth and androgen receptor activity in human prostate cancer
    • DOI 10.1210/me.2006-0048
    • Dong Z, Liu Y, Lu S, Wang A, Lee K, Wang LH et al. (2006). Vav3 oncogene is overexpressed and regulates cell growth and androgen receptor activity in human prostate cancer. Mol Endocrinol 20: 2315-2325. (Pubitemid 44496404)
    • (2006) Molecular Endocrinology , vol.20 , Issue.10 , pp. 2315-2325
    • Dong, Z.1    Liu, Y.2    Lu, S.3    Wang, A.4    Lee, K.5    Wang, L.-H.6    Revelo, M.7
  • 10
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • DOI 10.1126/science.275.5300.665
    • Franke TF, Kaplan DR, Cantley LC, Toker A. (1997). Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275: 665-668. (Pubitemid 27061333)
    • (1997) Science , vol.275 , Issue.5300 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 12
    • 8344226282 scopus 로고    scopus 로고
    • Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance
    • DOI 10.1016/j.molcel.2004.09.036, PII S109727650400588X
    • He B, Gampe Jr RT, Kole AJ, Hnat AT, Stanley TB, An G et al. (2004). Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol Cell 16: 425-438. (Pubitemid 39504796)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 425-438
    • He, B.1    Gampe Jr., R.T.2    Kole, A.J.3    Hnat, A.T.4    Stanley, T.B.5    An, G.6    Stewart, E.L.7    Kalman, R.I.8    Minges, J.T.9    Wilson, E.M.10
  • 13
    • 0033601249 scopus 로고    scopus 로고
    • Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH(2)-terminal domain
    • He B, Kemppainen JA, Voegel JJ, Gronemeyer H, Wilson EM. (1999). Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH(2)-terminal domain. J Biol Chem 274: 37219-37225.
    • (1999) J Biol Chem , vol.274 , pp. 37219-37225
    • He, B.1    Kemppainen, J.A.2    Voegel, J.J.3    Gronemeyer, H.4    Wilson, E.M.5
  • 14
    • 0037067766 scopus 로고    scopus 로고
    • 2- and COOH-terminal interaction
    • DOI 10.1074/jbc.M202809200
    • He B, Lee LW, Minges JT, Wilson EM. (2002). Dependence of selective gene activation on the androgen receptor NH2-and COOH-terminal interaction. J Biol Chem 277: 25631-25639. (Pubitemid 34951881)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25631-25639
    • He, B.1    Lee, L.W.2    Minges, J.T.3    Wilson, E.M.4
  • 15
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • DOI 10.1038/42750
    • Heery DM, Kalkhoven E, Hoare S, Parker MG. (1997). A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387: 733-736. (Pubitemid 27270617)
    • (1997) Nature , vol.387 , Issue.6634 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 17
    • 0344406838 scopus 로고    scopus 로고
    • The haematopoietic specific signal transducer Vav1 is expressed in a subset of human neuroblastomas
    • DOI 10.1002/path.1314
    • Hornstein I, Pikarsky E, Groysman M, Amir G, Peylan-Ramu N, Katzav S. (2003). The haematopoietic specific signal transducer Vav1 is expressed in a subset of human neuroblastomas. J Pathol 199: 526-533. (Pubitemid 36411229)
    • (2003) Journal of Pathology , vol.199 , Issue.4 , pp. 526-533
    • Hornstein, I.1    Pikarsky, E.2    Groysman, M.3    Amir, G.4    Peylan-Ramu, N.5    Katzav, S.6
  • 20
    • 0141978673 scopus 로고    scopus 로고
    • Comparative protein structure modeling by iterative alignment, model building and model assessment
    • DOI 10.1093/nar/gkg460
    • John B, Sali A. (2003). Comparative protein structure modeling by iterative alignment, model building and model assessment. Nucleic Acids Res 31: 3982-3992. (Pubitemid 37442277)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 3982-3992
    • John, B.1    Sali, A.2
  • 22
    • 0032847377 scopus 로고    scopus 로고
    • Structural basis for high-affinity phosphoinositide binding by pleckstrin homology domains
    • Lemmon MA. (1999). Structural basis for high-affinity phosphoinositide binding by pleckstrin homology domains. Biochem Soc Trans 27: 617-624.
