메뉴 건너뛰기




Volumn 15, Issue 2-3, 2015, Pages 300-309

Emerging roles of post-translational modifications in signal transduction and angiogenesis

Author keywords

Acetylation; Cell biology; Glycosylation; Phosphorylation; Tandem mass spectrometry; VEGF receptor

Indexed keywords

ARGININE; IMMUNOGLOBULIN; LYSINE; PROTEIN KINASE; SERINE; THREONINE; VASCULOTROPIN RECEPTOR 2;

EID: 84921352104     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400183     Document Type: Review
Times cited : (44)

References (63)
  • 1
    • 32944463899 scopus 로고    scopus 로고
    • Angiogenesis
    • Folkman, J., Angiogenesis. Ann. Rev. Med. 2006, 57, 1-18.
    • (2006) Ann. Rev. Med. , vol.57 , pp. 1-18
    • Folkman, J.1
  • 2
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • Carmeliet, P., Angiogenesis in life, disease and medicine. Nature 2005, 438, 932-936.
    • (2005) Nature , vol.438 , pp. 932-936
    • Carmeliet, P.1
  • 3
    • 60649116477 scopus 로고    scopus 로고
    • Silencing or fueling metastasis with VEGF inhibitors: antiangiogenesis revisited
    • Loges, S., Mazzone, M., Hohensinner, P., Carmeliet, P., Silencing or fueling metastasis with VEGF inhibitors: antiangiogenesis revisited. Cancer Cell 2009, 15, 167-170.
    • (2009) Cancer Cell , vol.15 , pp. 167-170
    • Loges, S.1    Mazzone, M.2    Hohensinner, P.3    Carmeliet, P.4
  • 4
    • 60649106195 scopus 로고    scopus 로고
    • Antiangiogenic therapy elicits malignant progression of tumors to increased local invasion and distant metastasis
    • Paez-Ribes, M., Allen, E., Hudock, J., Takeda, T. et al., Antiangiogenic therapy elicits malignant progression of tumors to increased local invasion and distant metastasis. Cancer Cell 2009, 15, 220-231.
    • (2009) Cancer Cell , vol.15 , pp. 220-231
    • Paez-Ribes, M.1    Allen, E.2    Hudock, J.3    Takeda, T.4
  • 5
    • 84881232071 scopus 로고    scopus 로고
    • Recent molecular discoveries in angiogenesis and antiangiogenic therapies in cancer
    • Welti, J., Loges, S., Dimmeler, S., Carmeliet, P., Recent molecular discoveries in angiogenesis and antiangiogenic therapies in cancer. J. Clin. Invest. 2013, 123, 3190-3200.
    • (2013) J. Clin. Invest. , vol.123 , pp. 3190-3200
    • Welti, J.1    Loges, S.2    Dimmeler, S.3    Carmeliet, P.4
  • 6
    • 60649087564 scopus 로고    scopus 로고
    • Accelerated metastasis after short-term treatment with a potent inhibitor of tumor angiogenesis
    • Ebos, J. M., Lee, C. R., Cruz-Munoz, W., Bjarnason, G. A. et al., Accelerated metastasis after short-term treatment with a potent inhibitor of tumor angiogenesis. Cancer Cell. 2009, 15, 232-239.
    • (2009) Cancer Cell. , vol.15 , pp. 232-239
    • Ebos, J.M.1    Lee, C.R.2    Cruz-Munoz, W.3    Bjarnason, G.A.4
  • 7
    • 84863718886 scopus 로고    scopus 로고
    • Differential drug class-specific metastatic effects following treatment with a panel of angiogenesis inhibitors
    • Chung, A. S., Kowanetz, M., Wu, X., Zhuang, G. et al., Differential drug class-specific metastatic effects following treatment with a panel of angiogenesis inhibitors. J. Pathol. 2012, 227, 404-416.
    • (2012) J. Pathol. , vol.227 , pp. 404-416
    • Chung, A.S.1    Kowanetz, M.2    Wu, X.3    Zhuang, G.4
  • 8
    • 84863691378 scopus 로고    scopus 로고
    • Modeling and predicting clinical efficacy for drugs targeting the tumor milieu
    • Singh, M., Ferrara, N., Modeling and predicting clinical efficacy for drugs targeting the tumor milieu. Nat. Biotechnol. 2012, 30, 648-657.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 648-657
    • Singh, M.1    Ferrara, N.2
  • 9
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A., Schlessinger, J., Cell signaling by receptor tyrosine kinases. Cell 2010, 141, 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 10
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams, D. B., Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci. 2006, 119, 615-623.
