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Volumn 27, Issue 12, 2013, Pages 4799-4810

VBP1 facilitates proteasome and autophagy-mediated degradation of MutS homologue hMSH4

Author keywords

DSB repair; P97; Ubiquitination; VHL

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEASOME; PROTEIN HMSH 4; PROTEIN MUTS; PROTEIN P97; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN; VON HIPPEL LINDAU PROTEIN 1;

EID: 84886896007     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.13-235127     Document Type: Article
Times cited : (20)

References (65)
  • 1
    • 75549087699 scopus 로고    scopus 로고
    • Genetics of mammalian meiosis: Regulation, dynamics and impact on fertility
    • Handel, M. A., and Schimenti, J. C. (2010) Genetics of mammalian meiosis: regulation, dynamics and impact on fertility. Nat. Rev. Genet. 11, 124-136
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 124-136
    • Handel, M.A.1    Schimenti, J.C.2
  • 2
    • 0028560427 scopus 로고
    • Mutation of a meiosis-specific muts homolog decreases crossing over but not mismatch correction
    • Ross-Macdonald, P., and Roeder, G. S. (1994) Mutation of a meiosis-specific MutS homolog decreases crossing over but not mismatch correction. Cell 79, 1069-1080
    • (1994) Cell , vol.79 , pp. 1069-1080
    • Ross-Macdonald, P.1    Roeder, G.S.2
  • 3
    • 0032755748 scopus 로고    scopus 로고
    • Crossing over during caenorhabditis elegans meiosis requires a conserved muts-based pathway that is partially dispensable in budding yeast
    • Zalevsky, J., MacQueen, A. J., Duffy, J. B., Kemphues, K. J., and Villeneuve, A. M. (1999) Crossing over during Caenorhabditis elegans meiosis requires a conserved MutS-based pathway that is partially dispensable in budding yeast. Genetics 153, 1271-1283
    • (1999) Genetics , vol.153 , pp. 1271-1283
    • Zalevsky, J.1    MacQueen, A.J.2    Duffy, J.B.3    Kemphues, K.J.4    Villeneuve, A.M.5
  • 5
    • 11144325648 scopus 로고    scopus 로고
    • Extreme heterogeneity in the molecular events leading to the establishment of chiasmata during meiosis iin human oocytes
    • Lenzi, M. L., Smith, J., Snowden, T., Kim, M., Fishel, R., Poulos, B. K., and Cohen, P. E. (2005) Extreme heterogeneity in the molecular events leading to the establishment of chiasmata during meiosis Iin human oocytes. Am. J. Hum. Genet. 76, 112-127
    • (2005) Am. J. Hum. Genet. , vol.76 , pp. 112-127
    • Lenzi, M.L.1    Smith, J.2    Snowden, T.3    Kim, M.4    Fishel, R.5    Poulos, B.K.6    Cohen, P.E.7
  • 7
    • 34249825237 scopus 로고    scopus 로고
    • Muts homologues hmsh4 and hmsh5: Diverse functional implications in humans
    • Her, C., Zhao, N., Wu, X., and Tompkins, J. D. (2007) MutS homologues hMSH4 and hMSH5: diverse functional implications in humans. Front. Biosci. 12, 905-911
    • (2007) Front. Biosci. , vol.12 , pp. 905-911
    • Her, C.1    Zhao, N.2    Wu, X.3    Tompkins, J.D.4
  • 8
    • 0030831360 scopus 로고    scopus 로고
    • Conserved properties between functionally distinct muts homologs in yeast
    • Pochart, P., Woltering, D., and Hollingsworth, N. M. (1997) Conserved properties between functionally distinct MutS homologs in yeast. J. Biol. Chem. 272, 30345-30349
    • (1997) J. Biol. Chem. , vol.272 , pp. 30345-30349
    • Pochart, P.1    Woltering, D.2    Hollingsworth, N.M.3
  • 9
    • 38049120174 scopus 로고    scopus 로고