    • (1999) Biochem Soc Trans , vol.27 , pp. 617-624
    • Lemmon, M.A.1
  • 23
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon MA. (2003). Phosphoinositide recognition domains. Traffic 4: 201-213.
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 24
    • 8744219635 scopus 로고    scopus 로고
    • Pleckstrin homology domains: Not just for phosphoinositides
    • Lemmon MA. (2004). Pleckstrin homology domains: not just for phosphoinositides. Biochem Soc Trans 32: 707-711.
    • (2004) Biochem Soc Trans , vol.32 , pp. 707-711
    • Lemmon, M.A..1
  • 25
    • 84872115717 scopus 로고    scopus 로고
    • Pleckstrin homology (PH) domains and phosphoinositides
    • Lemmon MA. (2007). Pleckstrin homology (PH) domains and phosphoinositides. Biochem Soc Symp 74: 81-93.
    • (2007) Biochem Soc Symp , vol.74 , pp. 81-93
    • Lemmon, M.A.1
  • 26
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon MA. (2008). Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9: 99-111.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 27
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon MA, Ferguson KM. (2000). Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem J 350 (Part 1): 1-18.
    • (2000) Biochem J , vol.350 , Issue.PART 1 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 28
    • 0034872365 scopus 로고    scopus 로고
    • Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides
    • DOI 10.1042/BST0290377
    • Lemmon MA, Ferguson KM. (2001). Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides. Biochem Soc Trans 29: 377-384. (Pubitemid 32783622)
    • (2001) Biochemical Society Transactions , vol.29 , Issue.4 , pp. 377-384
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 29
    • 0037138405 scopus 로고    scopus 로고
    • Pleckstrin homology domains and the cytoskeleton
    • DOI 10.1016/S0014-5793(01)03243-4, PII S0014579301032434
    • Lemmon MA, Ferguson KM, Abrams CS. (2002). Pleckstrin homology domains and the cytoskeleton. FEBS Lett 513: 71-76. (Pubitemid 34242981)
    • (2002) FEBS Letters , vol.513 , Issue.1 , pp. 71-76
    • Lemmon, M.A.1    Ferguson, K.M.2    Abrams, C.S.3
  • 30
    • 51049083823 scopus 로고    scopus 로고
    • Targeted overexpression of vav3 oncogene in prostatic epithelium induces nonbacterial prostatitis and prostate cancer
    • Liu Y, Mo JQ, Hu Q, Boivin G, Levin L, Lu S et al. (2008). Targeted overexpression of vav3 oncogene in prostatic epithelium induces nonbacterial prostatitis and prostate cancer. Cancer Res 68: 6396-6406.
    • (2008) Cancer Res , vol.68 , pp. 6396-6406
    • Liu, Y.1    Mo, J.Q.2    Hu, Q.3    Boivin, G.4    Levin, L.5    Lu, S.6
  • 31
    • 77149162686 scopus 로고    scopus 로고
    • The molecular mechanism of Vav3 oncogene on upregulation of androgen receptor activity in prostate cancer cells
    • Liu Y, Wu X, Dong Z, Lu S. (2010). The molecular mechanism of Vav3 oncogene on upregulation of androgen receptor activity in prostate cancer cells. Int J Oncol 36: 623-633.
