메뉴 건너뛰기




Volumn 3, Issue 5, 2011, Pages 301-308

Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2

Author keywords

histone methylation; HSP90; lysine methylation; SET domain; SMYD proteins

Indexed keywords

HEAT SHOCK PROTEIN 90; HISTONE DEMETHYLASE; HISTONE LYSINE METHYLTRANSFERASE; ISOENZYME; KDM1A PROTEIN, HUMAN; LYSINE; MULTIPROTEIN COMPLEX; PROTEOME; SMYD2 PROTEIN, HUMAN; SMYD3 PROTEIN, HUMAN;

EID: 80455141717     PISSN: 16742788     EISSN: 17594685     Source Type: Journal    
DOI: 10.1093/jmcb/mjr025     Document Type: Article
Times cited : (90)

References (60)
  • 1
    • 41549133493 scopus 로고    scopus 로고
    • The tale of two domains: Proteomics and genomics analysis of SMYD2, a new histone methyltransferase
    • Abu-Farha, M., Lambert, J. P., Al-Madhoun, A. S., et al. (2008). The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase. Mol. Cell. Proteomics 7, 560-572.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 560-572
    • Abu-Farha, M.1    Lambert, J.P.2    Al-Madhoun, A.S.3
  • 2
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • Bouchard, V. J., Rouleau, M., and Poirier, G. G. (2003). PARP-1, a determinant of cell survival in response to DNA damage. Exp. Hematol. 31, 446-454.
    • (2003) Exp. Hematol. , vol.31 , pp. 446-454
    • Bouchard, V.J.1    Rouleau, M.2    Poirier, G.G.3
  • 3
    • 33746832077 scopus 로고    scopus 로고
    • Identification and characterization of Smyd2: A split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown, M. A., Sims, R. J., III, Gottlieb, P. D., et al. (2006). Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer 5, 26.
    • (2006) Mol. Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims III, R.J.2    Gottlieb, P.D.3
  • 4
    • 0030746217 scopus 로고    scopus 로고
    • A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme
    • Cai, J., Gibbs, E., Uhlmann, F., et al. (1997). A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme. J. Biol. Chem. 272, 18974-18981.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18974-18981
    • Cai, J.1    Gibbs, E.2    Uhlmann, F.3
  • 5
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen, S., and Smith, D. F. (1998). Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 273, 35194-35200.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 6
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov, S., Kurash, J. K., Wilson, J. R., et al. (2004). Regulation of p53 activity through lysine methylation. Nature 432, 353-360.
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1    Kurash, J.K.2    Wilson, J.R.3
  • 7
    • 13944277701 scopus 로고    scopus 로고
    • The life and death of DNA-PK
    • Collis, S. J., DeWeese, T. L., Jeggo, P. A., et al. (2005). The life and death of DNA-PK. Oncogene 24, 949-961.
    • (2005) Oncogene , vol.24 , pp. 949-961
    • Collis, S.J.1    DeWeese, T.L.2    Jeggo, P.A.3
  • 8
    • 0029968413 scopus 로고    scopus 로고
    • Chromotin binding, nuclear localization and phosphorylation of Xenopus cdc21 are cell-cycle dependent and associated with the control of initiation of DNA replication
    • Coue, M., Kearsey, S. E., and Mechali, M. (1996). Chromotin binding, nuclear localization and phosphorylation of Xenopus cdc21 are cell-cycle dependent and associated with the control of initiation of DNA replication. EMBO J. 15, 1085-1097.
    • (1996) EMBO J. , vol.15 , pp. 1085-1097
    • Coue, M.1    Kearsey, S.E.2    Mechali, M.3
  • 9
    • 80052591715 scopus 로고    scopus 로고
    • Substrate and product specificities of SET domain methyltransferases
    • Del Rizzo, P. A., and Trievel, R. C. (2011). Substrate and product specificities of SET domain methyltransferases. Epigenetics 6, 1059-1067.
    • (2011) Epigenetics , vol.6 , pp. 1059-1067
    • Del Rizzo, P.A.1    Trievel, R.C.2
  • 10
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon, S. C., Zhang, X., Trievel, R. C., et al. (2005). The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol. 6, 227.
