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Volumn 286, Issue , 2004, Pages 149-185

Signaling through monoubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

CBL PROTEIN; GROWTH FACTOR; HISTONE; I KAPPA B KINASE; PROTEIN TYROSINE KINASE; UBIQUITIN;

EID: 3242685293     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-540-69494-6_6     Document Type: Review
Times cited : (139)

References (163)
  • 1
    • 0037135528 scopus 로고    scopus 로고
    • Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor
    • Ahn, S. et al. Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor. J Biol Chem 277, 26642-51 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 26642-26651
    • Ahn, S.1
  • 2
    • 12044256844 scopus 로고
    • Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene
    • Andoniou, C. E., Thien, C. B., Langdon, W. Y. Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene. Embo J 13, 4515-23 (1994)
    • (1994) Embo J , vol.13 , pp. 4515-4523
    • Andoniou, C.E.1    Thien, C.B.2    Langdon, W.Y.3
  • 3
    • 0033984433 scopus 로고    scopus 로고
    • The Cbl proto-oncogene product negatively regulates the Src-family tyrosine kinase Fyn by enhancing its degradation
    • Andoniou, C. E. et al. The Cbl proto-oncogene product negatively regulates the Src-family tyrosine kinase Fyn by enhancing its degradation. Mol Cell Biol 20, 851-67 (2000)
    • (2000) Mol Cell Biol , vol.20 , pp. 851-867
    • Andoniou, C.E.1
  • 4
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst, M., Katzmann, D. J., Estepa-Sabal, E. J., Meerloo, T., Emr, S. D. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 3, 271-82 (2002)
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 5
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B., Emr, S. D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 3, 283-9 (2002)
    • (2002) Dev Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 6
    • 0037397484 scopus 로고    scopus 로고
    • Orchestrating nuclear functions: Ubiquitin sets the rhythm
    • Bach, I., Ostendorff, H. P. Orchestrating nuclear functions: ubiquitin sets the rhythm. Trends Biochem Sci 28, 189-95 (2003)
    • (2003) Trends Biochem Sci , vol.28 , pp. 189-195
    • Bach, I.1    Ostendorff, H.P.2
  • 7
    • 0038323973 scopus 로고    scopus 로고
    • STAM Hrs are subunits of a multivalent Ubiquitin-binding complex on early endosomes
    • Bache, K. G., Raiborg, C., Mehlum, A., Stenmark, H. STAM and Hrs are subunits of a multivalent Ubiquitin-binding complex on early endosomes. J Biol Chem (2003)
    • (2003) J Biol Chem
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 8
    • 0024299523 scopus 로고
    • Reconstitution of SEC gene product-dependent intercompartmental protein transport
    • Baker, D., Hicke, L., Rexach, M., Schleyer, M., Schekman, R. Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell 54, 335-44 (1988)
    • (1988) Cell , vol.54 , pp. 335-344
    • Baker, D.1    Hicke, L.2    Rexach, M.3    Schleyer, M.4    Schekman, R.5
  • 9
    • 0034735517 scopus 로고    scopus 로고
    • Epidermal growth factor and membrane trafficking. EGF receptor activation of endocytosis requires Rab5a
    • Barbieri, M. A. et al. Epidermal growth factor and membrane trafficking. EGF receptor activation of endocytosis requires Rab5a. J Cell Biol 151, 539-50 (2000)
    • (2000) J Cell Biol , vol.151 , pp. 539-550
    • Barbieri, M.A.1
  • 10
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p Hselp complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C., Piper, R. C. The Vps27p Hselp complex binds ubiquitin and mediates endosomal protein sorting. Nat Cell Biol 4, 534-9 (2002)
    • (2002) Nat Cell Biol , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 11
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • Bishop, N., Horman, A., Woodman, P. Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J Cell Biol 157, 91-101 (2002)
    • (2002) J Cell Biol , vol.157 , pp. 91-101
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 12
    • 0036278105 scopus 로고    scopus 로고
    • Accessory protein recruitment motifs in clathrin-mediated endocytosis
    • Brett, T. J., Traub, L. M., Fremont, D. H. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure (Camb) 10, 797-809 (2002)
    • (2002) Structure (Camb) , vol.10 , pp. 797-809
    • Brett, T.J.1    Traub, L.M.2    Fremont, D.H.3
  • 13
    • 0036682364 scopus 로고    scopus 로고
    • Gene silencing: Trans-histone regulatory pathway in chromatin
    • Briggs, S. D. et al. Gene silencing: trans-histone regulatory pathway in chromatin. Nature 418, 498 (2002)
    • (2002) Nature , vol.418 , pp. 498
    • Briggs, S.D.1
  • 14
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • Buchberger, A. From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol 12, 216-21 (2002)
    • (2002) Trends Cell Biol , vol.12 , pp. 216-221
    • Buchberger, A.1
  • 15
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett, B., Li, F., Pittman, R. N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum Mol Genet (2003)
    • (2003) Hum Mol Genet
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 16
    • 0035816547 scopus 로고    scopus 로고
    • Persistent activation of NF-kappa B by the tax transforming protein involves chronic phosphorylation of IkappaB kinase subunits IKKbeta and IKKgamma
    • Carter, R. S., Geyer, B. C., Xie, M., Acevedo-Suarez, C. A., Ballard, D. W. Persistent activation of NF-kappa B by the tax transforming protein involves chronic phosphorylation of IkappaB kinase subunits IKKbeta and IKKgamma. J Biol Chem 276, 24445-8 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 24445-24448