    • (2006) J. Cell Sci. , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 11
    • 0035877708 scopus 로고    scopus 로고
    • Kinase insert domain receptor (KDR) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling
    • Tao, Q., Backer, M. V., Backer, J. M., Terman, B. I., Kinase insert domain receptor (KDR) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling. J. Biol. Chem. 2001, 276, 21916-21923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21916-21923
    • Tao, Q.1    Backer, M.V.2    Backer, J.M.3    Terman, B.I.4
  • 12
    • 83755162608 scopus 로고    scopus 로고
    • The antifungal drug itraconazole inhibits vascular endothelial growth factor receptor 2 (VEGFR2) glycosylation, trafficking, and signaling in endothelial cells
    • Nacev, B. A., Grassi, P., Dell, A., Haslam, S. M. et al., The antifungal drug itraconazole inhibits vascular endothelial growth factor receptor 2 (VEGFR2) glycosylation, trafficking, and signaling in endothelial cells. J. Biol. Chem. 2011, 286, 44045-44056.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44045-44056
    • Nacev, B.A.1    Grassi, P.2    Dell, A.3    Haslam, S.M.4
  • 13
    • 0031008750 scopus 로고    scopus 로고
    • The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLC-gamma pathway and partially induces mitotic signals in NIH3T3 fibroblasts
    • Takahashi, T, Shibuya, M, The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLC-gamma pathway and partially induces mitotic signals in NIH3T3 fibroblasts. Oncogene 1997, 14, 2079-2089.
    • (1997) Oncogene , vol.14 , pp. 2079-2089
    • Takahashi, T.1    Shibuya, M.2
  • 14
    • 84881402357 scopus 로고    scopus 로고
    • Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2
    • Srinivasan, S, Meyer, R. D., Lugo, R., Rahimi, N., Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2. J. Biol. Chem. 2013, 288, 23171-23181.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23171-23181
    • Srinivasan, S.1    Meyer, R.D.2    Lugo, R.3    Rahimi, N.4
  • 15
    • 0033602091 scopus 로고    scopus 로고
    • Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization
    • Dougher, M, Terman, B. I., Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization. Oncogene 1999, 18, 1619-1627.
    • (1999) Oncogene , vol.18 , pp. 1619-1627
    • Dougher, M.1    Terman, B.I.2
  • 16
    • 57349159403 scopus 로고    scopus 로고
    • IQGAP1-dependent signaling pathway regulates endothelial cell proliferation and angiogenesis
    • Meyer, R. D., Sacks, D. B., Rahimi, N., IQGAP1-dependent signaling pathway regulates endothelial cell proliferation and angiogenesis. PloS One 2008, 3, e3848.
    • (2008) PloS One , vol.3 , pp. e3848
    • Meyer, R.D.1    Sacks, D.B.2    Rahimi, N.3
  • 17
    • 22744447871 scopus 로고    scopus 로고
    • VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis
    • Matsumoto, T., Bohman, S., Dixelius, J., Berge, T. et al., VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis. EMBO J. 2005, 24, 2342-2353.
    • (2005) EMBO J. , vol.24 , pp. 2342-2353
    • Matsumoto, T.1    Bohman, S.2    Dixelius, J.3    Berge, T.4
  • 18
    • 16344380942 scopus 로고    scopus 로고
    • The carboxyl terminus of VEGFR-2 is required for PKC-mediated down-regulation
    • Singh, A. J., Meyer, R. D., Band, H., Rahimi, N., The carboxyl terminus of VEGFR-2 is required for PKC-mediated down-regulation. Mol. Biol. Cell. 2005, 16, 2106-2118.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 2106-2118
    • Singh, A.J.1    Meyer, R.D.2    Band, H.3    Rahimi, N.4
  • 19
    • 0346422442 scopus 로고    scopus 로고
    • The carboxyl terminus controls ligand-dependent activation of VEGFR-2 and its signaling
    • Meyer, R. D., Singh, A. J., Rahimi, N., The carboxyl terminus controls ligand-dependent activation of VEGFR-2 and its signaling. J. Bio. Chem. 2004, 279, 735-742.
