메뉴 건너뛰기




Volumn 116, Issue 4, 2010, Pages 603-613

Dimer-tetramer transition controls RUNX1/ETO leukemogenic activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL PROTEIN; DIMER; DNA; HYBRID PROTEIN; PROTEIN ETO; TETRAMER; TRANSCRIPTION FACTOR RUNX1; UNCLASSIFIED DRUG; MUTANT PROTEIN; ONCOPROTEIN; RUNX1T1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR;

EID: 77956017878     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2009-10-248047     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 0030658039 scopus 로고    scopus 로고
    • Oncogenic transcription factors in the human acute leukemias
    • DOI 10.1126/science.278.5340.1059
    • Look AT. Oncogenic transcription factors in the human acute leukemias. Science. 1997;278(5340):1059-1064. (Pubitemid 27517875)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1059-1064
    • Look, A.T.1
  • 2
    • 0037315894 scopus 로고    scopus 로고
    • Disruption of differentiation in human cancer: AML shows the way
    • Tenen DG. Disruption of differentiation in human cancer: AML shows the way. Nat Rev Cancer. 2003;3(2):89-101.
    • (2003) Nat Rev Cancer , vol.3 , Issue.2 , pp. 89-101
    • Tenen, D.G.1
  • 3
    • 10344255679 scopus 로고    scopus 로고
    • Deletion of an AML1-ETO C-terminal NcoR/SMRT-interacting region strongly induces leukemia development
    • Yan M, Burel SA, Peterson LF, et al. Deletion of an AML1-ETO C-terminal NcoR/SMRT-interacting region strongly induces leukemia development. Proc Natl Acad Sci U S A. 2004;101(49):17186-17191.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.49 , pp. 17186-17191
    • Yan, M.1    Burel, S.A.2    Peterson, L.F.3
  • 4
    • 33746843079 scopus 로고    scopus 로고
    • A previously unidentified alternatively spliced isoform of t(8;21) transcript promotes leukemogenesis
    • Yan M, Kanbe E, Peterson LF, et al. A previously unidentified alternatively spliced isoform of t(8;21) transcript promotes leukemogenesis. Nat Med. 2006;12(8):945-949.
    • (2006) Nat Med , vol.12 , Issue.8 , pp. 945-949
    • Yan, M.1    Kanbe, E.2    Peterson, L.F.3
  • 5
    • 4344669438 scopus 로고    scopus 로고
    • E protein silencing by the leukemogenic AML1-ETO fusion protein
    • DOI 10.1126/science.1097937
    • Zhang J, Kalkum M, Yamamura S, Chait BT, Roeder RG. E protein silencing by the leukemogenic AML1-ETO fusion protein. Science. 2004;305(5688):1286-1289. (Pubitemid 39129232)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1286-1289
    • Zhang, J.1    Kalkum, M.2    Yamamura, S.3    Chait, B.T.4    Roeder, R.G.5
  • 6
    • 57149101138 scopus 로고    scopus 로고
    • AML1/ETO oncoprotein is directed to AML1 binding regions and co-localizes with AML1 and HEB on its targets
    • Gardini A, Cesaroni M, Luzi L, et al. AML1/ETO oncoprotein is directed to AML1 binding regions and co-localizes with AML1 and HEB on its targets. PLoS Genet. 2008;4(11):e1000275.
    • (2008) PLoS Genet , vol.4 , Issue.11
    • Gardini, A.1    Cesaroni, M.2    Luzi, L.3
  • 7
    • 55949087445 scopus 로고    scopus 로고
    • Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding and promotes leukemogenesis
    • Ahn EY, Yan M, Malakhova OA, et al. Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding and promotes leukemogenesis. Proc Natl Acad Sci U S A. 2008;105(44):17103-17108.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.44 , pp. 17103-17108
    • Ahn, E.Y.1    Yan, M.2    Malakhova, O.A.3
  • 8
    • 2942612214 scopus 로고    scopus 로고
    • ETO interacting proteins
    • Hug BA, Lazar MA. ETO interacting proteins. Oncogene. 2004;23(24):4270-4274.
    • (2004) Oncogene , vol.23 , Issue.24 , pp. 4270-4274
    • Hug, B.A.1    Lazar, M.A.2
  • 9
    • 0031724804 scopus 로고    scopus 로고
    • ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors
    • Lutterbach B, Westendorf JJ, Linggi B, et al. ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors. Mol Cell Biol. 1998;18(12):7176-7184.