    • Carter, R.S.1    Geyer, B.C.2    Xie, M.3    Acevedo-Suarez, C.A.4    Ballard, D.W.5
  • 18
    • 0032552056 scopus 로고    scopus 로고
    • Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
    • Chen, H. et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 394, 793-7 (1998)
    • (1998) Nature , vol.394 , pp. 793-797
    • Chen, H.1
  • 19
    • 0141465416 scopus 로고    scopus 로고
    • Interaction between two E3 ubiquitin ligases of different classes, CBLC and AIP4/ITCH
    • Courbard, J. R. et al. Interaction between two E3 ubiquitin ligases of different classes, CBLC and AIP4/ITCH. J Biol Chem 10, 10 (2002)
    • (2002) J Biol Chem , vol.10 , pp. 10
    • Courbard, J.R.1
  • 20
    • 0042161939 scopus 로고    scopus 로고
    • The Fanconi road to cancer
    • D'Andrea, A. D. The Fanconi road to cancer. Genes Dev 17, 1933-6 (2003)
    • (2003) Genes Dev , vol.17 , pp. 1933-1936
    • D'Andrea, A.D.1
  • 21
    • 0037268338 scopus 로고    scopus 로고
    • The Fanconi anaemia/BRCA pathway
    • D'Andrea, A. D., Grompe, M. The Fanconi anaemia/BRCA pathway. Nat Rev Cancer 3, 23-34 (2003)
    • (2003) Nat Rev Cancer , vol.3 , pp. 23-34
    • D'Andrea, A.D.1    Grompe, M.2
  • 22
    • 18244392958 scopus 로고    scopus 로고
    • Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression
    • Debonneville, C. et al. Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression. Embo J 20, 7052-9 (2001)
    • (2001) Embo J , vol.20 , pp. 7052-7059
    • Debonneville, C.1
  • 23
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation
    • Delhase, M., Hayakawa, M., Chen, Y., Karin, M. Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science 284, 309-13 (1999)
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 24
    • 0034949705 scopus 로고    scopus 로고
    • c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • de Melker, A. A., van der Horst, G., Calafat, J., Jansen, H., Borst, J. c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route. J Cell Sci 114, 2167-78. (2001)
    • (2001) J Cell Sci , vol.114 , pp. 2167-2178
    • De Melker, A.A.1    Van Der Horst, G.2    Calafat, J.3    Jansen, H.4    Borst, J.5
  • 25
    • 17344363009 scopus 로고    scopus 로고
    • The Fanconi anaemia group G gene FANCG is identical with XRCC9
    • de Winter, J. P. et al. The Fanconi anaemia group G gene FANCG is identical with XRCC9. Nat Genet 20, 281-3 (1998)
    • (1998) Nat Genet , vol.20 , pp. 281-283
    • De Winter, J.P.1
  • 26
    • 0033759693 scopus 로고    scopus 로고
    • Isolation of a cDNA representing the Fanconi anemia complementation group E gene
    • de Winter, J. P. et al. Isolation of a cDNA representing the Fanconi anemia complementation group E gene. Am J Hum Genet 67, 1306-8 (2000)
    • (2000) Am J Hum Genet , vol.67 , pp. 1306-1308
    • De Winter, J.P.1
  • 27
    • 0034326299 scopus 로고    scopus 로고
    • The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG
    • de Winter, J. P. et al. The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG. Hum Mol Genet 9, 2665-74 (2000)
    • (2000) Hum Mol Genet , vol.9 , pp. 2665-2674
    • De Winter, J.P.1
  • 28
    • 0031730342 scopus 로고    scopus 로고
    • Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr
    • Dieckmann, T. et al. Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Nat Struct Biol 5, 1042-7 (1998)
    • (1998) Nat Struct Biol , vol.5 , pp. 1042-1047
    • Dieckmann, T.1
  • 29
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • Di Fiore, P. P., Polo, S., Hofmann, K. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat Rev Mol Cell Biol 4, 491-7 (2003)
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 30
    • 0037010186 scopus 로고    scopus 로고
    • CIN85/CMS family of adaptor molecules
    • Dikic, I. CIN85/CMS family of adaptor molecules. FEBS Lett 529, 110-5 (2002)
    • (2002) FEBS Lett , vol.529 , pp. 110-115
    • Dikic, I.1
  • 31
    • 0141637441 scopus 로고    scopus 로고
    • Cbl signaling networks in the regulation of cell function
    • Dikic, I., Szymkiewicz, I., Soubeyran, P. Cbl signaling networks in the regulation of cell function. Cell Mol Life Sci 60, 1805-27 (2003)
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1805-1827
    • Dikic, I.1    Szymkiewicz, I.2    Soubeyran, P.3
  • 32
    • 0042808497 scopus 로고    scopus 로고
    • Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates
    • Donaldson, K. M. et al. Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates. Proc Natl Acad Sci U S A 100, 8892-7 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8892-8897
    • Donaldson, K.M.1
  • 33
    • 0037316409 scopus 로고    scopus 로고
    • Ubiquitin signals protein trafficking via interaction with a novel ubiquitin binding domain in the membrane fusion regulator, Vps9p
    • Donaldson, K. M., Yin, H., Gekakis, N., Supek, F., Joazeiro, C. A. Ubiquitin Signals Protein Trafficking via Interaction with a Novel Ubiquitin Binding Domain in the Membrane Fusion Regulator, Vps9p. Curr Biol 13, 258-62 (2003)
    • (2003) Curr Biol , vol.13 , pp. 258-262
    • Donaldson, K.M.1    Yin, H.2    Gekakis, N.3    Supek, F.4    Joazeiro, C.A.5
  • 34
    • 0037047323 scopus 로고    scopus 로고
    • Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6
    • Dover, J. et al. Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6. J Biol Chem 277, 28368-71 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 28368-28371
    • Dover, J.1
  • 35
    • 0034010261 scopus 로고    scopus 로고
    • Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites
    • Drake, M. T., Downs, M. A., Traub, L. M. Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites. J Biol Chem 275, 6479-89 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 6479-6489
    • Drake, M.T.1    Downs, M.A.2    Traub, L.M.3
  • 36
    • 0042206678 scopus 로고    scopus 로고
    • Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis
    • Duan, L. et al. Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis. J Biol Chem 278, 28950-60 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 28950-28960
    • Duan, L.1
  • 37
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn, R., Hicke, L. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J Biol Chem 276, 25974-81 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 38
    • 0026521394 scopus 로고
    • Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails
    • Ekstrand, A. J., Sugawa, N., James, C. D., Collins, V. P. Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails. Proc Natl Acad Sci U S A 89, 4309-13 (1992)
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4309-4313
    • Ekstrand, A.J.1    Sugawa, N.2    James, C.D.3    Collins, V.P.4
  • 39
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad, K. et al. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol 155, 193-200 (2001)
    • (2001) J Cell Biol , vol.155 , pp. 193-200
    • Farsad, K.1
  • 40
    • 0041706190 scopus 로고    scopus 로고
    • Structure and ubiquitin binding of the ubiquitin interacting motif
    • Fisher, R. D. et al. Structure and ubiquitin binding of the ubiquitin interacting motif. J Biol Chem 278, 28976-84 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 28976-28984
    • Fisher, R.D.1
  • 42
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus, J. E. et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107, 55-65 (2001)
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1
  • 43
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • Giasson, B. I., Lee, V. M. Are ubiquitination pathways central to Parkinson's disease? Cell 114, 1-8 (2003)
    • (2003) Cell , vol.114 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 44
    • 0037432773 scopus 로고    scopus 로고
    • Polyubiquitination of p53 by a ubiquitin ligase activity of p300
    • Grossman, S. R. et al. Polyubiquitination of p53 by a ubiquitin ligase activity of p300. Science 300, 342-4 (2003)
    • (2003) Science , vol.300 , pp. 342-344
    • Grossman, S.R.1
  • 45
    • 0037328823 scopus 로고    scopus 로고
    • Regulation of the Fanconi anemia pathway by monoubiquitination
    • Gregory, R. C., Taniguchi, T., D'Andrea, A. D. Regulation of the Fanconi anemia pathway by monoubiquitination. Semin Cancer Biol 13, 77-82 (2003)
    • (2003) Semin Cancer Biol , vol.13 , pp. 77-82
    • Gregory, R.C.1    Taniguchi, T.2    D'Andrea, A.D.3
  • 46
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K. et al. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol 5, 461-6 (2003)
    • (2003) Nat Cell Biol , vol.5 , pp. 461-466
    • Haglund, K.1
  • 47
    • 0037125983 scopus 로고    scopus 로고
    • Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors
    • Haglund, K., Shimokawa, N., Szymkiewicz, I., Dikic, I. Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc Natl Acad Sci U S A 99, 12191-6 (2002)
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12191-12196
    • Haglund, K.1    Shimokawa, N.2    Szymkiewicz, I.3    Dikic, I.4
  • 48
    • 0033591319 scopus 로고    scopus 로고
    • Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport
    • Hama, H., Tall, G. G., Horazdovsky, B. F. Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport. J Biol Chem 274, 15284-91 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 15284-15291
    • Hama, H.1    Tall, G.G.2    Horazdovsky, B.F.3
  • 50
    • 0035823032 scopus 로고    scopus 로고
    • A new ticket for entry into budding vesicles-ubiquitin
    • Kicke, L. A new ticket for entry into budding vesicles-ubiquitin. Cell 106, 527-30 (2001)
    • (2001) Cell , vol.106 , pp. 527-530
    • Kicke, L.1
  • 51
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2, 195-201 (2001)
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 52
    • 0242413645 scopus 로고    scopus 로고
    • Effect of clathrin heavy chain- and alpha -adaptin specific small interfering RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells
    • Hinrichsen, L., Harborth, J., Andrees, L., Weber, K., Ungewickell, E. J. Effect of clathrin heavy chain- and alpha -adaptin specific small interfering RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells. J Biol Chem (2003)
    • (2003) J Biol Chem
    • Hinrichsen, L.1    Harborth, J.2    Andrees, L.3    Weber, K.4    Ungewickell, E.J.5
  • 53
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock, A. L., Auld, K., Gygi, S. P., Silver, P. A. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc Natl Acad Sci U S A 100, 12735-40 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 54
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-41 (2002)
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 55
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann, K., Bucher, P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21, 172-3 (1996)
    • (1996) Trends Biochem Sci , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 56
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • Hofmann, K., Falquet, L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem Sci 26, 347-50 (2001)
    • (2001) Trends Biochem Sci , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 57