    • (2004) J. Bio. Chem. , vol.279 , pp. 735-742
    • Meyer, R.D.1    Singh, A.J.2    Rahimi, N.3
  • 20
    • 34248385248 scopus 로고    scopus 로고
    • A critical role for the E3-ligase activity of c-Cbl in VEGFR-2-mediated PLCgamma1 activation and angiogenesis
    • Singh, A. J., Meyer, R. D., Navruzbekov, G., Shelke, R. et al., A critical role for the E3-ligase activity of c-Cbl in VEGFR-2-mediated PLCgamma1 activation and angiogenesis. Proc. Natl. Acad. Sci. USA 2007, 104, 5413-5418.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5413-5418
    • Singh, A.J.1    Meyer, R.D.2    Navruzbekov, G.3    Shelke, R.4
  • 21
    • 84864292241 scopus 로고    scopus 로고
    • VEGFR2 induces c-Src signaling and vascular permeability in vivo via the adaptor protein TSAd
    • Sun, Z., Li, X., Massena, S., Kutschera, S. et al., VEGFR2 induces c-Src signaling and vascular permeability in vivo via the adaptor protein TSAd. J. Exp. Med. 2012, 209, 1363-1377.
    • (2012) J. Exp. Med. , vol.209 , pp. 1363-1377
    • Sun, Z.1    Li, X.2    Massena, S.3    Kutschera, S.4
  • 22
    • 84885136080 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking
    • Subramani, J., Ghosh, M., Rahman, M. M., Caromile, L. A. et al., Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking. J. Immunol. 2013, 191, 3905-3912.
    • (2013) J. Immunol. , vol.191 , pp. 3905-3912
    • Subramani, J.1    Ghosh, M.2    Rahman, M.M.3    Caromile, L.A.4
  • 23
    • 12844264070 scopus 로고    scopus 로고
    • Essential role of Flk-1 (VEGF receptor 2) tyrosine residue 1173 in vasculogenesis in mice
    • Sakurai, Y., Ohgimoto, K., Kataoka, Y., Yoshida, N. et al., Essential role of Flk-1 (VEGF receptor 2) tyrosine residue 1173 in vasculogenesis in mice. Proc. Natl. Acad. Sci. USA 2005, 102, 1076-1081.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1076-1081
    • Sakurai, Y.1    Ohgimoto, K.2    Kataoka, Y.3    Yoshida, N.4
  • 24
    • 0035947584 scopus 로고    scopus 로고
    • Identification of tyrosine residues in vascular endothelial growth factor receptor-2/FLK-1 involved in activation of phosphatidylinositol 3-kinase and cell proliferation
    • Dayanir, V., Meyer, R. D., Lashkari, K., Rahimi, N., Identification of tyrosine residues in vascular endothelial growth factor receptor-2/FLK-1 involved in activation of phosphatidylinositol 3-kinase and cell proliferation. J. Biol. Chem. 2001, 276, 17686-17692.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17686-17692
    • Dayanir, V.1    Meyer, R.D.2    Lashkari, K.3    Rahimi, N.4
  • 25
    • 2542455474 scopus 로고    scopus 로고
    • The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration
    • Holmqvist, K., Cross, M. J., Rolny, C., Hagerkvist, R. et al., The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration. J. Biol. Chem. 2004, 279, 22267-22275.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22267-22275
    • Holmqvist, K.1    Cross, M.J.2    Rolny, C.3    Hagerkvist, R.4
  • 26
    • 0038460230 scopus 로고    scopus 로고
    • Recruitment and activation of phospholipase Cgamma1 by vascular endothelial growth factor receptor-2 are required for tubulogenesis and differentiation of endothelial cells
    • Meyer, R. D., Latz, C., Rahimi, N., Recruitment and activation of phospholipase Cgamma1 by vascular endothelial growth factor receptor-2 are required for tubulogenesis and differentiation of endothelial cells. J. Biol. Chem. 2003, 278, 16347-16355.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16347-16355
    • Meyer, R.D.1    Latz, C.2    Rahimi, N.3
  • 28
    • 33144459287 scopus 로고    scopus 로고
    • VEGFR-1 and VEGFR-2: two non-identical twins with a unique physiognomy
    • Rahimi, N., VEGFR-1 and VEGFR-2: two non-identical twins with a unique physiognomy. Front Biosci. 2006, 11, 818-829.
    • (2006) Front Biosci , vol.11 , pp. 818-829
    • Rahimi, N.1
  • 29
    • 79956098305 scopus 로고    scopus 로고
    • PEST motif serine and tyrosine phosphorylation controls vascular endothelial growth factor receptor 2 stability and downregulation
    • Meyer, R. D., Srinivasan, S., Singh, A. J., Mahoney, J. E. et al., PEST motif serine and tyrosine phosphorylation controls vascular endothelial growth factor receptor 2 stability and downregulation. Mol. Cell Biol. 2011, 31, 2010-2025.