    • (1998) Mol Cell Biol , vol.18 , Issue.12 , pp. 7176-7184
    • Lutterbach, B.1    Westendorf, J.J.2    Linggi, B.3
  • 11
    • 10344249429 scopus 로고    scopus 로고
    • The nuclear receptor co-repressor (N-CoR) utilizes repression domains I and III for interaction and co-repression with ETO
    • Lausen J, Cho S, Liu S, Werner MH. The nuclear receptor co-repressor (N-CoR) utilizes repression domains I and III for interaction and co-repression with ETO. J Biol Chem. 2004;279(47):49281-49288.
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 49281-49288
    • Lausen, J.1    Cho, S.2    Liu, S.3    Werner, M.H.4
  • 12
    • 33645778328 scopus 로고    scopus 로고
    • The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity
    • Liu Y, Cheney MD, Gaudet JJ, et al. The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity. Cancer Cell. 2006;9(4):249-260.
    • (2006) Cancer Cell , vol.9 , Issue.4 , pp. 249-260
    • Liu, Y.1    Cheney, M.D.2    Gaudet, J.J.3
  • 13
    • 59649122714 scopus 로고    scopus 로고
    • RUNX1/AML1 DNA-binding domain and ETO/MTG8 NHR2-dimerization domain are critical to AML1-ETO9a leukemogenesis
    • Yan M, Ahn EY, Hiebert SW, Zhang DE. RUNX1/AML1 DNA-binding domain and ETO/MTG8 NHR2-dimerization domain are critical to AML1-ETO9a leukemogenesis. Blood. 2009;113(4):883-886.
    • (2009) Blood , vol.113 , Issue.4 , pp. 883-886
    • Yan, M.1    Ahn, E.Y.2    Hiebert, S.W.3    Zhang, D.E.4
  • 14
    • 33947277861 scopus 로고    scopus 로고
    • Targeting the oligomerization domain of ETO interferes with RUNX1/ETO oncogenic activity in t(8;21)-positive leukemic cells
    • Wichmann C, Chen L, Heinrich M, et al. Targeting the oligomerization domain of ETO interferes with RUNX1/ETO oncogenic activity in t(8;21)-positive leukemic cells. Cancer Res. 2007;67(5):2280-2289.
    • (2007) Cancer Res , vol.67 , Issue.5 , pp. 2280-2289
    • Wichmann, C.1    Chen, L.2    Heinrich, M.3
  • 15
    • 0034665765 scopus 로고    scopus 로고
    • Analysis of the role of AML1-ETO in leukemogenesis, using an inducible transgenic mouse model
    • Rhoades KL, Hetherington CJ, Harakawa N, et al. Analysis of the role of AML1-ETO in leukemogenesis, using an inducible transgenic mouse model. Blood. 2000;96(6):2108-2115.
    • (2000) Blood , vol.96 , Issue.6 , pp. 2108-2115
    • Rhoades, K.L.1    Hetherington, C.J.2    Harakawa, N.3
  • 16
    • 0038047685 scopus 로고    scopus 로고
    • AML1/MTG8 oncogene suppression by small interfering RNAs supports myeloid differentiation of t(8;21)-positive leukemic cells
    • Heidenreich O, Krauter J, Riehle H, et al. AML1/MTG8 oncogene suppression by small interfering RNAs supports myeloid differentiation of t(8;21)-positive leukemic cells. Blood. 2003;101(8):3157-3163.
    • (2003) Blood , vol.101 , Issue.8 , pp. 3157-3163
    • Heidenreich, O.1    Krauter, J.2    Riehle, H.3
  • 17
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormone-receptor interface. Science. 1995;267(5196):383-386.
    • (1995) Science , vol.267 , Issue.5196 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 18
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol. 1998;280(1):1-9.
    • (1998) J Mol Biol , vol.280 , Issue.1 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 19
    • 33748578600 scopus 로고    scopus 로고
    • Targeting protein-protein interactions with small molecules: Challenges and perspectives for computational binding epitope detection and ligand finding
    • DOI 10.2174/092986706778201530
    • Gonzalez-Ruiz D, Gohlke H. Targeting protein-protein interactions with small molecules: challenges and perspectives for computational binding epitope detection and ligand finding. Curr Med Chem. 2006;13(22):2607-2625. (Pubitemid 44364140)
    • (2006) Current Medicinal Chemistry , vol.13 , Issue.22 , pp. 2607-2625
    • Gonzalez-Ruiz, D.1    Gohlke, H.2
  • 20
    • 23444454552 scopus 로고    scopus 로고
    • The Amber biomolecular simulation programs
    • Case DA, Cheatham TE 3rd, Darden T, et al. The Amber biomolecular simulation programs. J Comput Chem. 2005;26(16):1668-1688.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1668-1688
    • Case, D.A.1    Cheatham III, T.E.2    Darden, T.3
  • 21
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell WD, Cieplak CI, Bayly IR, et al. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J Am Chem Soc. 1995;117(19):5179-5197.
