메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Stability of HIB-Cul3 E3 ligase adaptor HIB Is Regulated by Self-degradation and Availability of Its Substrates

Author keywords

[No Author keywords available]

Indexed keywords

DROSOPHILA PROTEIN; PROTEASOME; UBIQUITIN PROTEIN LIGASE;

EID: 84939185883     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep12709     Document Type: Article
Times cited : (20)

References (55)
  • 1
    • 0028935165 scopus 로고
    • Ubiquitin proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. Ubiquitin proteasomes, and the regulation of intracellular protein degradation. Current opinion in cell biology 7, 215-223 (1995).
    • (1995) Current Opinion in Cell Biology , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 2
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Seminars in cell & developmental biology 11, 141-148, doi: 10.1006/scdb.2000.0164 (2000).
    • (2000) Seminars in Cell & Developmental Biology , vol.11 , pp. 141-148
    • Wilkinson . K, D.1
  • 3
    • 0027022693 scopus 로고
    • Ubiquitin and intracellular protein degradation
    • Hochstrasser, M. Ubiquitin and intracellular protein degradation. Current opinion in cell biology 4, 1024-1031 (1992).
    • (1992) Current Opinion in Cell Biology , vol.4 , pp. 1024-1031
    • Hochstrasser, M.1
  • 4
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. Ubiquitin-dependent protein degradation. Annual review of genetics 30, 405-439, doi: 10.1146/annurev. genet.30.1.405 (1996).
    • (1996) Annual Review of Genetics , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 5
    • 0034680909 scopus 로고    scopus 로고
    • Recognition and ubiquitination of Notch by Itch, a hect-type E3 ubiquitin ligase
    • Qiu, L. et al. Recognition and ubiquitination of Notch by Itch, a hect-type E3 ubiquitin ligase. The Journal of biological chemistry 275, 35734-35737, doi: 10.1074/jbc.M007300200 (2000).
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 35734-35737
    • Qiu, L.1
  • 6
    • 81755171430 scopus 로고    scopus 로고
    • Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination
    • Liu, J. & Nussinov, R. Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination. The Journal of biological chemistry 286, 40934-40942, doi: 10.1074/jbc.M111.277236 (2011).
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 40934-40942
    • Liu, J.1    Nussinov, R.2
  • 7
    • 28844496621 scopus 로고    scopus 로고
    • High-throughput screening for inhibitors of the e3 ubiquitin ligase APC
    • Huang, J. et al. High-throughput screening for inhibitors of the e3 ubiquitin ligase APC. Methods in enzymology 399, 740-754, doi: 10.1016/S0076-6879(05)99049-6 (2005).
    • (2005) Methods in Enzymology , vol.399 , pp. 740-754
    • Huang, J.1
  • 8
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou, P. & Howley, P. M. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Molecular cell 2, 571-580 (1998).
    • (1998) Molecular Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2
  • 9
    • 2542579359 scopus 로고    scopus 로고
    • Getting into position: The catalytic mechanisms of protein ubiquitylation
    • Passmore, L. A. & Barford, D. Getting into position: the catalytic mechanisms of protein ubiquitylation. The Biochemical journal 379, 513-525, doi: 10.1042/BJ20040198 (2004).
    • (2004) The Biochemical Journal , vol.379 , pp. 513-525
    • Passmore, L.A.1    Barford, D.2
  • 10
    • 79955416634 scopus 로고    scopus 로고
    • The cullin protein family
    • Sarikas, A., Hartmann, T. & Pan, Z. Q. The cullin protein family. Genome biology 12, 220, doi: 10.1186/gb-2011-12-4-220 (2011).
    • (2011) Genome Biology , vol.12 , pp. 220
    • Sarikas, A.1    Hartmann, T.2    Pan, Z.Q.3
  • 11
    • 84875158737 scopus 로고    scopus 로고
    • The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: Disease-causing mutations in KLHL3 and WNK4 disrupt interaction
    • Ohta, A. et al. The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction. The Biochemical journal 451, 111-122, doi: 10.1042/BJ20121903 (2013).