    • Hmsh4-hmsh5 adenosine nucleotide processing and interactions with homologous recombination machinery
    • Snowden, T., Shim, K. S., Schmutte, C., Acharya, S., and Fishel, R. (2008) hMSH4-hMSH5 adenosine nucleotide processing and interactions with homologous recombination machinery. J. Biol. Chem. 283, 145-154
    • (2008) J. Biol. Chem. , vol.283 , pp. 145-154
    • Snowden, T.1    Shim, K.S.2    Schmutte, C.3    Acharya, S.4    Fishel, R.5
  • 10
    • 0032191204 scopus 로고    scopus 로고
    • Cloning and characterization of the human and caenorhabditis elegans homologs of the saccharomyces cerevisiae msh5 gene
    • Winand, N. J., Panzer, J. A., and Kolodner, R. D. (1998) Cloning and characterization of the human and Caenorhabditis elegans homologs of the Saccharomyces cerevisiae MSH5 gene. Genomics 53, 69-80
    • (1998) Genomics , vol.53 , pp. 69-80
    • Winand, N.J.1    Panzer, J.A.2    Kolodner, R.D.3
  • 11
    • 4143086035 scopus 로고    scopus 로고
    • Hmsh4-hmsh5 recognizes holliday junctions and forms a meiosis-specific sliding clamp that embraces homologous chromosomes
    • Snowden, T., Acharya, S., Butz, C., Berardini, M., and Fishel, R. (2004) hMSH4-hMSH5 recognizes Holliday junctions and forms a meiosis-specific sliding clamp that embraces homologous chromosomes. Mol. Cell 15, 437-451
    • (2004) Mol. Cell , vol.15 , pp. 437-451
    • Snowden, T.1    Acharya, S.2    Butz, C.3    Berardini, M.4    Fishel, R.5
  • 12
    • 84878357168 scopus 로고    scopus 로고
    • Muts homologue hmsh4: Interaction with eif3f and a role in nhej-mediated dsb repair
    • Chu, Y. L., Wu, X., Xu, Y., and Her, C. (2013) MutS homologue hMSH4: interaction with eIF3f and a role in NHEJ-mediated DSB repair. Mol. Cancer 12, 51
    • (2013) Mol. Cancer , vol.12 , pp. 51
    • Chu, Y.L.1    Wu, X.2    Xu, Y.3    Her, C.4
  • 15
    • 0037098952 scopus 로고    scopus 로고
    • The dna mismatch-repair mlh3 protein interacts with msh4 in meiotic cells, supporting a role for this mutl homolog in mammalian meiotic recombination
    • Santucci-Darmanin, S., Neyton, S., Lespinasse, F., Saunieres, A., Gaudray, P., and Paquis-Flucklinger, V. (2002) The DNA mismatch-repair MLH3 protein interacts with MSH4 in meiotic cells, supporting a role for this MutL homolog in mammalian meiotic recombination. Hum. Mol. Genet. 11, 1697-1706
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1697-1706
    • Santucci-Darmanin, S.1    Neyton, S.2    Lespinasse, F.3    Saunieres, A.4    Gaudray, P.5    Paquis-Flucklinger, V.6
  • 16
    • 0037442714 scopus 로고    scopus 로고
    • Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1
    • Her, C., Wu, X., Griswold, M. D., and Zhou, F. (2003) Human MutS homologue MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1. Cancer Res. 63, 865-872
    • (2003) Cancer Res. , vol.63 , pp. 865-872
    • Her, C.1    Wu, X.2    Griswold, M.D.3    Zhou, F.4
  • 17
    • 0032529081 scopus 로고    scopus 로고
    • Cloning, structural characterization, and chromosomal localization of the human orthologue of saccharomyces cerevisiae msh5 gene
    • Her, C., and Doggett, N. A. (1998) Cloning, structural characterization, and chromosomal localization of the human orthologue of Saccharomyces cerevisiae MSH5 gene. Genomics 52, 50-61
    • (1998) Genomics , vol.52 , pp. 50-61
    • Her, C.1    Doggett, N.A.2
  • 19
    • 0029941650 scopus 로고    scopus 로고
    • Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product
    • Tsuchiya, H., Iseda, T., and Hino, O. (1996) Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product. Cancer Res. 56, 2881-2885
    • (1996) Cancer Res. , vol.56 , pp. 2881-2885
    • Tsuchiya, H.1    Iseda, T.2    Hino, O.3
  • 20
    • 0031259797 scopus 로고    scopus 로고
    • Characterization of the gene (VBP1) and transcript for the von Hippel-Lindau binding protein and isolation of the highly conserved murine homologue
    • Brinke, A., Green, P. M., and Giannelli, F. (1997) Characterization of the gene (VBP1) and transcript for the von Hippel-Lindau binding protein and isolation of the highly conserved murine homologue. Genomics 45, 105-112
    • (1997) Genomics , vol.45 , pp. 105-112
    • Brinke, A.1    Green, P.M.2    Giannelli, F.3
  • 22
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in vhl disrupt folding in vivo by interfering with chaperonin binding
    • Feldman, D. E., Spiess, C., Howard, D. E., and Frydman, J. (2003) Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Mol. Cell 12, 1213-1224
    • (2003) Mol. Cell , vol.12 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3    Frydman, J.4
  • 23
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the vhl-elongin bc tumor suppressor complex is mediated by the chaperonin tric
    • Feldman, D. E., Thulasiraman, V., Ferreyra, R. G., and Frydman, J. (1999) Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol. Cell 4, 1051-1061
    • (1999) Mol. Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 24
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the vhl tumor suppressor proceed through distinct chaperone pathways
    • McClellan, A. J., Scott, M. D., and Frydman, J. (2005) Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121, 739-748
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 25
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 26
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha-And gammatubulin
    • Geissler, S., Siegers, K., and Schiebel, E. (1998) A novel protein complex promoting formation of functional alpha-And gammatubulin. EMBO J. 17, 952-966
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 27
    • 0037223823 scopus 로고    scopus 로고
    • Regulation of microtubule stability by the von hippel-lindau tumour suppressor protein pvhl
    • Hergovich, A., Lisztwan, J., Barry, R., Ballschmieter, P., and Krek, W. (2003) Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL. Nat. Cell Biol. 5, 64-70
    • (2003) Nat. Cell Biol. , vol.5 , pp. 64-70
    • Hergovich, A.1    Lisztwan, J.2    Barry, R.3    Ballschmieter, P.4    Krek, W.5
  • 28
    • 54549113030 scopus 로고    scopus 로고
    • The von hippel-lindau tumour suppressor protein: O2 sensing and cancer
    • Kaelin, W. G., Jr. (2008) The von Hippel-Lindau tumour suppressor protein: O2 sensing and cancer. Nat. Rev. Cancer 8, 865-873
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 865-873
    • Kaelin Jr., W.G.1
  • 31
    • 52649138958 scopus 로고    scopus 로고
    • Ubxd7 binds multiple ubiquitin ligases and implicates p97 in hif1alpha turnover
    • Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R., and Deshaies, R. J. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134, 804-816
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 33
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): A "molecular gearbox" in the ubiquitin pathway?
