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Volumn 29, Issue 8, 2009, Pages 2181-2192

Association of C-terminal ubiquitin hydrolase BRCAl-associated protein 1 with cell cycle regulator host cell factor 1

Author keywords

[No Author keywords available]

Indexed keywords

BRCA1 ASSOCIATED PROTEIN 1; BRCA1 PROTEIN; HOST CELL FACTOR 1; LYSINE; NUCLEAR PROTEIN; PROTEIN VP16; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 64649106796     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01517-08     Document Type: Article
Times cited : (181)

References (50)
  • 1
    • 35748935572 scopus 로고    scopus 로고
    • Molecular analysis of deletions in human chromosome 3p21 and the role of resident cancer genes in disease
    • Angeloni, D. 2007. Molecular analysis of deletions in human chromosome 3p21 and the role of resident cancer genes in disease. Brief Funct. Genomic Proteomic 6:19-39.
    • (2007) Brief Funct. Genomic Proteomic , vol.6 , pp. 19-39
    • Angeloni, D.1
  • 2
    • 0036463388 scopus 로고    scopus 로고
    • Selective detection of membrane proteins without antibodies: A mass spectrometric version of the Western blot
    • Arnott, D., A. Kishiyama, E. A. Luis, S. G. Ludlum, J. C. Marsters, Jr., and J. T. Stults. 2002. Selective detection of membrane proteins without antibodies: a mass spectrometric version of the Western blot. Mol. Cell. Proteomics 1:148-156.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 148-156
    • Arnott, D.1    Kishiyama, A.2    Luis, E.A.3    Ludlum, S.G.4    Marsters Jr., J.C.5    Stults, J.T.6
  • 3
    • 0028241636 scopus 로고
    • Homozygous deletion, rearrangement and hypermethylation implicate chromosome region 3pl4.3-3p21.3 in sporadic breast-cancer development
    • Buchhagen, D. L., L. Qiu, and P. Etkind. 1994. Homozygous deletion, rearrangement and hypermethylation implicate chromosome region 3pl4.3-3p21.3 in sporadic breast-cancer development. Int. J. Cancer 57:473-479.
    • (1994) Int. J. Cancer , vol.57 , pp. 473-479
    • Buchhagen, D.L.1    Qiu, L.2    Etkind, P.3
  • 5
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang, L. C, F. D. Melandri, and R. L. Stein. 1998. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 37:1868-1879.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 8
  • 9
    • 0030687635 scopus 로고    scopus 로고
    • Viral mimicry: Common mode of association with HCF by VP16 and the cellular protein LZIP
    • Freiman, R. N., and W. Herr. 1997. Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP. Genes Dev. 11:3122-3127.
    • (1997) Genes Dev , vol.11 , pp. 3122-3127
    • Freiman, R.N.1    Herr, W.2
  • 10
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pro-teolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and A. Ciechanover. 2002. The ubiquitin-proteasome pro-teolytic pathway: destruction for the sake of construction. Physiol. Rev. 82:373-428.
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 12
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiq-uitinating enzyme UCH37 to 26S proteasomes
    • Hamazaki, J., S. Iemura, T. Natsume, H. Yashiroda, K. Tanaka, and S. Murata. 2006. A novel proteasome interacting protein recruits the deubiq-uitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25:4524-4536.
    • (2006) EMBO J , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 14
    • 0010267472 scopus 로고    scopus 로고
    • Defining biochemical functions for the BRCA1 tumor suppressor protein: Analysis of the BRCA1-binding protein BAP1
    • Jensen, D. E., and F. J. Rauscher III. 1999. Defining biochemical functions for the BRCA1 tumor suppressor protein: analysis of the BRCA1-binding protein BAP1. Cancer Lett. 143(Suppl. 1):S13-S17.
    • (1999) Cancer Lett , vol.143 , Issue.SUPPL. 1
    • Jensen, D.E.1    Rauscher III, F.J.2
  • 15
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston, S. C., C. N. Larsen, W. J. Cook, K. D. Wilkinson, and C. P. Hill. 1997. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16:3787-3796.
    • (1997) EMBO J , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 16
    • 2942674785 scopus 로고    scopus 로고
    • A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1
    • Julien, E., and W. Herr. 2004. A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1. Mol. Cell 14:713-725.
    • (2004) Mol. Cell , vol.14 , pp. 713-725
    • Julien, E.1    Herr, W.2
  • 17
    • 0038242360 scopus 로고    scopus 로고
    • Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1
    • Julien, E., and W. Herr. 2003. Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1. EMBO J. 22:2360-2369.
    • (2003) EMBO J , vol.22 , pp. 2360-2369
    • Julien, E.1    Herr, W.2
  • 18
    • 33748190398 scopus 로고    scopus 로고
    • Host cell factor-1 and E2F4 interact via multiple determinants in each protein
    • Knez, J., D. Piluso, P. Bilan, and J. P. Capone. 2006. Host cell factor-1 and E2F4 interact via multiple determinants in each protein. Mol. Cell. Biochem. 288:79-90.
    • (2006) Mol. Cell. Biochem , vol.288 , pp. 79-90
    • Knez, J.1    Piluso, D.2    Bilan, P.3    Capone, J.P.4
  • 19
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich, E., X. Li, and G. N. Demartino. 2008. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol. Biol. Cell 19:1072-1082.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    Demartino, G.N.3
  • 20
    • 85177006559 scopus 로고    scopus 로고
    • Kristie, T. M, J. L. Pomerantz, T. C. Twomey, S. A. Parent, and P. A, Sharp. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270:4387-4394.
    • Kristie, T. M, J. L. Pomerantz, T. C. Twomey, S. A. Parent, and P. A, Sharp. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270:4387-4394.
  • 21
    • 0033573922 scopus 로고    scopus 로고
    • Nuclear localization of the Cl factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency
    • Kristie, T. M, J. L. Vogel, and A. E. Sears. 1999. Nuclear localization of the Cl factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency. Proc. Natl. Acad. Sci. USA 96:1229-1233.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1229-1233
    • Kristie, T.M.1    Vogel, J.L.2    Sears, A.E.3
  • 22
    • 0040036654 scopus 로고    scopus 로고
    • HCF-dependent nuclear import of VP16
    • La Boissiere, S, T. Hughes, and P. O'Hare. 1999. HCF-dependent nuclear import of VP16. EMBO J. 18:480-489.
    • (1999) EMBO J , vol.18 , pp. 480-489
    • La Boissiere, S.1    Hughes, T.2    O'Hare, P.3
  • 23
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • Larsen, C. N., B. A. Krantz, and K. D. Wilkinson. 1998. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 37:3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 24
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: Identification of two active site residues
    • Larsen, C. N., J. S. Price, and K. D. Wilkinson. 1996. Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry 35:6735-6744.
    • (1996) Biochemistry , vol.35 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 25
    • 0034720458 scopus 로고    scopus 로고
    • Li, T., N. I. Naqvi, H. Yang, and T. S. Teo. 2000. Identification of a 26S proteasome-associated UCH in fission yeast. Biochem. Biophys. Res. Com-mun. 272:270-275.
    • Li, T., N. I. Naqvi, H. Yang, and T. S. Teo. 2000. Identification of a 26S proteasome-associated UCH in fission yeast. Biochem. Biophys. Res. Com-mun. 272:270-275.
  • 26
    • 0031878579 scopus 로고    scopus 로고
    • The herpesviras transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF
    • Lu, R., P. Yang, S. Padmakumar, and V. Misra. 1998. The herpesviras transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF. J. Virol. 72:6291-6297.
    • (1998) J. Virol , vol.72 , pp. 6291-6297
    • Lu, R.1    Yang, P.2    Padmakumar, S.3    Misra, V.4
  • 27
    • 0345803936 scopus 로고    scopus 로고
    • HCF-1 functions as a coactivator for the zinc finger protein Krox20
    • Luciano, R. L., and A. C. Wilson. 2003. HCF-1 functions as a coactivator for the zinc finger protein Krox20. J. Biol. Chem. 278:51116-51124.
    • (2003) J. Biol. Chem , vol.278 , pp. 51116-51124
    • Luciano, R.L.1    Wilson, A.C.2
  • 28
    • 0037122004 scopus 로고    scopus 로고
    • Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
    • Mallery, D. L., C. J. Vandenberg, and K. Hiom. 2002. Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J. 21:6755-6762.
    • (2002) EMBO J , vol.21 , pp. 6755-6762
    • Mallery, D.L.1    Vandenberg, C.J.2    Hiom, K.3
  • 29
    • 17744362278 scopus 로고    scopus 로고
    • Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activity
    • Maun, H. R., C. Eigenbrot, H. Raab, D. Arnott, L. Phu, S. Bullens, and R. A. Lazarus. 2005. Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activity. Protein Sci. 14:1171-1180.
    • (2005) Protein Sci , vol.14 , pp. 1171-1180
    • Maun, H.R.1    Eigenbrot, C.2    Raab, H.3    Arnott, D.4    Phu, L.5    Bullens, S.6    Lazarus, R.A.7