    • (2013) The Biochemical Journal , vol.451 , pp. 111-122
    • Ohta, A.1
  • 12
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • Pintard, L., Willems, A. & Peter, M. Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family. The EMBO journal 23, 1681-1687, doi: 10.1038/sj.emboj.7600186 (2004).
    • (2004) The EMBO Journal , vol.23 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 13
    • 33646893705 scopus 로고    scopus 로고
    • A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor
    • Zhang, Q. et al. A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor. Developmental cell 10, 719-729, doi: 10.1016/j.devcel.2006.05.004 (2006).
    • (2006) Developmental Cell , vol.10 , pp. 719-729
    • Zhang, Q.1
  • 14
    • 33646875414 scopus 로고    scopus 로고
    • Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus
    • Kent, D., Bush, E. W. & Hooper, J. E. Roadkill attenuates Hedgehog responses through degradation of Cubitus interruptus. Development 133, 2001-2010, doi: 10.1242/dev.02370 (2006).
    • (2006) Development , vol.133 , pp. 2001-2010
    • Kent, D.1    Bush, E.W.2    Hooper, J.E.3
  • 15
    • 75849129292 scopus 로고    scopus 로고
    • Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase
    • Zhang, Q. et al. Multiple Ser/Thr-rich degrons mediate the degradation of Ci/Gli by the Cul3-HIB/SPOP E3 ubiquitin ligase. Proceedings of the National Academy of Sciences of the United States of America 106, 21191-21196, doi: 10.1073/pnas.0912008106 (2009).
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , pp. 21191-21196
    • Zhang, Q.1
  • 16
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M. et al. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134, 995-1006, doi: 10.1016/j.cell.2008.07.022 (2008).
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1
  • 17
    • 24944452270 scopus 로고    scopus 로고
    • The BTB protein MEL-26 promotes cytokinesis in C. Elegans by a CUL-3-independent mechanism
    • Luke-Glaser, S., Pintard, L., Lu, C., Mains, P. E. & Peter, M. The BTB protein MEL-26 promotes cytokinesis in C. elegans by a CUL-3-independent mechanism. Current biology: CB 15, 1605-1615, doi: 10.1016/j.cub.2005.07.068 (2005).
    • (2005) Current Biology: CB , vol.15 , pp. 1605-1615
    • Luke-Glaser, S.1    Pintard, L.2    Lu, C.3    Mains, P.E.4    Peter, M.5
  • 18
    • 84867398821 scopus 로고    scopus 로고
    • The size of the proteasomal substrate determines whether its degradation will be mediated by mono- or polyubiquitylation
    • Shabek, N. et al. The size of the proteasomal substrate determines whether its degradation will be mediated by mono- or polyubiquitylation. Molecular cell 48, 87-97, doi: 10.1016/j.molcel.2012.07.011 (2012).
    • (2012) Molecular Cell , vol.48 , pp. 87-97
    • Shabek, N.1
  • 19
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu, Y. & Komander, D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nature reviews. Molecular cell biology 13, 508-523, doi: 10.1038/nrm3394 (2012).
    • (2012) Nature Reviews. Molecular Cell Biology , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 20
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21 (1994).
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 21
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • Geetha, T., Jiang, J. & Wooten, M. W. Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Molecular cell 20, 301-312, doi: 10.1016/j.molcel.2005.09.014 (2005).
    • (2005) Molecular Cell , vol.20 , pp. 301-312
    • Geetha, T.1    Jiang, J.2    Wooten, M.W.3
  • 22
    • 23944471680 scopus 로고    scopus 로고
    • The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle
    • Hershko, A. The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle. Cell death and differentiation 12, 1191-1197, doi: 10.1038/sj.cdd.4401702 (2005).
    • (2005) Cell Death and Differentiation , vol.12 , pp. 1191-1197
    • Hershko, A.1
  • 23
    • 77949269474 scopus 로고    scopus 로고
    • Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent manner
    • Liao, B. & Jin, Y. Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent manner. Cell research 20, 332-344, doi: 10.1038/cr.2009.136 (2010).