    • (2010) Int J Oncol , vol.36 , pp. 623-633
    • Liu, Y.1    Wu, X.2    Dong, Z.3    Lu, S.4
  • 32
    • 0037894847 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav
    • DOI 10.1128/MCB.20.5.1678-1691.2000
    • Lopez-Lago M, Lee H, Cruz C, Movilla N, Bustelo XR. (2000). Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav. Mol Cell Biol 20: 1678-1691. (Pubitemid 30100187)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.5 , pp. 1678-1691
    • Lopez-Lago, M.1    Hyunmi, L.2    Cruz, C.3    Movilla, N.4    Bustelo, X.R.5
  • 33
    • 33746512473 scopus 로고    scopus 로고
    • Vav3, a Rho GTPase guanine nucleotide exchange factor, increases during progression to androgen independence in prostate cancer cells and potentiates androgen receptor transcriptional activity
    • Lyons LS, Burnstein KL. (2006). Vav3, a Rho GTPase guanine nucleotide exchange factor, increases during progression to androgen independence in prostate cancer cells and potentiates androgen receptor transcriptional activity. Mol Endocrinol 20: 1061-1072.
    • (2006) Mol Endocrinol , vol.20 , pp. 1061-1072
    • Lyons, L.S.1    Burnstein, K.L.2
  • 34
    • 40849113350 scopus 로고    scopus 로고
    • Ligand-independent activation of androgen receptors by Rho GTPase signaling in prostate cancer
    • DOI 10.1210/me.2007-0158
    • Lyons LS, Rao S, Balkan W, Faysal J, Maiorino CA, Burnstein KL. (2008). Ligand-independent activation of androgen receptors by Rho GTPase signaling in prostate cancer. Mol Endocrinol 22: 597-608. (Pubitemid 351397788)
    • (2008) Molecular Endocrinology , vol.22 , Issue.3 , pp. 597-608
    • Lyons, L.S.1    Rao, S.2    Balkan, W.3    Faysal, J.4    Maiorino, C.A.5    Burnstein, K.L.6
  • 35
    • 0041765784 scopus 로고    scopus 로고
    • Role of pleckstrin homology domain in regulating membrane targeting and metabolic function of insulin receptor substrate 3
    • DOI 10.1210/me.2001-0211
    • Maffucci T, Razzini G, Ingrosso A, Chen H, Iacobelli S, Sciacchitano S et al. (2003). Role of pleckstrin homology domain in regulating membrane targeting and metabolic function of insulin receptor substrate 3. Mol Endocrinol 17: 1568-1579. (Pubitemid 36930471)
    • (2003) Molecular Endocrinology , vol.17 , Issue.8 , pp. 1568-1579
    • Maffucci, T.1    Razzini, G.2    Ingrosso, A.3    Chen, H.4    Iacobelli, S.5    Sciacchitano, S.6    Quon, M.J.7    Falasca, M.8
  • 37
    • 78149435915 scopus 로고    scopus 로고
    • Bypass mechanisms of the androgen receptor pathway in therapy-resistant prostate cancer cell models
    • Marques RB, Dits NF, Erkens-Schulze S, van Weerden WM, Jenster G. (2010). Bypass mechanisms of the androgen receptor pathway in therapy-resistant prostate cancer cell models. PLoS One 5: e13500.
    • (2010) PLoS One , vol.5
    • Marques, R.B.1    Dits, N.F.2    Erkens-Schulze, S.3    Van Weerden, W.M.4    Jenster, G.5
  • 39
    • 15444365135 scopus 로고    scopus 로고
    • Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor
    • Miller SL, DeMaria JE, Freier DO, Riegel AM, Clevenger CV. (2005). Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor. Mol Endocrinol 19: 939-949.
    • (2005) Mol Endocrinol , vol.19 , pp. 939-949
    • Miller, S.L.1    Demaria, J.E.2    Freier, D.O.3    Riegel, A.M.4    Clevenger, C.V.5
  • 41
    • 49249119358 scopus 로고    scopus 로고
    • Maintenance of intratumoral androgens in metastatic prostate cancer: A mechanism for castration-resistant tumor growth
    • Montgomery RB, Mostaghel EA, Vessella R, Hess DL, Kalhorn TF, Higano CS et al. (2008). Maintenance of intratumoral androgens in metastatic prostate cancer: a mechanism for castration-resistant tumor growth. Cancer Res 68: 4447-4454.