  • 30
    • 34249845272 scopus 로고    scopus 로고
    • Meray, R. K., and P. T. Lansbury, Jr. 2007. Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1. J. Biol. Chem. 282:10567-10575.
    • Meray, R. K., and P. T. Lansbury, Jr. 2007. Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1. J. Biol. Chem. 282:10567-10575.
  • 31
    • 12544253837 scopus 로고    scopus 로고
    • Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate
    • Misaghi, S., P. J. Galardy, W. J. Meester, H. Ovaa, H. L. Ploegh, and R. Gaudet. 2005. Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. 280:1512-1520.
    • (2005) J. Biol. Chem , vol.280 , pp. 1512-1520
    • Misaghi, S.1    Galardy, P.J.2    Meester, W.J.3    Ovaa, H.4    Ploegh, H.L.5    Gaudet, R.6
  • 32
    • 34547467103 scopus 로고    scopus 로고
    • The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesviras immediate-early promoters for initiation of infection
    • Narayanan, A., W. T. Ruyechan, and T. M. Kristie. 2007. The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesviras immediate-early promoters for initiation of infection. Proc. Natl. Acad. Sci. USA 104:10835-10840.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10835-10840
    • Narayanan, A.1    Ruyechan, W.T.2    Kristie, T.M.3
  • 33
    • 58249095937 scopus 로고    scopus 로고
    • BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity
    • Nishikawa, H., W. Wu, A. Koike, R. Kojima, H. Gomi, M. Fukuda, and T. Ohta. 2009. BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity. Cancer Res. 69:111-119.
    • (2009) Cancer Res , vol.69 , pp. 111-119
    • Nishikawa, H.1    Wu, W.2    Koike, A.3    Kojima, R.4    Gomi, H.5    Fukuda, M.6    Ohta, T.7
  • 34
    • 0037195811 scopus 로고    scopus 로고
    • Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1
    • Piluso, D., P. Bilan, and J. P. Capone. 2002. Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1. J. Biol. Chem. 277:46799-46808.
    • (2002) J. Biol. Chem , vol.277 , pp. 46799-46808
    • Piluso, D.1    Bilan, P.2    Capone, J.P.3
  • 35
    • 33845713194 scopus 로고    scopus 로고
    • hRpnl3/ADRMl/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • Qiu, X. B., S. Y. Ouyang, C. J. Li, S. Miao, L. Wang, and A. L. Goldberg. 2006. hRpnl3/ADRMl/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J. 25:5742-5753.
    • (2006) EMBO J , vol.25 , pp. 5742-5753
    • Qiu, X.B.1    Ouyang, S.Y.2    Li, C.J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 36
    • 0030951418 scopus 로고    scopus 로고
    • Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements
    • Simmen, K. A., A. Newell, M. Robinson, J. S. Mills, G. Canning, R, Handa, K. Parkes, N. Borkakoti, and R. Jupp. 1997. Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements. J. Virol. 71:3886-3894.
    • (1997) J. Virol , vol.71 , pp. 3886-3894
    • Simmen, K.A.1    Newell, A.2    Robinson, M.3    Mills, J.S.4    Canning, G.5    Handa, R.6    Parkes, K.7    Borkakoti, N.8    Jupp, R.9
  • 37
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • Smith, E. R., C. Cayrou, R. Huang, W. S. Lane, J. Cote, and J. C. Lucchesi. 2005. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol. Cell. Biol. 25:9175-9188.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9175-9188
    • Smith, E.R.1    Cayrou, C.2    Huang, R.3    Lane, W.S.4    Cote, J.5    Lucchesi, J.C.6
  • 38
    • 41549142601 scopus 로고    scopus 로고
    • Reverse the curse-the role of deubiquitination in cell cycle control
    • Song, L., and M. Rape. 2008. Reverse the curse-the role of deubiquitination in cell cycle control. Curr. Opin. Cell Biol. 20:156-163.
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 156-163
    • Song, L.1    Rape, M.2
  • 39
    • 7944230364 scopus 로고    scopus 로고
    • Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast
    • Stone, M, R. Hartmann-Petersen, M. Seeger, D. Bech-Otschir, M. Wallace, and C. Gordon. 2004. Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast. J. Mol. Biol. 344:697-706.
    • (2004) J. Mol. Biol , vol.344 , pp. 697-706
    • Stone, M.1    Hartmann-Petersen, R.2    Seeger, M.3    Bech-Otschir, D.4    Wallace, M.5    Gordon, C.6
  • 40
    • 34250823511 scopus 로고    scopus 로고
    • E2F activation of S phase promoters via association with HCF-1 and the MLL family of histone H3K4 methyltransferases