    • (2010) Cell Research , vol.20 , pp. 332-344
    • Liao, B.1    Jin, Y.2
  • 24
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. & Ashwell, J. D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nature cell biology 8, 398-406, doi: 10.1038/ncb1384 (2006).
    • (2006) Nature Cell Biology , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 25
    • 84879551893 scopus 로고    scopus 로고
    • Ter94 ATPase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation
    • Zhang, Z. et al. Ter94 ATPase complex targets k11-linked ubiquitinated ci to proteasomes for partial degradation. Developmental cell 25, 636-644, doi: 10.1016/j.devcel.2013.05.006 (2013).
    • (2013) Developmental Cell , vol.25 , pp. 636-644
    • Zhang, Z.1
  • 26
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425, 316-321, doi: 10.1038/nature01985 (2003).
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1
  • 27
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa, M. & Xiong, Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Molecular and cellular biology 25, 162-171, doi: 10.1128/MCB.25.1.162-171.2005 (2005).
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 28
    • 84899941599 scopus 로고    scopus 로고
    • Hedgehog signaling downregulates suppressor of fused through the HIB/SPOP-Crn axis in Drosophila
    • Liu, C. et al. Hedgehog signaling downregulates suppressor of fused through the HIB/SPOP-Crn axis in Drosophila. Cell research 24, 595-609, doi: 10.1038/cr.2014.29 (2014).
    • (2014) Cell Research , vol.24 , pp. 595-609
    • Liu, C.1
  • 29
    • 70349769327 scopus 로고    scopus 로고
    • Structures of SPOP-substrate complexes: Insights into molecular architectures of BTB-Cul3 ubiquitin ligases
    • Zhuang, M. et al. Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Molecular cell 36, 39-50, doi: 10.1016/j.molcel.2009.09.022 (2009).
    • (2009) Molecular Cell , vol.36 , pp. 39-50
    • Zhuang, M.1
  • 30
    • 84863505152 scopus 로고    scopus 로고
    • Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase
    • Errington, W. J. et al. Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. Structure 20, 1141-1153, doi: 10.1016/j.str.2012.04.009 (2012).
    • (2012) Structure , vol.20 , pp. 1141-1153
    • Errington, W.J.1
  • 31
    • 17144450753 scopus 로고    scopus 로고
    • The N-terminal P O Z domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity
    • Espinas, M. L. et al. The N-terminal P O Z domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity. The Journal of biological chemistry 274, 16461-16469 (1999).
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 16461-16469
    • Espinas, M.L.1
  • 32
    • 0033081466 scopus 로고    scopus 로고
    • Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology
    • Katsani, K. R., Hajibagheri, M. A. & Verrijzer, C. P. Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology. The EMBO journal 18, 698-708, doi: 10.1093/emboj/18.3.698 (1999).
    • (1999) The EMBO Journal , vol.18 , pp. 698-708
    • Katsani, K.R.1    Hajibagheri, M.A.2    Verrijzer, C.P.3
  • 33
    • 68049083828 scopus 로고    scopus 로고
    • BTB protein, dKLHL18/CG3571, serves as an adaptor subunit for a dCul3 ubiquitin ligase complex
    • Fujiyama-Nakamura, S. et al. BTB protein, dKLHL18/CG3571, serves as an adaptor subunit for a dCul3 ubiquitin ligase complex. Genes to cells : devoted to molecular & cellular mechanisms 14, 965-973, doi: 10.1111/j.1365-2443.2009.01323.x (2009).
    • (2009) Genes to Cells : Devoted to Molecular & Cellular Mechanisms , vol.14 , pp. 965-973
    • Fujiyama-Nakamura, S.1
  • 34
    • 79551610653 scopus 로고    scopus 로고
    • Redox regulation by Keap1 and Nrf2 controls intestinal stem cell proliferation in Drosophila
    • Hochmuth, C. E., Biteau, B., Bohmann, D. & Jasper, H. Redox regulation by Keap1 and Nrf2 controls intestinal stem cell proliferation in Drosophila. Cell stem cell 8, 188-199, doi: 10.1016/j.stem.2010.12.006 (2011).
