메뉴 건너뛰기




Volumn 36, Issue 1, 2009, Pages 39-50

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases

Author keywords

PROTEINS

Indexed keywords

CELL PROTEIN; CI PROTEIN; DEOXYRIBONUCLEOPROTEIN; MACROLH2A PROTEIN; PHOSPHATASE; PUC PROTEIN; REGULATOR PROTEIN; SPOP PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; UNCLASSIFIED DRUG;

EID: 70349769327     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.09.022     Document Type: Article
Times cited : (374)

References (60)
  • 1
    • 27744494043 scopus 로고    scopus 로고
    • Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival
    • Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., and Yang Y. Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. Nature 438 (2005) 224-228
    • (2005) Nature , vol.438 , pp. 224-228
    • Allen, E.1    Ding, J.2    Wang, W.3    Pramanik, S.4    Chou, J.5    Yau, V.6    Yang, Y.7
  • 2
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., and Zheng N. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443 (2006) 590-593
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 3
    • 33645714061 scopus 로고    scopus 로고
    • The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation
    • Angers S., Thorpe C.J., Biechele T.L., Goldenberg S.J., Zheng N., MacCoss M.J., and Moon R.T. The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation. Nat. Cell Biol. 8 (2006) 348-357
    • (2006) Nat. Cell Biol. , vol.8 , pp. 348-357
    • Angers, S.1    Thorpe, C.J.2    Biechele, T.L.3    Goldenberg, S.J.4    Zheng, N.5    MacCoss, M.J.6    Moon, R.T.7
  • 4
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., and Elledge S.J. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86 (1996) 263-274
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 5
    • 0028040875 scopus 로고
    • The POZ domain: a conserved protein-protein interaction motif
    • Bardwell V.J., and Treisman R. The POZ domain: a conserved protein-protein interaction motif. Genes Dev. 8 (1994) 1664-1677
    • (1994) Genes Dev. , vol.8 , pp. 1664-1677
    • Bardwell, V.J.1    Treisman, R.2
  • 6
    • 55149099596 scopus 로고    scopus 로고
    • Characterization of RhoBTB-dependent Cul3 ubiquitin ligase complexes-evidence for an autoregulatory mechanism
    • Berthold J., Schenková K., Ramos S., Miura Y., Furukawa M., Aspenström P., and Rivero F. Characterization of RhoBTB-dependent Cul3 ubiquitin ligase complexes-evidence for an autoregulatory mechanism. Exp. Cell Res. 314 (2008) 3453-3465
    • (2008) Exp. Cell Res. , vol.314 , pp. 3453-3465
    • Berthold, J.1    Schenková, K.2    Ramos, S.3    Miura, Y.4    Furukawa, M.5    Aspenström, P.6    Rivero, F.7
  • 7
    • 40749153516 scopus 로고    scopus 로고
    • Cullin-RING ubiquitin ligases: global regulation and activation cycles
    • Bosu D.R., and Kipreos E.T. Cullin-RING ubiquitin ligases: global regulation and activation cycles. Cell Div. 3 (2008) 7
    • (2008) Cell Div. , vol.3 , pp. 7
    • Bosu, D.R.1    Kipreos, E.T.2
  • 8
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: insights into a molecular machine
    • Cardozo T., and Pagano M. The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol. 5 (2004) 739-751
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 9
    • 33947261954 scopus 로고    scopus 로고
    • Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells-evidence for Cullin dimerization
    • Chew E.H., Poobalasingam T., Hawkey C.J., and Hagen T. Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells-evidence for Cullin dimerization. Cell. Signal. 19 (2007) 1071-1080
    • (2007) Cell. Signal. , vol.19 , pp. 1071-1080
    • Chew, E.H.1    Poobalasingam, T.2    Hawkey, C.J.3    Hagen, T.4
  • 10
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan S.B., Gordan J.D., Jin J., Harper J.W., and Diehl J.A. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol. Cell. Biol. 24 (2004) 8477-8486
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 11
    • 0031717483 scopus 로고    scopus 로고
    • Genetic and molecular characterization of the Caenorhabditis elegans gene, mel-26, a postmeiotic negative regulator of mei-1, a meiotic-specific spindle component
    • Dow M.R., and Mains P.E. Genetic and molecular characterization of the Caenorhabditis elegans gene, mel-26, a postmeiotic negative regulator of mei-1, a meiotic-specific spindle component. Genetics 150 (1998) 119-128
    • (1998) Genetics , vol.150 , pp. 119-128
    • Dow, M.R.1    Mains, P.E.2
  • 12
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of Cullin-RING ligases: conformational control of conjugation
    • Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., and Schulman B.A. Structural insights into NEDD8 activation of Cullin-RING ligases: conformational control of conjugation. Cell 134 (2008) 995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 13
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman R.M., Correll C.C., Kaplan K.B., and Deshaies R.J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91 (1997) 221-230
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 14
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa M., He Y.J., Borchers C., and Xiong Y. Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nat. Cell Biol. 5 (2003) 1001-1007
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 15
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R., Wee S., Anderson S., Yates J., and Wolf D.A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12 (2003) 783-790
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 16
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • Hao B., Oehlmann S., Sowa M.E., Harper J.W., and Pavletich N.P. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol. Cell 26 (2007) 131-143
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 18
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., and Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13 (1999) 76-86
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 19
    • 0036282703 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: an extended look
    • Jackson P.K., and Eldridge A.G. The SCF ubiquitin ligase: an extended look. Mol. Cell 9 (2002) 923-925
    • (2002) Mol. Cell , vol.9 , pp. 923-925
    • Jackson, P.K.1    Eldridge, A.G.2
  • 20
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • Jiang J., and Struhl G. Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature 391 (1998) 493-496
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 21
    • 33646875414 scopus 로고    scopus 로고
    • Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus
    • Kent D., Bush E.W., and Hooper J.E. Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus. Development 133 (2006) 2001-2010
    • (2006) Development , vol.133 , pp. 2001-2010
    • Kent, D.1    Bush, E.W.2    Hooper, J.E.3
  • 22
    • 0242525238 scopus 로고    scopus 로고
    • BTB proteins as henchmen of Cul3-based ubiquitin ligases
    • Krek W. BTB proteins as henchmen of Cul3-based ubiquitin ligases. Nat. Cell Biol. 5 (2003) 950-951
    • (2003) Nat. Cell Biol. , vol.5 , pp. 950-951
    • Krek, W.1
  • 23
    • 33646886500 scopus 로고    scopus 로고
    • BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase
    • Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., et al. BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase. J. Biol. Chem. 281 (2006) 12664-12672
    • (2006) J. Biol. Chem. , vol.281 , pp. 12664-12672
    • Kwon, J.E.1    La, M.2    Oh, K.H.3    Oh, Y.M.4    Kim, G.R.5    Seol, J.H.6    Baek, S.H.7    Chiba, T.8    Tanaka, K.9    Bang, O.S.10
  • 24
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase
    • Li T., Chen X., Garbutt K.C., Zhou P., and Zheng N. Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase. Cell 124 (2006) 105-117
    • (2006) Cell , vol.124 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 26
    • 33747606306 scopus 로고    scopus 로고
    • Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
    • Lo S.C., Li X., Henzl M.T., Beamer L.J., and Hannink M. Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. EMBO J. 25 (2006) 3605-3617
    • (2006) EMBO J. , vol.25 , pp. 3605-3617
    • Lo, S.C.1    Li, X.2    Henzl, M.T.3    Beamer, L.J.4    Hannink, M.5
  • 28
    • 0037821802 scopus 로고    scopus 로고
    • Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon M., Itoh K., Yamamoto M., and Hayes J.D. Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J. Biol. Chem. 278 (2003) 21592-21600
    • (2003) J. Biol. Chem. , vol.278 , pp. 21592-21600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 29
    • 0037462424 scopus 로고    scopus 로고
    • Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase
    • Orlicky S., Tang X., Willems A., Tyers M., and Sicheri F. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 112 (2003) 243-256
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 31
    • 0032031607 scopus 로고    scopus 로고
    • Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box proteincomplexes that regulate cell division and methionine biosynthesis in yeast
    • Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., and Tyers M. Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box proteincomplexes that regulate cell division and methionine biosynthesis in yeast. Genes Dev. 12 (1998) 692-705
    • (1998) Genes Dev. , vol.12 , pp. 692-705
    • Patton, E.E.1    Willems, A.R.2    Sa, D.3    Kuras, L.4    Thomas, D.5    Craig, K.L.6    Tyers, M.7