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R. M., Pickart, C. M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96, 645-53 (1999)
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 58
    • 0037108963 scopus 로고    scopus 로고
    • Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
    • Hook, S. S., Orian, A., Cowley, S. M., Eisenman, R. N. Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc Natl Acad Sci U S A 99, 13425-30 (2002)
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13425-13430
    • Hook, S.S.1    Orian, A.2    Cowley, S.M.3    Eisenman, R.N.4
  • 59
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi, H. et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 90, 1149-59 (1997)
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1
  • 60
    • 18444362122 scopus 로고    scopus 로고
    • Biallelic inactivation of BRCA2 in Fanconi anemia
    • Howlett, N. G. et al. Biallelic inactivation of BRCA2 in Fanconi anemia. Science 297, 606-9 (2002)
    • (2002) Science , vol.297 , pp. 606-609
    • Howlett, N.G.1
  • 61
    • 0037590956 scopus 로고    scopus 로고
    • Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85
    • Hutchings, N. J., Clarkson, N., Chalkley, R., Barclay, A. N., Brown, M. H. Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. J Biol Chem 278, 22396-403 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 22396-22403
    • Hutchings, N.J.1    Clarkson, N.2    Chalkley, R.3    Barclay, A.N.4    Brown, M.H.5
  • 62
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang, W. W. et al. A Conserved RING Finger Protein Required for Histone H2B Monoubiquitination and Cell Size Control. Mol Cell 11, 261-6 (2003)
    • (2003) Mol Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1
  • 63
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • Jiang, X., Huang, F., Marusyk, A., Sorkin, A. Grb2 Regulates Internalization of EGF Receptors through Clathrin-coated Pits. Mol Biol Cell 14, 858-70 (2003)
    • (2003) Mol Biol Cell , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 64
    • 0042202634 scopus 로고    scopus 로고
    • Epidermal growth factor receptor internalization through clathrin-coated pits requires Cbl RING finger and proline-rich domains but not receptor polyubiquitylation
    • Jiang, X., Sorkin, A. Epidermal growth factor receptor internalization through clathrin-coated pits requires Cbl RING finger and proline-rich domains but not receptor polyubiquitylation. Traffic 4, 529-43 (2003)
    • (2003) Traffic , vol.4 , pp. 529-543
    • Jiang, X.1    Sorkin, A.2
  • 65
    • 0038820381 scopus 로고    scopus 로고
    • Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding
    • Kang, R. S. et al. Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell 113, 621-30 (2003)
    • (2003) Cell , vol.113 , pp. 621-630
    • Kang, R.S.1
  • 66
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz, M. et al. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3, 740-51 (2002)
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1
  • 67
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J., Babst, M., Emr, S. D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106, 145-55 (2001)
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 68
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., Odorizzi, G., Emr, S. D. Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 3, 893-905 (2002)
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 69
    • 0035895966 scopus 로고    scopus 로고
    • The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction
    • Kirsch, K. H. et al. The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction. J Biol Chem 276, 4957-63 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 4957-4963
    • Kirsch, K.H.1
  • 70
    • 0037163084 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination
    • Klapisz, E. et al. A ubiquitin-interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination. J Biol Chem 277, 30746-53 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 30746-30753
    • Klapisz, E.1
  • 71
    • 0033151614 scopus 로고    scopus 로고
    • Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis
    • Komada, M., Soriano, P. Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev 13, 1475-85 (1999)
    • (1999) Genes Dev , vol.13 , pp. 1475-1485
    • Komada, M.1    Soriano, P.2
  • 72
    • 0141994813 scopus 로고    scopus 로고
    • Identification of a novel proline-arginine motif involved in CIN85-dependent clustering of Cbl and down-regulation of epidermal growth factor receptors
    • Kowanetz, K. et al. Identification of a novel proline-arginine motif involved in CIN85-dependent clustering of Cbl and down-regulation of epidermal growth factor receptors. J Biol Chem 278, 39735-46 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 39735-39746
    • Kowanetz, K.1
  • 73
    • 0035853045 scopus 로고    scopus 로고
    • Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling
    • Lafont, F., Simons, K. Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE- triggered cell signaling. Proc Natl Acad Sci U S A 98, 3180-4. (2001)
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3180-3184
    • Lafont, F.1    Simons, K.2
  • 74
    • 0035903157 scopus 로고    scopus 로고
    • Human mdm2 mediates multiple mono-ubiquitination of p53 by a mechanism requiring enzyme isomerization
    • Lai, Z. et al. Human mdm2 mediates multiple mono-ubiquitination of p53 by a mechanism requiring enzyme isomerization. J Biol Chem 276, 31357-67 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 31357-31367