    • Jentsch, S., and Rumpf, S. (2007) Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem. Sci. 32, 6-11
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 34
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an aaa atpase
    • Ye, Y. (2006) Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol. 156, 29-40
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 35
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the vcp/p97 aaa-Atpase in the ubiquitin system
    • Meyer, H., Bug, M., and Bremer, S. (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 36
  • 37
    • 80053606383 scopus 로고    scopus 로고
    • Cdc-48/p97 coordinates cdt-1 degradation with gins chromatin dissociation to ensure faithful dna replication
    • Franz, A., Orth, M., Pirson, P. A., Sonneville, R., Blow, J. J., Gartner, A., Stemmann, O., and Hoppe, T. (2011) CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication. Mol. Cell 44, 85-96
    • (2011) Mol. Cell , vol.44 , pp. 85-96
    • Franz, A.1    Orth, M.2    Pirson, P.A.3    Sonneville, R.4    Blow, J.J.5    Gartner, A.6    Stemmann, O.7    Hoppe, T.8
  • 39
    • 80053583606 scopus 로고    scopus 로고
    • A genome-wide screen identifies p97 as an essential regulator of dna damage-dependent cdt1 destruction
    • Raman, M., Havens, C. G., Walter, J. C., and Harper, J. W. (2011) A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction. Mol. Cell 44, 72-84
    • (2011) Mol. Cell , vol.44 , pp. 72-84
    • Raman, M.1    Havens, C.G.2    Walter, J.C.3    Harper, J.W.4
  • 40
    • 29244488526 scopus 로고    scopus 로고
    • Formation of hmsh4-hmsh5 heterocomplex is a prerequisite for subsequent gps2 recruitment
    • Lee, T. H., Yi, W., Griswold, M. D., Zhu, F., and Her, C. (2006) Formation of hMSH4-hMSH5 heterocomplex is a prerequisite for subsequent GPS2 recruitment. DNA Repair (Amst.) 5, 32-42
    • (2006) DNA Repair (Amst. , vol.5 , pp. 32-42
    • Lee, T.H.1    Yi, W.2    Griswold, M.D.3    Zhu, F.4    Her, C.5
  • 41
    • 19444381510 scopus 로고    scopus 로고
    • Two variants of muts homolog hmsh5: Prevalence in humans and effects on protein interaction
    • Yi, W., Wu, X., Lee, T. H., Doggett, N. A., and Her, C. (2005) Two variants of MutS homolog hMSH5: prevalence in humans and effects on protein interaction. Biochem. Biophys. Res. Commun. 332, 524-532
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 524-532
    • Yi, W.1    Wu, X.2    Lee, T.H.3    Doggett, N.A.4    Her, C.5
  • 42
    • 19444379003 scopus 로고    scopus 로고
    • Hmre11 deficiency leads to microsatellite instability and defective dna mismatch repair
    • Vo, A. T., Zhu, F., Wu, X., Yuan, F., Gao, Y., Gu, L., Li, G. M., Lee, T. H., and Her, C. (2005) hMRE11 deficiency leads to microsatellite instability and defective DNA mismatch repair. EMBO Rep. 6, 438-444
    • (2005) EMBO Rep. , vol.6 , pp. 438-444
    • Vo, A.T.1    Zhu, F.2    Wu, X.3    Yuan, F.4    Gao, Y.5    Gu, L.6    Li, G.M.7    Lee, T.H.8    Her, C.9
  • 43
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the aaa atpases nsf and p97 in the secretory pathway
    • Dalal, S., Rosser, M. F., Cyr, D. M., and Hanson, P. I. (2004) Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol. Biol. Cell 15, 637-648
    • (2004) Mol. Biol. Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 44
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-ufd1-npl4 complex in retrotranslocation from the er to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71-84
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 46
    • 79955978424 scopus 로고    scopus 로고
    • K63-linked ubiquitination and neurodegeneration
    • Lim, K. L., and Lim, G. G. (2011) K63-linked ubiquitination and neurodegeneration. Neurobiol. Dis. 43, 9-16
    • (2011) Neurobiol. Dis. , vol.43 , pp. 9-16
    • Lim, K.L.1    Lim, G.G.2
  • 47
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26s proteasome
    • Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh-e, A., and Tanaka, K. (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 28, 359-371
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-e, A.6    Tanaka, K.7
  • 48
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima, N., Yoshimori, T., and Levine, B. (2010) Methods in mammalian autophagy research. Cell 140, 313-326
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 50
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I., and Dikic, I. (2009) A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 52
    • 84861532088 scopus 로고    scopus 로고
    • Killing a cancer: What are the alternatives?