    • (2008) Cancer Res , vol.68 , pp. 4447-4454
    • Montgomery, R.B.1    Mostaghel, E.A.2    Vessella, R.3    Hess, D.L.4    Kalhorn, T.F.5    Higano, C.S.6
  • 42
    • 0032696592 scopus 로고    scopus 로고
    • Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins
    • Movilla N, Bustelo XR. (1999). Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins. Mol Cell Biol 19: 7870-7885. (Pubitemid 29493450)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.11 , pp. 7870-7885
    • Movilla, N.1    Bustelo, X.R.2
  • 43
    • 70350537033 scopus 로고    scopus 로고
    • Nuclear receptor coregulators in cancer biology
    • O'Malley BW, Kumar R. (2009). Nuclear receptor coregulators in cancer biology. Cancer Res 69: 8217-8222.
    • (2009) Cancer Res , vol.69 , pp. 8217-8222
    • O'Malley, B.W.1    Kumar, R.2
  • 45
    • 0037131365 scopus 로고    scopus 로고
    • Critical role of the pleckstrin homology and cysteine-rich domains in Vav signaling and transforming activity
    • DOI 10.1074/jbc.M202641200
    • Palmby TR, Abe K, Der CJ. (2002). Critical role of the pleckstrin homology and cysteine-rich domains in Vav signaling and transforming activity. J Biol Chem 277: 39350-39359. (Pubitemid 35190908)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39350-39359
    • Palmby, T.R.1    Abe, K.2    Der, C.J.3
  • 46
    • 34447341463 scopus 로고    scopus 로고
    • Persistent activation of Rac1 in squamous carcinomas of the head and neck: Evidence for an EGFR/Vav2 signaling axis involved in cell invasion
    • DOI 10.1093/carcin/bgm008
    • Patel V, Rosenfeldt HM, Lyons R, Servitja JM, Bustelo XR, Siroff M et al. (2007). Persistent activation of Rac1 in squamous carcinomas of the head and neck: evidence for an EGFR/Vav2 signaling axis involved in cell invasion. Carcinogenesis 28: 1145-1152. (Pubitemid 47062672)
    • (2007) Carcinogenesis , vol.28 , Issue.6 , pp. 1145-1152
    • Patel, V.1    Rosenfeldt, H.M.2    Lyons, R.3    Servitja, J.-M.4    Bustelo, X.R.5    Siroff, M.6    Gutkind, J.S.7
  • 47
    • 46449113353 scopus 로고    scopus 로고
    • Crucial structural role for the PH and C1 domains of the Vav1 exchange factor
    • DOI 10.1038/embor.2008.80, PII EMBOR200880
    • Rapley J, Tybulewicz VL, Rittinger K. (2008). Crucial structural role for the PH and C1 domains of the Vav1 exchange factor. EMBO Rep 9: 655-661. (Pubitemid 351927686)
    • (2008) EMBO Reports , vol.9 , Issue.7 , pp. 655-661
    • Rapley, J.1    Tybulewicz, V.L.J.2    Rittinger, K.3
  • 48
    • 1942502336 scopus 로고    scopus 로고
    • The coactivator LXXLL nuclear receptor recognition motif
    • DOI 10.1111/j.1399-3011.2004.00126.x
    • Savkur RS, Burris TP. (2004). The coactivator LXXLL nuclear receptor recognition motif. J Pept Res 63: 207-212. (Pubitemid 38496672)
    • (2004) Journal of Peptide Research , vol.63 , Issue.3 , pp. 207-212
    • Savkur, R.S.1    Burris, T.P.2
  • 49
    • 70350441994 scopus 로고    scopus 로고
    • Effects of the 5 alpha-reductase inhibitor dutasteride on gene expression in prostate cancer xenografts
    • Schmidt LJ, Regan KM, Anderson SK, Sun Z, Ballman KV, Tindall DJ. (2009). Effects of the 5 alpha-reductase inhibitor dutasteride on gene expression in prostate cancer xenografts. Prostate 69: 1730-1743.