    • (1995) J Am Chem Soc , vol.117 , Issue.19 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, C.I.2    Bayly, I.R.3
  • 22
    • 0037174385 scopus 로고    scopus 로고
    • Allatom structure prediction and folding simulations of a stable protein
    • Simmerling C, Strockbine B, Roitberg AE. Allatom structure prediction and folding simulations of a stable protein. J Am Chem Soc. 2002;124(38):11258- 11259.
    • (2002) J Am Chem Soc , vol.124 , Issue.38 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 23
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J. 2000;78(3):1606-1619.
    • (2000) Biophys J , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 24
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J. 2002;82(2):1096-1111. (Pubitemid 34111246)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Hewlett, G.J.4    Schubert, D.5
  • 25
    • 20144384488 scopus 로고    scopus 로고
    • Optimized retroviral transduction protocol which preserves the primitive subpopulation of human hematopoietic cells
    • Tonks A, Tonks AJ, Pearn L, Mohamad Z, Burnett AK, Darley RL. Optimized retroviral transduction protocol which preserves the primitive subpopulation of human hematopoietic cells. Biotechnol Prog. 2005;21(3):953-958.
    • (2005) Biotechnol Prog , vol.21 , Issue.3 , pp. 953-958
    • Tonks, A.1    Tonks, A.J.2    Pearn, L.3    Mohamad, Z.4    Burnett, A.K.5    Darley, R.L.6
  • 26
    • 62449178451 scopus 로고    scopus 로고
    • Transforming activity of AML1-ETO is independent of CBFbeta and ETO interaction but requires formation of homo-oligomeric complexes
    • Kwok C, Zeisig BB, Qiu J, Dong S, So CW. Transforming activity of AML1-ETO is independent of CBFbeta and ETO interaction but requires formation of homo-oligomeric complexes. Proc Natl Acad Sci U S A. 2009;106(8):2853-2858.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.8 , pp. 2853-2858
    • Kwok, C.1    Zeisig, B.B.2    Qiu, J.3    Dong, S.4    So, C.W.5
  • 27
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H, Kiel C, Case DA. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol. 2003;330(4):891-913.
    • (2003) J Mol Biol , vol.330 , Issue.4 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 28
    • 0035895423 scopus 로고    scopus 로고
    • Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase
    • DOI 10.1006/jmbi.2000.4285
    • Archontis G, Simonson T, Karplus M. Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations: application to amino acid recognition by aspartyl-tRNA synthetase. J Mol Biol. 2001;306(2):307-327. (Pubitemid 33032882)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.2 , pp. 307-327
    • Archontis, G.1    Simonson, T.2    Karplus, M.3
  • 29
    • 0032789936 scopus 로고    scopus 로고
    • Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding
    • Hendsch ZS, Tidor B. Electrostatic interactions in the GCN4 leucine zipper: substantial contributions arise from intramolecular interactions enhanced on binding. Protein Sci. 1999;8(7):1381-1392.
    • (1999) Protein Sci , vol.8 , Issue.7 , pp. 1381-1392
    • Hendsch, Z.S.1    Tidor, B.2
  • 30
    • 54049106547 scopus 로고    scopus 로고
    • Transcriptional repression of the RUNX3/AML2 gene by the t(8;21) and inv(16) fusion proteins in acute myeloid leukemia
    • Cheng CK, Li L, Cheng SH, et al. Transcriptional repression of the RUNX3/AML2 gene by the t(8;21) and inv(16) fusion proteins in acute myeloid leukemia. Blood. 2008;112(8):3391-3402.
    • (2008) Blood , vol.112 , Issue.8 , pp. 3391-3402
    • Cheng, C.K.1    Li, L.2    Cheng, S.H.3
  • 31
    • 37549052500 scopus 로고    scopus 로고
    • PU.1 is a major downstream target of AML1 (RUNX1) in adult mouse hematopoiesis
    • Huang G, Zhang P, Hirai H, et al. PU.1 is a major downstream target of AML1 (RUNX1) in adult mouse hematopoiesis. Nat Genet. 2008;40(1):51-60.