    • (2011) Cell Stem Cell , vol.8 , pp. 188-199
    • Hochmuth, C.E.1    Biteau, B.2    Bohmann, D.3    Jasper, H.4
  • 35
    • 84875445593 scopus 로고    scopus 로고
    • A Cul-3-BTB ubiquitylation pathway regulates junctional levels and asymmetry of core planar polarity proteins
    • Strutt, H., Searle, E., Thomas-Macarthur, V., Brookfield, R. & Strutt, D. A Cul-3-BTB ubiquitylation pathway regulates junctional levels and asymmetry of core planar polarity proteins. Development 140, 1693-1702, doi: 10.1242/dev.089656 (2013).
    • (2013) Development , vol.140 , pp. 1693-1702
    • Strutt, H.1    Searle, E.2    Thomas-Macarthur, V.3    Brookfield, R.4    Strutt, D.5
  • 36
    • 37749024370 scopus 로고    scopus 로고
    • Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in Drosophila
    • Sykiotis, G. P. & Bohmann, D. Keap1/Nrf2 signaling regulates oxidative stress tolerance and lifespan in Drosophila. Developmental cell 14, 76-85, doi: 10.1016/j.devcel.2007.12.002 (2008).
    • (2008) Developmental Cell , vol.14 , pp. 76-85
    • Sykiotis, G.P.1    Bohmann, D.2
  • 37
    • 84872137966 scopus 로고    scopus 로고
    • Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage
    • Bae, S. H. et al. Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage. Cell metabolism 17, 73-84, doi: 10.1016/j.cmet.2012.12.002 (2013).
    • (2013) Cell Metabolism , vol.17 , pp. 73-84
    • Bae, S.H.1
  • 39
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang, D. D. et al. Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. The Journal of biological chemistry 280, 30091-30099, doi: 10.1074/jbc.M501279200 (2005).
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 30091-30099
    • Zhang, D.D.1
  • 40
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C. & Andre, B. K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. The Journal of cell biology 185, 493-502, doi: 10.1083/jcb.200810114 (2009).
    • (2009) The Journal of Cell Biology , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    Andre, B.3
  • 41
    • 79955978424 scopus 로고    scopus 로고
    • K63-linked ubiquitination and neurodegeneration
    • Lim, K. L. & Lim, G. G. K63-linked ubiquitination and neurodegeneration. Neurobiology of disease 43, 9-16, doi: 10.1016/j. nbd.2010.08.001 (2011).
    • (2011) Neurobiology of Disease , vol.43 , pp. 9-16
    • Lim, K.L.1    Lim, G.G.2
  • 42
    • 38049014824 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination: A signal for targeting misfolded proteins to the aggresome-autophagy pathway
    • Olzmann, J. A. & Chin, L. S. Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway. Autophagy 4, 85-87 (2008).
    • (2008) Autophagy , vol.4 , pp. 85-87
    • Olzmann, J.A.1    Chin, L.S.2
  • 44
    • 1642442587 scopus 로고    scopus 로고
    • Stability of homologue of Slimb F-box protein is regulated by availability of its substrate
    • Li, Y., Gazdoiu, S., Pan, Z. Q. & Fuchs, S. Y. Stability of homologue of Slimb F-box protein is regulated by availability of its substrate. The Journal of biological chemistry 279, 11074-11080, doi: 10.1074/jbc.M312301200 (2004).
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 11074-11080
    • Li, Y.1    Gazdoiu, S.2    Pan, Z.Q.3    Fuchs, S.Y.4
  • 45
    • 11144244006 scopus 로고    scopus 로고
    • Crystal structure of the Kelch domain of human Keap1
    • Li, X., Zhang, D., Hannink, M. & Beamer, L. J. Crystal structure of the Kelch domain of human Keap1. The Journal of biological chemistry 279, 54750-54758, doi: 10.1074/jbc.M410073200 (2004).
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 54750-54758
    • Li, X.1    Zhang, D.2    Hannink, M.3    Beamer, L.J.4
  • 46
    • 84863393216 scopus 로고    scopus 로고
    • Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges
    • Christie, J. M. et al. Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges. Science 335, 1492-1496, doi: 10.1126/science.1218091 (2012).