    • (2009) Prostate , vol.69 , pp. 1730-1743
    • Schmidt, L.J.1    Regan, K.M.2    Anderson, S.K.3    Sun, Z.4    Ballman, K.V.5    Tindall, D.J.6
  • 51
    • 22844437980 scopus 로고    scopus 로고
    • State of research for prostate cancer: Excerpt from the report of the Prostate Cancer Progress Review Group
    • Tindall DJ, Scardino PJ. (2001). State of research for prostate cancer: excerpt from the report of the Prostate Cancer Progress Review Group. Urology 57: 28-30.
    • (2001) Urology , vol.57 , pp. 28-30
    • Tindall, D.J.1    Scardino, P.J.2
  • 52
    • 0034615581 scopus 로고    scopus 로고
    • Major transcript variants of VAV3, a new member of the VAV family of guanine nucleotide exchange factors
    • DOI 10.1016/S0378-1119(00)00026-3, PII S0378111900000263
    • Trenkle T, McClelland M, Adlkofer K, Welsh J. (2000). Major transcript variants of VAV3, a new member of the VAV family of guanine nucleotide exchange factors. Gene 245: 139-149. (Pubitemid 30125373)
    • (2000) Gene , vol.245 , Issue.1 , pp. 139-149
    • Trenkle, T.1    McClelland, M.2    Adlkofer, K.3    Welsh, J.4
  • 53
    • 27844469655 scopus 로고    scopus 로고
    • 3 suggest their interaction with protein binding partners
    • DOI 10.1242/jcs.02606
    • Varnai P, Bondeva T, Tamas P, Toth B, Buday L, Hunyady L et al. (2005). Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners. J Cell Sci 118: 4879-4888. (Pubitemid 41646394)
    • (2005) Journal of Cell Science , vol.118 , Issue.20 , pp. 4879-4888
    • Varni, P.1    Bondeva, T.2    Tamas, P.3    Toth, B.4    Buday, L.5    Hunyady, L.6    Balla, T.7
  • 54
    • 24044540381 scopus 로고    scopus 로고
    • Spatial and temporal recruitment of androgen receptor and its coactivators involves chromosomal looping and polymerase tracking
    • DOI 10.1016/j.molcel.2005.07.018, PII S1097276505015066
    • Wang Q, Carroll JS, Brown M. (2005). Spatial and temporal recruitment of androgen receptor and its coactivators involves chromosomal looping and polymerase tracking. Mol cell 19: 631-642. (Pubitemid 41219439)
    • (2005) Molecular Cell , vol.19 , Issue.5 , pp. 631-642
    • Wang, Q.1    Carroll, J.S.2    Brown, M.3
  • 55
    • 77950367603 scopus 로고    scopus 로고
    • N-terminal PH domain and C-terminal auto-inhibitory region of CKIP-1 coordinate to determine its nucleus-plasma membrane shuttling
    • Xi S, Tie Y, Lu K, Zhang M, Yin X, Chen J et al. (2010). N-terminal PH domain and C-terminal auto-inhibitory region of CKIP-1 coordinate to determine its nucleus-plasma membrane shuttling. FEBS Lett 584: 1223-1230.
    • (2010) FEBS Lett , vol.584 , pp. 1223-1230
    • Xi, S.1    Tie, Y.2    Lu, K.3    Zhang, M.4    Yin, X.5    Chen, J.6
  • 56
    • 0034461581 scopus 로고    scopus 로고
    • Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation
    • DOI 10.1128/MCB.20.24.9212-9224.2000
    • Zeng L, Sachdev P, Yan L, Chan JL, Trenkle T, McClelland M et al. (2000). Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation. Mol Cell Biol 20: 9212-9224. (Pubitemid 32246108)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.24 , pp. 9212-9224
    • Zeng, L.1    Sachdev, P.2    Yan, L.3    Chan, J.L.4    Trenkle, T.5    McClelland, M.6    Welsh, J.7    Wang, L.-H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.