    • (2005) Genome Biol. , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3
  • 11
    • 78650981194 scopus 로고    scopus 로고
    • A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability
    • Esteve, P. O., Chang, Y., Samaranayake, M., et al. (2011). A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability. Nat. Struct. Mol. Biol. 18, 42-48.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 42-48
    • Esteve, P.O.1    Chang, Y.2    Samaranayake, M.3
  • 12
    • 0036578662 scopus 로고    scopus 로고
    • Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis
    • Gottlieb, P. D., Pierce, S. A., Sims, R. J., et al. (2002). Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis. Nat. Genet. 31, 25-32.
    • (2002) Nat. Genet. , vol.31 , pp. 25-32
    • Gottlieb, P.D.1    Pierce, S.A.2    Sims, R.J.3
  • 13
    • 4143074854 scopus 로고    scopus 로고
    • SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
    • Hamamoto, R., Furukawa, Y., Morita, M., et al. (2004). SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. 6, 731-740.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 731-740
    • Hamamoto, R.1    Furukawa, Y.2    Morita, M.3
  • 14
    • 33644929027 scopus 로고    scopus 로고
    • Enhanced SMYD3 expression is essential for the growth of breast cancer cells
    • Hamamoto, R., Silva, F. P., Tsuge, M., et al. (2006). Enhanced SMYD3 expression is essential for the growth of breast cancer cells. Cancer Sci. 97, 113-118.
    • (2006) Cancer Sci. , vol.97 , pp. 113-118
    • Hamamoto, R.1    Silva, F.P.2    Tsuge, M.3
  • 15
    • 3042856481 scopus 로고    scopus 로고
    • Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones
    • Hatakeyama, S., Matsumoto, M., Yada, M., et al. (2004). Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells 9, 533-548.
    • (2004) Genes Cells , vol.9 , pp. 533-548
    • Hatakeyama, S.1    Matsumoto, M.2    Yada, M.3
  • 16
    • 65949117245 scopus 로고    scopus 로고
    • Identification of Smyd4 as a potential tumor suppressor gene involved in breast cancer development
    • Hu, L., Zhu, Y. T., Qi, C., et al. (2009). Identification of Smyd4 as a potential tumor suppressor gene involved in breast cancer development. Cancer Res. 69, 4067-4072.
    • (2009) Cancer Res. , vol.69 , pp. 4067-4072
    • Hu, L.1    Zhu, Y.T.2    Qi, C.3
  • 17
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • Huang, J., and Berger, S. L. (2008). The emerging field of dynamic lysine methylation of non-histone proteins. Curr. Opin. Genet. Dev. 18, 152-158.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 18
    • 33845204856 scopus 로고    scopus 로고
    • Repression of p53 activity by Smyd2-mediated methylation
    • Huang, J., Perez-Burgos, L., Placek, B. J., et al. (2006). Repression of p53 activity by Smyd2-mediated methylation. Nature 444, 629-632.
    • (2006) Nature , vol.444 , pp. 629-632
    • Huang, J.1    Perez-Burgos, L.2    Placek, B.J.3
  • 19
    • 34548513035 scopus 로고    scopus 로고
    • P53 is regulated by the lysine demethylase LSD1
    • Huang, J., Sengupta, R., Espejo, A. B., et al. (2007). p53 is regulated by the lysine demethylase LSD1. Nature 449, 105-108.
    • (2007) Nature , vol.449 , pp. 105-108
    • Huang, J.1    Sengupta, R.2    Espejo, A.B.3
  • 20
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • Johnson, A., and O'Donnell, M. (2005). Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem. 74, 283-315.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 21
    • 67650102336 scopus 로고    scopus 로고
    • Overexpression of SMYD2 relates to tumor cell proliferation and malignant outcome of esophageal squamous cell carcinoma
    • Komatsu, S., Imoto, I., Tsuda, H., et al. (2009). Overexpression of SMYD2 relates to tumor cell proliferation and malignant outcome of esophageal squamous cell carcinoma. Carcinogenesis 30, 1139-1146.
    • (2009) Carcinogenesis , vol.30 , pp. 1139-1146
    • Komatsu, S.1    Imoto, I.2    Tsuda, H.3
  • 22
    • 73249143709 scopus 로고    scopus 로고
    • Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
    • Kundrat, L., and Regan, L. (2010). Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP. J. Mol. Biol. 395, 587-594.
    • (2010) J. Mol. Biol. , vol.395 , pp. 587-594
    • Kundrat, L.1    Regan, L.2
  • 23
    • 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., et al. (2007). The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. Cancer Res. 67, 10759-10765.