    • (2011) Mol. Cell Biol. , vol.31 , pp. 2010-2025
    • Meyer, R.D.1    Srinivasan, S.2    Singh, A.J.3    Mahoney, J.E.4
  • 30
    • 84864296672 scopus 로고    scopus 로고
    • SCF(beta-TRCP) suppresses angiogenesis and thyroid cancer cell migration by promoting ubiquitination and destruction of VEGF receptor 2
    • Shaik, S., Nucera, C., Inuzuka, H., Gao, D. et al., SCF(beta-TRCP) suppresses angiogenesis and thyroid cancer cell migration by promoting ubiquitination and destruction of VEGF receptor 2. J. Exp. Med. 2012, 209, 1289-1307.
    • (2012) J. Exp. Med. , vol.209 , pp. 1289-1307
    • Shaik, S.1    Nucera, C.2    Inuzuka, H.3    Gao, D.4
  • 31
    • 20444385832 scopus 로고    scopus 로고
    • Activation of p38 has opposing effects on the proliferation and migration of endothelial cells
    • McMullen, M. E., Bryant, P. W., Glembotski, C. C., Vincent, P. A. et al., Activation of p38 has opposing effects on the proliferation and migration of endothelial cells. J. Biol. Chem. 2005, 280, 20995-21003.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20995-21003
    • McMullen, M.E.1    Bryant, P.W.2    Glembotski, C.C.3    Vincent, P.A.4
  • 32
    • 0037313641 scopus 로고    scopus 로고
    • p38 MAP kinase-a molecular switch between VEGF-induced angiogenesis and vascular hyperpermeability
    • Issbrucker, K., Marti, H. H., Hippenstiel, S., Springmann, G. et al., p38 MAP kinase-a molecular switch between VEGF-induced angiogenesis and vascular hyperpermeability. FASEB J. 2003, 17, 262-264.
    • (2003) FASEB J. , vol.17 , pp. 262-264
    • Issbrucker, K.1    Marti, H.H.2    Hippenstiel, S.3    Springmann, G.4
  • 33
    • 0035839556 scopus 로고    scopus 로고
    • Akt down-regulation of p38 signaling provides a novel mechanism of vascular endothelial growth factor-mediated cytoprotection in endothelial cells
    • Gratton, J. P., Morales-Ruiz, M., Kureishi, Y., Fulton, D. et al., Akt down-regulation of p38 signaling provides a novel mechanism of vascular endothelial growth factor-mediated cytoprotection in endothelial cells. J. Biol. Chem. 2001, 276, 30359-30365.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30359-30365
    • Gratton, J.P.1    Morales-Ruiz, M.2    Kureishi, Y.3    Fulton, D.4
  • 34
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford, M. T., Richard, S., Arginine methylation an emerging regulator of protein function. Mol. Cell. 2005, 18, 263-272.
    • (2005) Mol. Cell. , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 35
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • Huang, J., Berger, S. L., The emerging field of dynamic lysine methylation of non-histone proteins. Curr. Opin. Genet. Dev. 2008, 18, 152-158.
    • (2008) Curr. Opin. Genet. Dev , vol.18 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 36
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: the field of protein methylation
    • Paik, W. K., Paik, D. C., Kim, S., Historical review: the field of protein methylation. Trends Biochem. Sci. 2007, 32, 146-152.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 37
    • 1642284876 scopus 로고    scopus 로고
    • Automated identification of putative methyltransferases from genomic open reading frames
    • Katz, J. E., Dlakic, M, Clarke, S., Automated identification of putative methyltransferases from genomic open reading frames. Mol. Cell. Proteomics 2003, 2, 525-540.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 525-540
    • Katz, J.E.1    Dlakic, M.2    Clarke, S.3
  • 38
    • 38349035858 scopus 로고    scopus 로고
    • Arginine methylation at a glance
    • Bedford, M. T., Arginine methylation at a glance. J.Cell Sci. 2007, 120, 4243-4246.
    • (2007) J.Cell Sci , vol.120 , pp. 4243-4246
    • Bedford, M.T.1
  • 39
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin, C., Zhang, Y., The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell. Biol. 2005, 6, 838-849.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 40
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: protein lysine methyltransferases
    • Dillon, S. C., Zhang, X., Trievel, R. C., Cheng, X., The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol. 2005, 6, 227.