    • Lai, Z.1
  • 75
    • 0033169024 scopus 로고    scopus 로고
    • The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation
    • Lee, P. S. et al. The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation. Embo J 18, 3616-28 (1999)
    • (1999) Embo J , vol.18 , pp. 3616-3628
    • Lee, P.S.1
  • 76
    • 0032217156 scopus 로고    scopus 로고
    • c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz, G. et al. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev 12, 3663-74. (1998)
    • (1998) Genes Dev , vol.12 , pp. 3663-3674
    • Levkowitz, G.1
  • 77
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz, G. et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 4, 1029-40 (1999)
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1
  • 78
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • Li, L., Cohen, S. N. Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell 85, 319-29 (1996)
    • (1996) Cell , vol.85 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 79
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li, Q., Verma, I. M. NF-kappaB regulation in the immune system. Nat Rev Immunol 2, 725-34 (2002)
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 80
    • 1842337370 scopus 로고    scopus 로고
    • Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA
    • Lo Ten Foe, J. R. et al. Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA. Nat Genet 14, 320-3 (1996)
    • (1996) Nat Genet , vol.14 , pp. 320-323
    • Lo Ten Foe, J.R.1
  • 81
    • 0242290342 scopus 로고    scopus 로고
    • WW domain HECT E3 s target Cbl RING finger E3 s for proteasomal degradation
    • Magnifico, A. et al. WW Domain HECT E3 s Target Cbl RING Finger E3 s for Proteasomal Degradation. J Biol Chem 278, 43169-77 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 43169-43177
    • Magnifico, A.1
  • 82
    • 0037177868 scopus 로고    scopus 로고
    • c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms
    • Mancini, A., Koch, A., Wilms, R., Tamura, T. c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms. J Biol Chem 277, 14635-40. (2002)
    • (2002) J Biol Chem , vol.277 , pp. 14635-14640
    • Mancini, A.1    Koch, A.2    Wilms, R.3    Tamura, T.4
  • 83
    • 0038724478 scopus 로고    scopus 로고
    • Energetics and specificity of interactions within Ub.Uev.Ubc 13 human ubiquitin conjugation complexes
    • McKenna, S. et al. Energetics and specificity of interactions within Ub.Uev.Ubc13 human ubiquitin conjugation complexes. Biochemistry 42, 7922-30 (2003)
    • (2003) Biochemistry , vol.42 , pp. 7922-7930
    • McKenna, S.1
  • 84
    • 0141484612 scopus 로고    scopus 로고
    • A novel ubiquitin ligase is deficient in Fanconi anemia
    • Meetei, A. R. et al. A novel ubiquitin ligase is deficient in Fanconi anemia. Nat Genet 35, 165-70 (2003)
    • (2003) Nat Genet , vol.35 , pp. 165-170
    • Meetei, A.R.1
  • 85
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-nonclassical ubiquitin
    • Melchior, F. SUMO-nonclassical ubiquitin. Annu Rev Cell Dev Biol 16, 591-626 (2000)
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 86
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer, H. H., Wang, Y., Warren, G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. Embo J 21, 5645-52 (2002)
    • (2002) Embo J , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 87
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha
    • Miyake, S., Lupher, M. L., Jr., Druker, B., Band, H. The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha. Proc Natl Acad Sci U S A 95, 7927-32 (1998)
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7927-7932
    • Miyake, S.1    Lupher Jr., M.L.2    Druker, B.3    Band, H.4
  • 88
    • 0036196880 scopus 로고    scopus 로고
    • The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae
    • Mochida, J., Yamamoto, T., Fujimura-Kamada, K., Tanaka, K. The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae. Genetics 160, 923-34 (2002)
    • (2002) Genetics , vol.160 , pp. 923-934
    • Mochida, J.1    Yamamoto, T.2    Fujimura-Kamada, K.3    Tanaka, K.4
  • 89
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson, Y. et al. Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J Biol Chem 278, 21323-6 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 21323-21326
    • Mosesson, Y.1
  • 90
    • 0027402689 scopus 로고
    • Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling
    • Mori, S., Heldin, C. H., Claesson-Welsh, L. Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling. J Biol Chem 268, 577-83 (1993)
    • (1993) J Biol Chem , vol.268 , pp. 577-583
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 91
    • 0042232673 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis in AP-2-depleted cells
    • Motley, A., Bright, N. A., Seaman, M. N., Robinson, M. S. Clathrin-mediated endocytosis in AP-2-depleted cells. J Cell Biol 162, 909-18 (2003)
    • (2003) J Cell Biol , vol.162 , pp. 909-918
    • Motley, A.1    Bright, N.A.2    Seaman, M.N.3    Robinson, M.S.4
  • 92
    • 0036300780 scopus 로고    scopus 로고
    • Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
    • Mueller, T. D., Feigon, J. Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J Mol Biol 319, 1243-55 (2002)
    • (2002) J Mol Biol , vol.319 , pp. 1243-1255
    • Mueller, T.D.1    Feigon, J.2
  • 94
    • 0034912714 scopus 로고    scopus 로고
    • Transcriptional coactivator complexes
    • Naar, A. M., Lemon, B. D., Tjian, R. Transcriptional coactivator complexes. Annu Rev Biochem 70, 475-501 (2001)