    • (2007) Cancer Res. , vol.67 , pp. 10759-10765
    • Kunizaki, M.1    Hamamoto, R.2    Silva, F.P.3
  • 24
    • 55249118199 scopus 로고    scopus 로고
    • The heterochromatin protein 1 (HP1) family: Put away a bias toward HP1
    • Kwon, S. H., and Workman, J. L. (2008). The heterochromatin protein 1 (HP1) family: put away a bias toward HP1. Mol. Cells 26, 217-227.
    • (2008) Mol. Cells , vol.26 , pp. 217-227
    • Kwon, S.H.1    Workman, J.L.2
  • 25
    • 78650308842 scopus 로고    scopus 로고
    • Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling
    • Levy, D., Kuo, A. J., Chang, Y., et al. (2011). Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling. Nat. Immunol. 12, 29-36.
    • (2011) Nat. Immunol. , vol.12 , pp. 29-36
    • Levy, D.1    Kuo, A.J.2    Chang, Y.3
  • 26
    • 33744965571 scopus 로고    scopus 로고
    • Functional roles of p12, the fourth subunit of human DNA polymerase delta
    • Li, H., Xie, B., Zhou, Y., et al. (2006). Functional roles of p12, the fourth subunit of human DNA polymerase delta. J. Biol. Chem. 281, 14748-14755.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14748-14755
    • Li, H.1    Xie, B.2    Zhou, Y.3
  • 27
    • 75349089845 scopus 로고    scopus 로고
    • SMYD1, the myogenic activator, is a direct target of serum response factor and myogenin
    • Li, D., Niu, Z., Yu, W., et al. (2009a). SMYD1, the myogenic activator, is a direct target of serum response factor and myogenin. Nucleic Acids Res. 37, 7059-7071.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7059-7071
    • Li, D.1    Niu, Z.2    Yu, W.3
  • 28
    • 70449672959 scopus 로고    scopus 로고
    • PCNA is required for initiation of recombination-associated DNA synthesis by DNA polymerase delta
    • Li, X., Stith, C. M., Burgers, P. M., et al. (2009b). PCNA is required for initiation of recombination-associated DNA synthesis by DNA polymerase delta. Mol. Cell 36, 704-713.
    • (2009) Mol. Cell , vol.36 , pp. 704-713
    • Li, X.1    Stith, C.M.2    Burgers, P.M.3
  • 29
    • 0037593900 scopus 로고    scopus 로고
    • Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
    • Lotz, G. P., Lin, H., Harst, A., et al. (2003). Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. 278, 17228-17235.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17228-17235
    • Lotz, G.P.1    Lin, H.2    Harst, A.3
  • 30
    • 33750088144 scopus 로고    scopus 로고
    • CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA synthesis
    • Lutz, T., Stoger, R., and Nieto, A. (2006). CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA synthesis. FEBS Lett. 580, 5851-5857.
    • (2006) FEBS Lett. , vol.580 , pp. 5851-5857
    • Lutz, T.1    Stoger, R.2    Nieto, A.3
  • 31
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin, C., and Zhang, Y. (2005). The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838-849.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 32
    • 20844444338 scopus 로고    scopus 로고
    • S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
    • Martinez-Ruiz, A., Villanueva, L., Gonzalez de Orduna, C., et al. (2005). S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl Acad. Sci. USA 102, 8525-8530.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8525-8530
    • Martinez-Ruiz, A.1    Villanueva, L.2    Gonzalez De Orduna, C.3
  • 33
    • 77951623834 scopus 로고    scopus 로고
    • Lysine methylation regulates the pRb tumour suppressor protein
    • Munro, S., Khaire, N., Inche, A., et al. (2010). Lysine methylation regulates the pRb tumour suppressor protein. Oncogene 29, 2357-2367.
    • (2010) Oncogene , vol.29 , pp. 2357-2367
    • Munro, S.1    Khaire, N.2    Inche, A.3
  • 34
    • 78049379279 scopus 로고    scopus 로고
    • Replication factor C recruits DNA polymerase delta to sites of nucleotide excision repair but is not required for PCNA recruitment
    • Overmeer, R. M., Gourdin, A. M., Giglia-Mari, A., et al. (2010). Replication factor C recruits DNA polymerase delta to sites of nucleotide excision repair but is not required for PCNA recruitment. Mol. Cell. Biol. 30, 4828-4839.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4828-4839
    • Overmeer, R.M.1    Gourdin, A.M.2    Giglia-Mari, A.3
  • 35
    • 77649090565 scopus 로고    scopus 로고
    • Identification of arginineand lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications
    • Pang, C. N., Gasteiger, E., and Wilkins, M. R. (2010). Identification of arginineand lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications. BMC Genomics 11, 92.