    • (2005) Genome Biol. , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 41
    • 78651080914 scopus 로고    scopus 로고
    • Uncovering the human methyltransferasome
    • M110 000976.
    • Petrossian, T. C., Clarke, S. G., Uncovering the human methyltransferasome. Mol. Cell. Proteomics 2011, 10, M110 000976.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Petrossian, T.C.1    Clarke, S.G.2
  • 42
    • 0038349436 scopus 로고    scopus 로고
    • Identification and analysis of chromodomain-containing proteins encoded in the mouse transcriptome
    • Tajul-Arifin, K., Teasdale, R., Ravasi, T., Hume, D. A. et al., Identification and analysis of chromodomain-containing proteins encoded in the mouse transcriptome. Genome Res. 2003, 13, 1416-1429.
    • (2003) Genome Res. , vol.13 , pp. 1416-1429
    • Tajul-Arifin, K.1    Teasdale, R.2    Ravasi, T.3    Hume, D.A.4
  • 43
    • 30944452960 scopus 로고    scopus 로고
    • The PHD finger, a nuclear protein-interaction domain
    • Bienz, M., The PHD finger, a nuclear protein-interaction domain. Trends Biochem. Sci. 2006, 31, 35-40.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 35-40
    • Bienz, M.1
  • 44
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T., Chromatin modifications and their function. Cell 2007, 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 45
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister, A. J., Kouzarides, T., Regulation of chromatin by histone modifications. Cell Res. 2011, 21, 381-395.
    • (2011) Cell Res. , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 46
    • 0035664074 scopus 로고    scopus 로고
    • WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases
    • Li, D., Roberts, R., WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell. Mol. Life Sci. 2001, 58, 2085-2097.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 2085-2097
    • Li, D.1    Roberts, R.2
  • 47
    • 0034717290 scopus 로고    scopus 로고
    • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains
    • Bedford, M. T., Frankel, A., Yaffe, M. B., Clarke, S. et al., Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J. Biol. Chem. 2000, 275, 16030-16036.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16030-16036
    • Bedford, M.T.1    Frankel, A.2    Yaffe, M.B.3    Clarke, S.4
  • 48
    • 0037184022 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase
    • Zhu, W., Mustelin, T., David, M., Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase. J. Biol. Chem. 2002, 277, 35787-35790.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35787-35790
    • Zhu, W.1    Mustelin, T.2    David, M.3
  • 49
    • 57049087451 scopus 로고    scopus 로고
    • Arginine methylation regulates the p53 response
    • Jansson, M., Durant, S. T., Cho, E. C., Sheahan, S. et al., Arginine methylation regulates the p53 response. Nat. Cell Biol. 2008, 10, 1431-1439.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1431-1439
    • Jansson, M.1    Durant, S.T.2    Cho, E.C.3    Sheahan, S.4
  • 50
    • 53949087832 scopus 로고    scopus 로고
    • Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt
    • Yamagata, K., Daitoku, H., Takahashi, Y., Namiki, K. et al., Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt. Mol. Cell. 2008, 32, 221-231.
    • (2008) Mol. Cell , vol.32 , pp. 221-231
    • Yamagata, K.1    Daitoku, H.2    Takahashi, Y.3    Namiki, K.4
  • 51
    • 84896735708 scopus 로고    scopus 로고
    • Signaling cross-talk in the resistance to HER family receptor targeted therapy
    • Yamaguchi, H., Chang, S. S., Hsu, J. L., Hung, M. C., Signaling cross-talk in the resistance to HER family receptor targeted therapy. Oncogene 2014, 33, 1073-1081.
    • (2014) Oncogene , vol.33 , pp. 1073-1081
    • Yamaguchi, H.1    Chang, S.S.2    Hsu, J.L.3    Hung, M.C.4
  • 52
    • 79551606798 scopus 로고    scopus 로고
    • Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation
    • Hsu, J. M., Chen, C. T., Chou, C. K., Kuo, H. P. et al., Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation. Nat. Cell Biol. 2011, 13, 174-181.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 174-181
    • Hsu, J.M.1    Chen, C.T.2    Chou, C.K.3    Kuo, H.P.4
  • 53
    • 36348996694 scopus 로고    scopus 로고
    • The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3
    • Kunizaki, M., Hamamoto, R., Silva, F. P., Yamaguchi, K. et al., The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. Cancer Res. 2007, 67, 10759-10765.