  • 32
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., and Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6 (2005) 9-20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 34
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • Pintard L., Willems A., and Peter M. Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. EMBO J. 23 (2004) 1681-1687
    • (2004) EMBO J. , vol.23 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 36
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha A., and Deshaies R.J. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 32 (2008) 21-31
    • (2008) Mol. Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 37
    • 33845978455 scopus 로고    scopus 로고
    • Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway
    • Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., and Marshall J. Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway. J. Biol. Chem. 281 (2006) 40164-40173
    • (2006) J. Biol. Chem. , vol.281 , pp. 40164-40173
    • Salinas, G.D.1    Blair, L.A.2    Needleman, L.A.3    Gonzales, J.D.4    Chen, Y.5    Li, M.6    Singer, J.D.7    Marshall, J.8
  • 41
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra D., Craig K.L., Tyers M., Elledge S.J., and Harper J.W. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91 (1997) 209-219
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 42
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • Stebbins C.E., Kaelin Jr. W.G., and Pavletich N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284 (1999) 455-461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 47
    • 35648970026 scopus 로고    scopus 로고
    • Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response
    • Tong K.I., Padmanabhan B., Kobayashi A., Shang C., Hirotsu Y., Yokoyama S., and Yamamoto M. Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Mol. Cell. Biol. 27 (2007) 7511-7521
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7511-7521
    • Tong, K.I.1    Padmanabhan, B.2    Kobayashi, A.3    Shang, C.4    Hirotsu, Y.5    Yokoyama, S.6    Yamamoto, M.7
  • 49
    • 34047255191 scopus 로고    scopus 로고
    • Fbw7/hCDC4 dimerization regulates its substrate interactions
    • Welcker M., and Clurman B.E. Fbw7/hCDC4 dimerization regulates its substrate interactions. Cell Div. 2 (2007) 7
    • (2007) Cell Div. , vol.2 , pp. 7
    • Welcker, M.1    Clurman, B.E.2
  • 51
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • Willems A.R., Schwab M., and Tyers M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695 (2004) 133-170
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 52
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu L., Wei Y., Reboul J., Vaglio P., Shin T.H., Vidal M., Elledge S.J., and Harper J.W. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425 (2003) 316-321
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8
  • 53
    • 50449110781 scopus 로고    scopus 로고
    • Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail
    • Yamoah K., Oashi T., Sarikas A., Gazdoiu S., Osman R., and Pan Z.Q. Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail. Proc. Natl. Acad. Sci. USA 105 (2008) 12230-12235
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12230-12235
    • Yamoah, K.1    Oashi, T.2    Sarikas, A.3    Gazdoiu, S.4    Osman, R.5    Pan, Z.Q.6
  • 56
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang D.D., and Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23 (2003) 8137-8151
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 57
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang D.D., Lo S.C., Cross J.V., Templeton D.J., and Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol. Cell. Biol. 24 (2004) 10941-10953
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 58
    • 33646893705 scopus 로고    scopus 로고
    • A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor
    • Zhang Q., Zhang L., Wang B., Ou C.Y., Chien C.T., and Jiang J. A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor. Dev. Cell 10 (2006) 719-729
    • (2006) Dev. Cell , vol.10 , pp. 719-729
    • Zhang, Q.1    Zhang, L.2    Wang, B.3    Ou, C.Y.4    Chien, C.T.5    Jiang, J.6
  • 60
    • 0028110129 scopus 로고
    • The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila
    • Zollman S., Godt D., Privé G.G., Couderc J.L., and Laski F.A. The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. Proc. Natl. Acad. Sci. USA 91 (1994) 10717-10721
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10717-10721
    • Zollman, S.1    Godt, D.2    Privé, G.G.3    Couderc, J.L.4    Laski, F.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.