    • (2008) Nat Genet , vol.40 , Issue.1 , pp. 51-60
    • Huang, G.1    Zhang, P.2    Hirai, H.3
  • 32
    • 51649109222 scopus 로고    scopus 로고
    • t(8;21)(q22;q22) fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression
    • Okumura AJ, Peterson LF, Okumura F, Boyapati A, Zhang DE. t(8;21)(q22;q22) fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression. Blood. 2008;112(4):1392-1401.
    • (2008) Blood , vol.112 , Issue.4 , pp. 1392-1401
    • Okumura, A.J.1    Peterson, L.F.2    Okumura, F.3    Boyapati, A.4    Zhang, D.E.5
  • 33
    • 0035831044 scopus 로고    scopus 로고
    • Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta
    • Tahirov TH, Inoue-Bungo T, Morii H, et al. Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta. Cell. 2001;104(5):755-767.
    • (2001) Cell , vol.104 , Issue.5 , pp. 755-767
    • Tahirov, T.H.1    Inoue-Bungo, T.2    Morii, H.3
  • 34
    • 0034941566 scopus 로고    scopus 로고
    • Dichotomy of AML1-ETO functions: Growth arrest versus block of differentiation
    • DOI 10.1128/MCB.21.16.5577-5590.2001
    • Burel SA, Harakawa N, Zhou L, Pabst T, Tenen DG, Zhang DE. Dichotomy of AML1-ETO functions: growth arrest versus block of differentiation. Mol Cell Biol. 2001;21(16):5577-5590. (Pubitemid 32702461)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.16 , pp. 5577-5590
    • Burel, S.A.1    Harakawa, N.2    Zhou, L.3    Pabst, T.4    Tenen, D.G.5    Zhang, D.-E.6
  • 35
    • 0036095217 scopus 로고    scopus 로고
    • The AML1-ETO fusion protein promotes the expansion of human hematopoietic stem cells
    • Mulloy JC, Cammenga J, MacKenzie KL, Berguido FJ, Moore MA, Nimer SD. The AML1-ETO fusion protein promotes the expansion of human hematopoietic stem cells. Blood. 2002;99(1):15-23.
    • (2002) Blood , vol.99 , Issue.1 , pp. 15-23
    • Mulloy, J.C.1    Cammenga, J.2    MacKenzie, K.L.3    Berguido, F.J.4    Moore, M.A.5    Nimer, S.D.6
  • 36
    • 0037092966 scopus 로고    scopus 로고
    • Cooperative function of Aml1-ETO corepressor recruitment domains in the expansion of primary bone marrow cells
    • Hug BA, Lee SY, Kinsler EL, Zhang J, Lazar MA. Cooperative function of Aml1-ETO corepressor recruitment domains in the expansion of primary bone marrow cells. Cancer Res. 2002;62(10):2906-2912.
    • (2002) Cancer Res , vol.62 , Issue.10 , pp. 2906-2912
    • Hug, B.A.1    Lee, S.Y.2    Kinsler, E.L.3    Zhang, J.4    Lazar, M.A.5
  • 37
    • 0036463950 scopus 로고    scopus 로고
    • Expression of a conditional AML1-ETO oncogene bypasses embryonic lethality and establishes a murine model of human t(8;21) acute myeloid leukemia
    • Higuchi M, O'Brien D, Kumaravelu P, Lenny N, Yeoh EJ, Downing JR. Expression of a conditional AML1-ETO oncogene bypasses embryonic lethality and establishes a murine model of human t(8;21) acute myeloid leukemia. Cancer Cell. 2002;1(1):63-74.
    • (2002) Cancer Cell , vol.1 , Issue.1 , pp. 63-74
    • Higuchi, M.1    O'Brien, D.2    Kumaravelu, P.3    Lenny, N.4    Yeoh, E.J.5    Downing, J.R.6
  • 39
    • 19944431828 scopus 로고    scopus 로고
    • Stat5 tetramer formation is associated with leukemogenesis
    • Moriggl R, Sexl V, Kenner L, et al. Stat5 tetramer formation is associated with leukemogenesis. Cancer Cell. 2005;7(1):87-99.