    • (2007) Cancer Res. , vol.67 , pp. 10759-10765
    • Kunizaki, M.1    Hamamoto, R.2    Silva, F.P.3    Yamaguchi, K.4
  • 54
    • 33644863484 scopus 로고    scopus 로고
    • A single amino acid substitution in the activation loop defines the decoy characteristic of VEGFR-1/FLT-1
    • Meyer, R. D., Mohammadi, M., Rahimi, N., A single amino acid substitution in the activation loop defines the decoy characteristic of VEGFR-1/FLT-1. J. Biol. Chem. 2006, 281, 867-875.
    • (2006) J. Biol. Chem. , vol.281 , pp. 867-875
    • Meyer, R.D.1    Mohammadi, M.2    Rahimi, N.3
  • 55
    • 0034595635 scopus 로고    scopus 로고
    • Receptor chimeras indicate that the vascular endothelial growth factor receptor-1 (VEGFR-1) modulates mitogenic activity of VEGFR-2 in endothelial cells
    • Rahimi, N., Dayanir, V., Lashkari, K., Receptor chimeras indicate that the vascular endothelial growth factor receptor-1 (VEGFR-1) modulates mitogenic activity of VEGFR-2 in endothelial cells. J. Biol. Chem. 2000, 275, 16986-16992.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16986-16992
    • Rahimi, N.1    Dayanir, V.2    Lashkari, K.3
  • 56
    • 84889238946 scopus 로고    scopus 로고
    • Lysine methylation promotes VEGFR-2 activation and angiogenesis
    • Hartsough, E. J., Meyer, R. D., Chitalia, V., Jiang, Y. et al., Lysine methylation promotes VEGFR-2 activation and angiogenesis. Sci. Signal. 2013, 6, ra104.
    • (2013) Sci. Signal , vol.6 , pp. ra104
    • Hartsough, E.J.1    Meyer, R.D.2    Chitalia, V.3    Jiang, Y.4
  • 57
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang, X. J., Seto, E., Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 2008, 31, 449-461.
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 58
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S. L., The complex language of chromatin regulation during transcription. Nature 2007, 447, 407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 59
    • 41149145576 scopus 로고    scopus 로고
    • Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription
    • Sabo, A., Lusic, M., Cereseto, A., Giacca, M., Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription. J. Mol. Cell Biol. 2008, 28, 2201-2212.
    • (2008) J. Mol. Cell Biol , vol.28 , pp. 2201-2212
    • Sabo, A.1    Lusic, M.2    Cereseto, A.3    Giacca, M.4
  • 60
    • 84874769490 scopus 로고    scopus 로고
    • articl, Reversible acetylation regulates salt-inducible kinase (SIK2) and its function in autophagy. .
    • Yang, F. C., Tan, B. C., Chen, W. H., Lin, Y. H. et al., Reversible acetylation regulates salt-inducible kinase (SIK2) and its function in autophagy. J. Biol. Chem. 2013, 288, 6227-6237.
    • (2013) J. Biol. Chem , vol.288 , pp. 6227-6237
    • Yang, F.C.1    Tan, B.C.2    Chen, W.H.3    Lin, Y.H.4
  • 61
    • 84899675551 scopus 로고    scopus 로고
    • Reversible acetylation regulates vascular endothelial growth factor receptor-2 activity
    • Zecchin, A., Pattarini, L., Gutierrez, M. I., Mano, M. et al., Reversible acetylation regulates vascular endothelial growth factor receptor-2 activity. J. Mol. Cell Biol. 2014, 6, 116-127.
    • (2014) J. Mol. Cell Biol , vol.6 , pp. 116-127
    • Zecchin, A.1    Pattarini, L.2    Gutierrez, M.I.3    Mano, M.4
  • 62
    • 84887206685 scopus 로고    scopus 로고
    • Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization
    • Lv, L., Xu, Y. P., Zhao, D., Li, F. L. et al., Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization. Mol. Cell. 2013, 52, 340-352.
    • (2013) Mol. Cell , vol.52 , pp. 340-352
    • Lv, L.1    Xu, Y.P.2    Zhao, D.3    Li, F.L.4
  • 63
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • Kouzarides, T., Acetylation: a regulatory modification to rival phosphorylation? EMBO Journal. 2000, 19, 1176-1179.
    • (2000) EMBO Journal , vol.19 , pp. 1176-1179
    • Kouzarides, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.