    • (2012) Science , vol.335 , pp. 1492-1496
    • Christie, J.M.1
  • 47
    • 21144446865 scopus 로고    scopus 로고
    • Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
    • Hernandez-Munoz, I. et al. Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase. Proceedings of the National Academy of Sciences of the United States of America 102, 7635-7640, doi: 10.1073/pnas.0408918102 (2005).
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , pp. 7635-7640
    • Hernandez-Munoz, I.1
  • 48
    • 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. et al. BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase. The Journal of biological chemistry 281, 12664-12672, doi: 10.1074/jbc.M600204200 (2006).
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 12664-12672
    • Kwon, J.E.1
  • 49
    • 84855889543 scopus 로고    scopus 로고
    • Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex
    • Kim, B. et al. Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the Cul3-SPOP E3 ubiquitin ligase complex. Biochemical and biophysical research communications 415, 720-726, doi: 10.1016/j.bbrc.2011.10.154 (2011).
    • (2011) Biochemical and Biophysical Research Communications , vol.415 , pp. 720-726
    • Kim, B.1
  • 50
    • 84866730732 scopus 로고    scopus 로고
    • Insight in glioma susceptibility through an analysis of 6p22.3, 12p13.33-12.1, 17q22-23.2 and 18q23 SNP genotypes in familial and non-familial glioma
    • Liu, Y. et al. Insight in glioma susceptibility through an analysis of 6p22.3, 12p13.33-12.1, 17q22-23.2 and 18q23 SNP genotypes in familial and non-familial glioma. Human genetics 131, 1507-1517, doi: 10.1007/s00439-012-1187-x (2012).
    • (2012) Human Genetics , vol.131 , pp. 1507-1517
    • Liu, Y.1
  • 51
    • 84861581164 scopus 로고    scopus 로고
    • Exome sequencing identifies recurrent SPOP, FOXA1 and MED12 mutations in prostate cancer
    • Barbieri, C. E. et al. Exome sequencing identifies recurrent SPOP, FOXA1 and MED12 mutations in prostate cancer. Nature genetics 44, 685-689, doi: 10.1038/ng.2279 (2012).
    • (2012) Nature Genetics , vol.44 , pp. 685-689
    • Barbieri, C.E.1
  • 52
    • 84870532434 scopus 로고    scopus 로고
    • Exome sequencing of serous endometrial tumors identifies recurrent somatic mutations in chromatinremodeling and ubiquitin ligase complex genes
    • Le Gallo, M. et al. Exome sequencing of serous endometrial tumors identifies recurrent somatic mutations in chromatinremodeling and ubiquitin ligase complex genes. Nature genetics 44, 1310-1315, doi: 10.1038/ng.2455 (2012).
    • (2012) Nature Genetics , vol.44 , pp. 1310-1315
    • Le Gallo, M.1
  • 53
    • 43749117536 scopus 로고    scopus 로고
    • Coordinated activation of the nuclear ubiquitin ligase Cul3-SPOP by the generation of phosphatidylinositol 5-phosphate
    • Bunce, M. W., Boronenkov, I. V. & Anderson, R. A. Coordinated activation of the nuclear ubiquitin ligase Cul3-SPOP by the generation of phosphatidylinositol 5-phosphate. The Journal of biological chemistry 283, 8678-8686, doi: 10.1074/jbc.M710222200 (2008).
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 8678-8686
    • Bunce, M.W.1    Boronenkov, I.V.2    Anderson, R.A.3
  • 54
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin, G. M. & Spradling, A. C. Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353 (1982).
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 55
    • 0031716573 scopus 로고    scopus 로고
    • Use of FLP/FRT system to study Drosophila development
    • Theodosiou, N. A. & Xu, T. Use of FLP/FRT system to study Drosophila development. Methods 14, 355-365, doi: 10.1006/ meth.1998.0591 (1998).
    • (1998) Methods , vol.14 , pp. 355-365
    • Theodosiou, N.A.1    Xu, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.