    • Kreuzaler, P., and Watson, C. J. (2012) Killing a cancer: what are the alternatives? Nat. Rev. Cancer 12, 411-424
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 411-424
    • Kreuzaler, P.1    Watson, C.J.2
  • 53
    • 79957614921 scopus 로고    scopus 로고
    • Prefoldin subunits are protected from ubiquitin-proteasome system-mediated degradation by forming complex with other constituent subunits
    • Miyazawa, M., Tashiro, E., Kitaura, H., Maita, H., Suto, H., Iguchi-Ariga, S. M., and Ariga, H. (2011) Prefoldin subunits are protected from ubiquitin-proteasome system-mediated degradation by forming complex with other constituent subunits. J. Biol. Chem. 286, 19191-19203
    • (2011) J. Biol. Chem. , vol.286 , pp. 19191-19203
    • Miyazawa, M.1    Tashiro, E.2    Kitaura, H.3    Maita, H.4    Suto, H.5    Iguchi-Ariga, S.M.6    Ariga, H.7
  • 54
    • 79955642715 scopus 로고    scopus 로고
    • The cullin-ring ubiquitinprotein ligases
    • Hua, Z., and Vierstra, R. D. (2011) The cullin-RING ubiquitinprotein ligases. Annu. Rev. Plant Biol. 62, 299-334
    • (2011) Annu. Rev. Plant Biol. , vol.62 , pp. 299-334
    • Hua, Z.1    Vierstra, R.D.2
  • 55
    • 44949242505 scopus 로고    scopus 로고
    • Regulation of cullin ring ligases
    • Hotton, S. K., and Callis, J. (2008) Regulation of cullin RING ligases. Annu. Rev. Plant Biol. 59, 467-489
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 467-489
    • Hotton, S.K.1    Callis, J.2
  • 56
    • 10644276385 scopus 로고    scopus 로고
    • Vhl-box and socs-box domains determine binding specificity for cul2-rbx1 and cul5-rbx2 modules of ubiquitin ligases
    • Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., and Nakayama, K. I. (2004) VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18, 3055-3065
    • (2004) Genes Dev. , vol.18 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 57
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects cdc48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 59
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., and Rape, M. (2009) Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 10, 755-764
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 60
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • Jin, L., Williamson, A., Banerjee, S., Philipp, I., and Rape, M. (2008) Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133, 653-665
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 61
    • 77952533111 scopus 로고    scopus 로고
    • Vcp/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause ibmpfd
    • Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T. P., Dantuma, N. P., and Taylor, J. P. (2010) VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6, 217-227
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 63
    • 41949134141 scopus 로고    scopus 로고
    • Ubiquitin recognition by the ubiquitin-Associated domain of p62 involves a novel conformational switch
    • Long, J., Gallagher, T. R., Cavey, J. R., Sheppard, P. W., Ralston, S. H., Layfield, R., and Searle, M. S. (2008) Ubiquitin recognition by the ubiquitin-Associated domain of p62 involves a novel conformational switch. J. Biol. Chem. 283, 5427-5440
    • (2008) J. Biol. Chem. , vol.283 , pp. 5427-5440
    • Long, J.1    Gallagher, T.R.2    Cavey, J.R.3    Sheppard, P.W.4    Ralston, S.H.5    Layfield, R.6    Searle, M.S.7
  • 65
    • 77649131406 scopus 로고    scopus 로고
    • Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis
    • Moynahan, M. E., and Jasin, M. (2010) Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis. Nat. Rev. Mol. Cell Biol. 11, 196-207
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 196-207
    • Moynahan, M.E.1    Jasin, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.