    • (2010) BMC Genomics , vol.11 , pp. 92
    • Pang, C.N.1    Gasteiger, E.2    Wilkins, M.R.3
  • 36
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B., and Toft, D. O. (2003). Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228, 111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 37
    • 70449710842 scopus 로고    scopus 로고
    • Hsp90 is regulated by a switch point in the C-terminal domain
    • Retzlaff, M., Stahl, M., Eberl, H. C., et al. (2009). Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep. 10, 1147-1153.
    • (2009) EMBO Rep. , vol.10 , pp. 1147-1153
    • Retzlaff, M.1    Stahl, M.2    Eberl, H.C.3
  • 38
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50 (cdc37)
    • Roe, S. M., Ali, M. M., Meyer, P., et al. (2004). The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50 (cdc37). Cell 116, 87-98.
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3
  • 39
    • 78349236076 scopus 로고    scopus 로고
    • Methylation of the retinoblastoma tumor suppressor by SMYD2
    • Saddic, L. A., West, L. E., Aslanian, A., et al. (2010). Methylation of the retinoblastoma tumor suppressor by SMYD2. J. Biol. Chem. 285, 37733-37740.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37733-37740
    • Saddic, L.A.1    West, L.E.2    Aslanian, A.3
  • 40
    • 0037455691 scopus 로고    scopus 로고
    • Overexpression of a protein fragment of RNA helicase A causes inhibition of endogenous BRCA1 function and defects in ploidy and cytokinesis in mammary epithelial cells
    • Schlegel, B. P., Starita, L. M., and Parvin, J. D. (2003). Overexpression of a protein fragment of RNA helicase A causes inhibition of endogenous BRCA1 function and defects in ploidy and cytokinesis in mammary epithelial cells. Oncogene 22, 983-991.
    • (2003) Oncogene , vol.22 , pp. 983-991
    • Schlegel, B.P.1    Starita, L.M.2    Parvin, J.D.3
  • 41
    • 35148835080 scopus 로고    scopus 로고
    • Functional analysis of the transcription repressor PLU-1/JARID1B
    • Scibetta, A. G., Santangelo, S., Coleman, J., et al. (2007). Functional analysis of the transcription repressor PLU-1/JARID1B. Mol. Cell. Biol. 27, 7220-7235.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7220-7235
    • Scibetta, A.G.1    Santangelo, S.2    Coleman, J.3
  • 42
    • 35348858091 scopus 로고    scopus 로고
    • Post-translational modification of heatshock protein 90: Impact on chaperone function
    • Scroggins, B. T., and Neckers, L. (2007). Post-translational modification of heatshock protein 90: impact on chaperone function. Expert Opin. Drug Discov. 2, 1403-1414.
    • (2007) Expert Opin. Drug Discov. , vol.2 , pp. 1403-1414
    • Scroggins, B.T.1    Neckers, L.2
  • 43
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins, B. T., Robzyk, K., Wang, D. X., et al. (2007). An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol. Cell 25, 151-159.
    • (2007) Mol. Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.X.3
  • 44
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y., Lan, F., Matson, C., et al. (2004). Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3
  • 45
    • 0037135616 scopus 로고    scopus 로고
    • M-Bop, a repressor protein essential for cardiogenesis, interacts with skNAC, a heart-and musclespecific transcription factor
    • Sims, R. J., III, Weihe, E. K., Zhu, L., et al. (2002). m-Bop, a repressor protein essential for cardiogenesis, interacts with skNAC, a heart-and musclespecific transcription factor. J. Biol. Chem. 277, 26524-26529.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26524-26529
    • Sims III, R.J.1    Weihe, E.K.2    Zhu, L.3
  • 46
    • 33646507676 scopus 로고    scopus 로고
    • Structure and functional analysis of the MYND domain
    • Spadaccini, R., Perrin, H., Bottomley, M. J., et al. (2006). Structure and functional analysis of the MYND domain. J. Mol. Biol. 358, 498-508.
    • (2006) J. Mol. Biol. , vol.358 , pp. 498-508
    • Spadaccini, R.1    Perrin, H.2    Bottomley, M.J.3
  • 47
    • 42949142112 scopus 로고    scopus 로고
    • Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase
    • Subramanian, K., Jia, D., Kapoor-Vazirani, P., et al. (2008). Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase. Mol. Cell 30, 336-347.