    • Tyagi, S., A. L. Chabes, J. Wysocka, and W. Herr. 2007. E2F activation of S phase promoters via association with HCF-1 and the MLL family of histone H3K4 methyltransferases. Mol. Cell 27:107-119.
    • (2007) Mol. Cell , vol.27 , pp. 107-119
    • Tyagi, S.1    Chabes, A.L.2    Wysocka, J.3    Herr, W.4
  • 41
    • 52049085265 scopus 로고    scopus 로고
    • BRCAl-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization
    • Ventii, K. H., N. S. Devi, K. L. Friedrich, T. A. Chernova, M. Tighiouart, E. G. Van Meir, and K. D. Wilkinson. 2008. BRCAl-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization. Cancer Res. 68:6953-6962.
    • (2008) Cancer Res , vol.68 , pp. 6953-6962
    • Ventii, K.H.1    Devi, N.S.2    Friedrich, K.L.3    Chernova, T.A.4    Tighiouart, M.5    Van Meir, E.G.6    Wilkinson, K.D.7
  • 42
    • 0033816990 scopus 로고    scopus 로고
    • HCF-1 amino-and carboxy-terminal subunit association through two separate sets of interaction modules: Involvement of fibronectin type 3 repeats
    • Wilson, A. C., M. Boutros, K. M. Johnson, and W. Herr. 2000. HCF-1 amino-and carboxy-terminal subunit association through two separate sets of interaction modules: involvement of fibronectin type 3 repeats. Mol. Cell. Biol. 20:6721-6730.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 6721-6730
    • Wilson, A.C.1    Boutros, M.2    Johnson, K.M.3    Herr, W.4
  • 43
    • 0030863636 scopus 로고    scopus 로고
    • Wilson, A, C, R. N. Freiman, H. Goto, T. Nishimoto, and W. Herr. 1997. VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. Mol. Cell. Biol. 17:6139-6146.
    • Wilson, A, C, R. N. Freiman, H. Goto, T. Nishimoto, and W. Herr. 1997. VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. Mol. Cell. Biol. 17:6139-6146.
  • 44
    • 0028860944 scopus 로고
    • The HCF repeat is an unusual proteolytic cleavage signal
    • Wilson, A. C, M. G. Peterson, and W. Herr. 1995. The HCF repeat is an unusual proteolytic cleavage signal. Genes Dev. 9:2445-2458.
    • (1995) Genes Dev , vol.9 , pp. 2445-2458
    • Wilson, A.C.1    Peterson, M.G.2    Herr, W.3
  • 45
    • 0037401872 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: The importance of driving in reverse along the ubiquitin-proteasome pathway
    • Wing, S. S. 2003. Deubiquitinating enzymes: the importance of driving in reverse along the ubiquitin-proteasome pathway. Int. J. Biochem. Cell Biol. 35:590-605.
    • (2003) Int. J. Biochem. Cell Biol , vol.35 , pp. 590-605
    • Wing, S.S.1
  • 46
    • 0038434062 scopus 로고    scopus 로고
    • The herpes simplex virus VP16-induced complex: The makings of a regulatory switch
    • Wysocka, J., and W. Herr. 2003. The herpes simplex virus VP16-induced complex: the makings of a regulatory switch. Trends Biochem. Sci. 28:294-304.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 294-304
    • Wysocka, J.1    Herr, W.2
  • 47
    • 0037382574 scopus 로고    scopus 로고
    • Human Sin3 deacetylase and trithorax-related Setl/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1
    • Wysocka, J., M. P. Myers, C. D. Laherty, R. N. Eisenman, and W. Herr. 2003. Human Sin3 deacetylase and trithorax-related Setl/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 17:896-911.
    • (2003) Genes Dev , vol.17 , pp. 896-911
    • Wysocka, J.1    Myers, M.P.2    Laherty, C.D.3    Eisenman, R.N.4    Herr, W.5
  • 48
    • 0035019156 scopus 로고    scopus 로고
    • Loss of HCF-1 -chromatin association precedes temperature-induced growth arrest of tsBN67 cells
    • Wysocka, J., P. T. Reilly, and W. Herr. 2001. Loss of HCF-1 -chromatin association precedes temperature-induced growth arrest of tsBN67 cells. Mol. Cell. Biol. 21:3820-3829.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 3820-3829
    • Wysocka, J.1    Reilly, P.T.2    Herr, W.3
  • 50
    • 2942715029 scopus 로고    scopus 로고
    • Leukemia proto-oncoprotein MLL forms a SETl-like histone methyltransferase complex with menin to regulate Hox gene expression
    • Yokoyama, A., Z. Wang, J. Wysocka, M. Sanyal, D. J. Aufiero, I. Kitabayashi, W. Herr, and M. L. Cleary. 2004. Leukemia proto-oncoprotein MLL forms a SETl-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol. Cell. Biol. 24:5639-5649.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 5639-5649
    • Yokoyama, A.1    Wang, Z.2    Wysocka, J.3    Sanyal, M.4    Aufiero, D.J.5    Kitabayashi, I.6    Herr, W.7    Cleary, M.L.8


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