    • (2005) Cancer Cell , vol.7 , Issue.1 , pp. 87-99
    • Moriggl, R.1    Sexl, V.2    Kenner, L.3
  • 40
    • 0035066381 scopus 로고    scopus 로고
    • The leukemia-associated AML1 (Runx1)-CBF beta complex functions as a DNA-induced molecular clamp
    • Bravo J, Li Z, Speck NA, Warren AJ. The leukemia-associated AML1 (Runx1)-CBF beta complex functions as a DNA-induced molecular clamp. Nat Struct Biol. 2001;8(4):371-378.
    • (2001) Nat Struct Biol , vol.8 , Issue.4 , pp. 371-378
    • Bravo, J.1    Li, Z.2    Speck, N.A.3    Warren, A.J.4
  • 41
  • 42
    • 0034708704 scopus 로고    scopus 로고
    • Biophysical characterization of interactions between the core binding factor alpha and beta subunits and DNA
    • Tang YY, Crute BE, Kelley JJ, et al. Biophysical characterization of interactions between the core binding factor alpha and beta subunits and DNA. FEBS Lett. 2000;470(2):167-172.
    • (2000) FEBS Lett , vol.470 , Issue.2 , pp. 167-172
    • Tang, Y.Y.1    Crute, B.E.2    Kelley, J.J.3
  • 43
    • 2942682886 scopus 로고    scopus 로고
    • Role of the TEL-AML1 fusion gene in the molecular pathogenesis of childhood acute lymphoblastic leukaemia
    • Zelent A, Greaves M, Enver T. Role of the TEL-AML1 fusion gene in the molecular pathogenesis of childhood acute lymphoblastic leukaemia. Oncogene. 2004;23(24):4275-4283.
    • (2004) Oncogene , vol.23 , Issue.24 , pp. 4275-4283
    • Zelent, A.1    Greaves, M.2    Enver, T.3
  • 45
    • 0034228707 scopus 로고    scopus 로고
    • Peptide and protein recognition by designed molecules
    • Peczuh MW, Hamilton AD. Peptide and protein recognition by designed molecules. Chem Rev. 2000;100(7):2479-2494.
    • (2000) Chem Rev , vol.100 , Issue.7 , pp. 2479-2494
    • Peczuh, M.W.1    Hamilton, A.D.2
  • 46
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • Toogood PL. Inhibition of protein-protein association by small molecules: approaches and progress. J Med Chem. 2002;45(8):1543-1558.
    • (2002) J Med Chem , vol.45 , Issue.8 , pp. 1543-1558
    • Toogood, P.L.1
  • 48
    • 13844272064 scopus 로고    scopus 로고
    • Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces
    • DOI 10.1016/j.str.2004.12.012
    • Li Y, Huang Y, Swaminathan CP, Smith-Gill SJ, Mariuzza RA. Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces. Structure. 2005;13(2):297-307. (Pubitemid 40247705)
    • (2005) Structure , vol.13 , Issue.2 , pp. 297-307
    • Li, Y.1    Huang, Y.2    Swaminathan, C.P.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 49
    • 0037452709 scopus 로고    scopus 로고
    • Binding of small molecules to an adaptive protein-protein interface
    • Arkin MR, Randal M, DeLano WL, et al. Binding of small molecules to an adaptive protein-protein interface. Proc Natl Acad Sci U S A. 2003;100(4):1603-1608.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.4 , pp. 1603-1608
    • Arkin, M.R.1    Randal, M.2    DeLano, W.L.3
  • 50
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov. 2004;3(4):301-317.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 51
    • 0033638969 scopus 로고    scopus 로고
    • Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation
    • Minucci S, Maccarana M, Cioce M, et al. Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation. Mol Cell. 2000;5(5):811-820.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 811-820
    • Minucci, S.1    Maccarana, M.2    Cioce, M.3
  • 52
    • 0033634946 scopus 로고    scopus 로고
    • Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers
    • Lin RJ, Evans RM. Acquisition of oncogenic potential by RAR chimeras in acute promyelocytic leukemia through formation of homodimers. Mol Cell. 2000;5(5):821-830.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 821-830
    • Lin, R.J.1    Evans, R.M.2
  • 53
    • 3843124232 scopus 로고    scopus 로고
    • Dimerization: A versatile switch for oncogenesis
    • So CW, Cleary ML. Dimerization: a versatile switch for oncogenesis. Blood. 2004;104(4):919-922.
    • (2004) Blood , vol.104 , Issue.4 , pp. 919-922
    • So, C.W.1    Cleary, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.