    • (2008) Mol. Cell , vol.30 , pp. 336-347
    • Subramanian, K.1    Jia, D.2    Kapoor-Vazirani, P.3
  • 48
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale, M., Jarosz, D. F., and Lindquist, S. (2010). HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11, 515-528.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 49
    • 33644542409 scopus 로고    scopus 로고
    • SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos
    • Tan, X., Rotllant, J., Li, H., et al. (2006). SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos. Proc. Natl Acad. Sci. USA 103, 2713-2718.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2713-2718
    • Tan, X.1    Rotllant, J.2    Li, H.3
  • 50
    • 51749088536 scopus 로고    scopus 로고
    • A Drosophila Smyd4 homologue is a muscle-specific transcriptional modulator involved in development
    • Thompson, E. C., and Travers, A. A. (2008). A Drosophila Smyd4 homologue is a muscle-specific transcriptional modulator involved in development. PLoS One 3, e3008.
    • (2008) PLoS One , vol.3
    • Thompson, E.C.1    Travers, A.A.2
  • 52
    • 70449522304 scopus 로고    scopus 로고
    • Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription
    • Tuduri, S., Crabbe, L., Conti, C., et al. (2009). Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription. Nat. Cell Biol. 11, 1315-1324.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1315-1324
    • Tuduri, S.1    Crabbe, L.2    Conti, C.3
  • 53
    • 0030986962 scopus 로고    scopus 로고
    • Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities
    • Uhlmann, F., Cai, J., Gibbs, E., et al. (1997). Deletion analysis of the large subunit p140 in human replication factor C reveals regions required for complex formation and replication activities. J. Biol. Chem. 272, 10058-10064.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10058-10064
    • Uhlmann, F.1    Cai, J.2    Gibbs, E.3
  • 54
    • 43249122483 scopus 로고    scopus 로고
    • Knockdown of SMYD3 by RNA interference inhibits cervical carcinoma cell growth and invasion in vitro
    • Wang, S. Z., Luo, X. G., Shen, J., et al. (2008). Knockdown of SMYD3 by RNA interference inhibits cervical carcinoma cell growth and invasion in vitro. BMB Rep. 41, 294-299.
    • (2008) BMB Rep. , vol.41 , pp. 294-299
    • Wang, S.Z.1    Luo, X.G.2    Shen, J.3
  • 55
    • 69449100367 scopus 로고    scopus 로고
    • Human RIF1 encodes an anti-apoptotic factor required for DNA repair
    • Wang, H., Zhao, A., Chen, L., et al. (2009). Human RIF1 encodes an anti-apoptotic factor required for DNA repair. Carcinogenesis 30, 1314-1319.
    • (2009) Carcinogenesis , vol.30 , pp. 1314-1319
    • Wang, H.1    Zhao, A.2    Chen, L.3
  • 57
    • 78650218014 scopus 로고    scopus 로고
    • SMYD3 interacts with HTLV-1 Tax and regulates subcellular localization of Tax
    • Yamamoto, K., Ishida, T., Nakano, K., et al. (2011). SMYD3 interacts with HTLV-1 Tax and regulates subcellular localization of Tax. Cancer Sci. 102, 260-266.
    • (2011) Cancer Sci. , vol.102 , pp. 260-266
    • Yamamoto, K.1    Ishida, T.2    Nakano, K.3
  • 58
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang, Y., Rao, R., Shen, J., et al. (2008). Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res. 68, 4833-4842.
    • (2008) Cancer Res. , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3
  • 59
    • 77950642805 scopus 로고    scopus 로고
    • Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB
    • Yang, X. D., Tajkhorshid, E., and Chen, L. F. (2010). Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB. Mol. Cell. Biol. 30, 2170-2180.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2170-2180
    • Yang, X.D.1    Tajkhorshid, E.2    Chen, L.F.3
  • 60
    • 67349218722 scopus 로고    scopus 로고
    • Knockdown of SMYD3 by RNA interference down-regulates c-Met expression and inhibits cells migration and invasion induced by HGF
    • Zou, J. N., Wang, S. Z., Yang, J. S., et al. (2009). Knockdown of SMYD3 by RNA interference down-regulates c-Met expression and inhibits cells migration and invasion induced by HGF. Cancer Lett. 280, 78-85.
    • (2009) Cancer Lett. , vol.280 , pp. 78-85
    • Zou, J.N.1    Wang, S.Z.2    Yang, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.