    • (2001) Annu Rev Biochem , vol.70 , pp. 475-501
    • Naar, A.M.1    Lemon, B.D.2    Tjian, R.3
  • 95
    • 0034714368 scopus 로고    scopus 로고
    • A Di-leucine signal in the ubiquitin moiety. Possible involvement in ubiquitination-mediated endocytosis
    • Nakatsu, F. et al. A Di-leucine signal in the ubiquitin moiety. Possible involvement in ubiquitination-mediated endocytosis. J Biol Chem 275, 26213-9 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 26213-26219
    • Nakatsu, F.1
  • 96
    • 0036948433 scopus 로고    scopus 로고
    • Toward maintaining the genome: DNA damage and replication checkpoints
    • Nyberg, K. A., Michelson, R. J., Putnam, C. W., Weinert, T. A. Toward maintaining the genome: DNA damage and replication checkpoints. Annu Rev Genet 36, 617-56 (2002)
    • (2002) Annu Rev Genet , vol.36 , pp. 617-656
    • Nyberg, K.A.1    Michelson, R.J.2    Putnam, C.W.3    Weinert, T.A.4
  • 97
    • 0037046805 scopus 로고    scopus 로고
    • The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination
    • Oldham, C. E., Mohney, R. P., Miller, S. L., Hanes, R. N., O'Bryan, J. P. The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination. Curr Biol 12, 1112-6 (2002)
    • (2002) Curr Biol , vol.12 , pp. 1112-1116
    • Oldham, C.E.1    Mohney, R.P.2    Miller, S.L.3    Hanes, R.N.4    O'Bryan, J.P.5
  • 98
    • 0034282219 scopus 로고    scopus 로고
    • The DNA repair protein rad23 is a negative regulator of multiubiquitin chain assembly
    • Ortolan, T. G. et al. The DNA repair protein rad23 is a negative regulator of multiubiquitin chain assembly. Nat Cell Biol 2, 601-8 (2000)
    • (2000) Nat Cell Biol , vol.2 , pp. 601-608
    • Ortolan, T.G.1
  • 99
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng, J. et al. A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21, 921-926 (2003)
    • (2003) Nat Biotechnol , vol.21 , pp. 921-926
    • Peng, J.1
  • 100
    • 0035930341 scopus 로고    scopus 로고
    • Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein
    • Peschard, P. et al. Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein. Mol Cell 8, 995-1004. (2001)
    • (2001) Mol Cell , vol.8 , pp. 995-1004
    • Peschard, P.1
  • 101
    • 0037075606 scopus 로고    scopus 로고
    • The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met
    • Petrelli, A. et al. The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met. Nature 416, 187-90. (2002)
    • (2002) Nature , vol.416 , pp. 187-190
    • Petrelli, A.1
  • 102
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila
    • Pham, A. D., Sauer, F. Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila. Science 289, 2357-60 (2000)
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.D.1    Sauer, F.2
  • 103
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart, C. M. Ubiquitin in chains. Trends Biochem Sci 25, 544-8 (2000)
    • (2000) Trends Biochem Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 104
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu Rev Biochem 70, 503-33 (2001)
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 105
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R. C., Cooper, A. A., Yang, H., Stevens, T. H. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J Cell Biol 131, 603-17 (1995)
    • (1995) J Cell Biol , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.4
  • 106
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451-5 (2002)
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1
  • 107
    • 0034667598 scopus 로고    scopus 로고
    • Proteins of the endoplasmic-reticulum-associated degradation pathway: Domain detection and function prediction
    • Ponting, C. P. Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. Biochem J 351 Pt 2, 527-35 (2000)
    • (2000) Biochem J , vol.351 , Issue.PART 2 , pp. 527-535
    • Ponting, C.P.1
  • 108
    • 0037093316 scopus 로고    scopus 로고
    • Structure and functional interactions of the Tsg101 UEV domain
    • Pornillos, O. et al. Structure and functional interactions of the Tsg101 UEV domain. Embo J 21, 2397-406 (2002)
    • (2002) Embo J , vol.21 , pp. 2397-2406
    • Pornillos, O.1
  • 109
    • 0038820382 scopus 로고    scopus 로고
    • Mechanism of ubiquitin recognition by the CUE domain of Vps9p
    • Prag, G. et al. Mechanism of ubiquitin recognition by the CUE domain of Vps9p. Cell 113, 609-20 (2003)
    • (2003) Cell , vol.113 , pp. 609-620
    • Prag, G.1
  • 110
    • 0036094538 scopus 로고    scopus 로고
    • Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
    • Raiborg, C. et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nat Cell Biol 4, 394-8 (2002)
    • (2002) Nat Cell Biol , vol.4 , pp. 394-398
    • Raiborg, C.1
  • 111
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23
    • Rao, H., Sastry, A. Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277, 11691-5 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 11691-11695
    • Rao, H.1    Sastry, A.2
  • 113
    • 0033199465 scopus 로고    scopus 로고
    • Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis
    • Ringstad, N. et al. Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. Neuron 24, 143-54 (1999)
    • (1999) Neuron , vol.24 , pp. 143-154
    • Ringstad, N.1
  • 114
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk, K., Recht, J., Osley, M. A. Rad6-dependent ubiquitination of histone H2B in yeast. Science 287, 501-4 (2000)
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 115
    • 0242684548 scopus 로고    scopus 로고
    • Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops
    • Rubin, C. et al. Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops. Curr Biol 13, 297-307 (2003)
    • (2003) Curr Biol , vol.13 , pp. 297-307
    • Rubin, C.1
  • 116
    • 0033730605 scopus 로고    scopus 로고
    • Functional analyses of interacting factors involved in both pre-mRNA splicing and cell cycle progression in Saccharomyces cerevisiae
    • Russell, C. S., Ben-Yehuda, S., Dix, I., Kupiec, M., Beggs, J. D. Functional analyses of interacting factors involved in both pre-mRNA splicing and cell cycle progression in Saccharomyces cerevisiae. Rna 6, 1565-72 (2000)
    • (2000) Rna , vol.6 , pp. 1565-1572
    • Russell, C.S.1    Ben-Yehuda, S.2    Dix, I.3    Kupiec, M.4    Beggs, J.D.5
  • 118
    • 0035960748 scopus 로고    scopus 로고
    • The Cbl family: Ubiquitin ligases regulating signaling by tyrosine kinases
    • Sanjay, A., Horne, W. C., Baron, R. The Cbl family: ubiquitin ligases regulating signaling by tyrosine kinases. Sci STKE 2001, E40. (2001)
    • (2001) Sci STKE , vol.2001
    • Sanjay, A.1    Horne, W.C.2    Baron, R.3
  • 119
    • 0033539120 scopus 로고    scopus 로고
    • Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid
    • Schmidt, A. et al. Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid. Nature 401, 133-41 (1999)
    • (1999) Nature , vol.401 , pp. 133-141
    • Schmidt, A.1
  • 120
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell, J. D., Hicke, L. Non-traditional Functions of Ubiquitin and Ubiquitin-binding proteins. J Biol Chem (2003)
    • (2003) J Biol Chem
    • Schnell, J.D.1    Hicke, L.2
  • 121
    • 0037016681 scopus 로고    scopus 로고
    • Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion
    • Seachrist, J. L. et al. Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion. J Biol Chem 277, 679-85 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 679-685
    • Seachrist, J.L.1
  • 122
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny, D. et al. Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol Cell Biol 21, 8035-44 (2001)
    • (2001) Mol Cell Biol , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1
  • 123
    • 0036392305 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins
    • Shekhtman, A., Cowburn, D. A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochem Biophys Res Commun 296, 1222-7 (2002)
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 1222-1227
    • Shekhtman, A.1    Cowburn, D.2
  • 124
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih, S. C., Sloper-Mould, K. E., Hicke, L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. Embo J 19, 187-98 (2000)
    • (2000) Embo J , vol.19 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 125
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih, S. C. et al. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 4, 389-93 (2002)
    • (2002) Nat Cell Biol , vol.4 , pp. 389-393
    • Shih, S.C.1
  • 126
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • Shih, S. C. et al. A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. Embo J 22, 1273-81 (2003)
    • (2003) Embo J , vol.22 , pp. 1273-1281
    • Shih, S.C.1
  • 127
    • 0026061323 scopus 로고
    • Dissecting the activating mutations in v-erbB of avian erythroblastosis virus strain R
    • Shu, H. K., Pelley, R. J., Kung, H. J. Dissecting the activating mutations in v-erbB of avian erythroblastosis virus strain R. J Virol 65, 6173-80 (1991)
    • (1991) J Virol , vol.65 , pp. 6173-6180
    • Shu, H.K.1    Pelley, R.J.2    Kung, H.J.3
  • 128
    • 0037016772 scopus 로고    scopus 로고
    • Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel
    • Snyder, P. M., Olson, D. R., Thomas, B. C. Serum and glucocorticoid- regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. J Biol Chem 277, 5-8 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 5-8
    • Snyder, P.M.1    Olson, D.R.2    Thomas, B.C.3
  • 129
    • 0034859108 scopus 로고    scopus 로고
    • Internalization of the epidermal growth factor receptor: Role in signalling
    • Sorkin, A. Internalization of the epidermal growth factor receptor: role in signalling. Biochem Soc Trans 29, 480-4 (2001)
    • (2001) Biochem Soc Trans , vol.29 , pp. 480-484
    • Sorkin, A.1
  • 130
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y., Dikic, I. Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416, 183-7. (2002)
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 131
    • 0034607805 scopus 로고    scopus 로고
    • Polyubiquitination of the epidermal growth factor receptor occurs at the plasma membrane upon ligand-induced activation
    • Stang, E., Johannessen, L. E., Knardal, S. L., Madshus, I. H. Polyubiquitination of the epidermal growth factor receptor occurs at the plasma membrane upon ligand-induced activation. J Biol Chem 275, 13940-7 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 13940-13947
    • Stang, E.1    Johannessen, L.E.2    Knardal, S.L.3    Madshus, I.H.4
  • 132
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P., Ulrich, H. D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-91 (2003)
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 133
    • 0026735882 scopus 로고
    • Cloning of cDNAs for Fanconi's anaemia by functional complementation
    • Strathdee, C. A., Gavish, H., Shannon, W. R., Buchwald, M. Cloning of cDNAs for Fanconi's anaemia by functional complementation. Nature 358, 434 (1992)
    • (1992) Nature , vol.358 , pp. 434
    • Strathdee, C.A.1    Gavish, H.2    Shannon, W.R.3    Buchwald, M.4
  • 134
    • 0037010119 scopus 로고    scopus 로고
    • Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function
    • Strous, G. J., Gent, J. Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function. FEBS Lett 529, 102-9 (2002)
    • (2002) FEBS Lett , vol.529 , pp. 102-109
    • Strous, G.J.1    Gent, J.2
  • 135
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A., Schwartz, A. L. The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. Embo J 15, 3806-12. (1996)
    • (1996) Embo J , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 136
    • 0033596125 scopus 로고    scopus 로고
    • Persistent activation of NF-kappaB by the tax transforming protein of HTLV-1: Hijacking cellular IkappaB kinases
    • Sun, S. C., Ballard, D. W. Persistent activation of NF-kappaB by the tax transforming protein of HTLV-1: hijacking cellular IkappaB kinases. Oncogene 18, 6948-58 (1999)
    • (1999) Oncogene , vol.18 , pp. 6948-6958
    • Sun, S.C.1    Ballard, D.W.2
  • 137
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z. W., Allis, C. D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-8 (2002)
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 138
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L., Radhakrishnan, I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. Embo J 22, 4597-606 (2003)
    • (2003) Embo J , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 139
    • 0037131177 scopus 로고    scopus 로고
    • CIN85 Participates in Cbl-b-mediated Down-regulation of Receptor Tyrosine Kinases
    • Szymkiewicz, I. et al. CIN85 Participates in Cbl-b-mediated Down-regulation of Receptor Tyrosine Kinases. J Biol Chem 277, 39666-72. (2002)
    • (2002) J Biol Chem , vol.277 , pp. 39666-39672
    • Szymkiewicz, I.1
  • 140
    • 0036784661 scopus 로고    scopus 로고
    • c-Cbl is involved in met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination
    • Taher, T. E. et al. c-Cbl Is Involved in Met Signaling in B Cells and Mediates Hepatocyte Growth Factor-Induced Receptor Ubiquitination. J Immunol 169, 3793-800. (2002)
    • (2002) J Immunol , vol.169 , pp. 3793-3800
    • Taher, T.E.1
  • 141
    • 0036463957 scopus 로고    scopus 로고
    • Molecular pathogenesis of fanconi anemia
    • Taniguchi, T., Dandrea, A. D. Molecular pathogenesis of fanconi anemia. Int J Hematol 75, 123-8 (2002)
    • (2002) Int J Hematol , vol.75 , pp. 123-128
    • Taniguchi, T.1    Dandrea, A.D.2
  • 142
    • 0036785375 scopus 로고    scopus 로고
    • S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51
    • Taniguchi, T. et al. S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51. Blood 100, 2414-20 (2002)
    • (2002) Blood , vol.100 , pp. 2414-2420
    • Taniguchi, T.1
  • 143
    • 0037123768 scopus 로고    scopus 로고
    • Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways
    • Taniguchi, T. et al. Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways. Cell 109, 459-72 (2002)
    • (2002) Cell , vol.109 , pp. 459-472
    • Taniguchi, T.1
  • 144
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., Shih, S., Dunn, R., Hicke, L. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell 1, 193-202 (1998)
    • (1998) Mol Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 145
    • 0035106341 scopus 로고    scopus 로고
    • RING finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation
    • Thien, C. B., Walker, F., Langdon, W. Y. RING finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation. Mol Cell 7, 355-65. (2001)
    • (2001) Mol Cell , vol.7 , pp. 355-365
    • Thien, C.B.1    Walker, F.2    Langdon, W.Y.3
  • 147
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark, A. P., Hofmann, R. M., Tsui, C., Pickart, C. M., Wolberger, C. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 105, 711-20 (2001)
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 148
    • 0042671242 scopus 로고    scopus 로고
    • BRCA1-independent ubiquitination of FANCD2
    • Vandenberg, C. J. et al. BRCA1-independent ubiquitination of FANCD2. Mol Cell 12, 247-54 (2003)
    • (2003) Mol Cell , vol.12 , pp. 247-254
    • Vandenberg, C.J.1
  • 149
    • 0035861729 scopus 로고    scopus 로고
    • Rab5-dependent trafficking of the m4 muscarinic acetylcholine receptor to the plasma membrane, early endosomes, and multivesicular bodies
    • Volpicelli, L. A., Lah, J. J., Levey, A. I. Rab5-dependent trafficking of the m4 muscarinic acetylcholine receptor to the plasma membrane, early endosomes, and multivesicular bodies. J Biol Chem 276, 47590-8 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 47590-47598
    • Volpicelli, L.A.1    Lah, J.J.2    Levey, A.I.3
  • 150
    • 0033813625 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis and human disease
    • Vu, P. K., Sakamoto, K. M. Ubiquitin-mediated proteolysis and human disease. Mol Genet Metab 71, 261-6 (2000)
    • (2000) Mol Genet Metab , vol.71 , pp. 261-266
    • Vu, P.K.1    Sakamoto, K.M.2
  • 151
    • 0038036801 scopus 로고    scopus 로고
    • Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4
    • Wang, B. et al. Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4. J Biol Chem 278, 20225-34 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 20225-20234
    • Wang, B.1
  • 152
    • 0032890156 scopus 로고    scopus 로고
    • CSF-1 stimulated multiubiquitination of the CSF-1 receptor and of Cbl follows their tyrosine phosphorylation and association with other signaling proteins
    • Wang, Y., Yeung, Y. G., Stanley, E. R. CSF-1 stimulated multiubiquitination of the CSF-1 receptor and of Cbl follows their tyrosine phosphorylation and association with other signaling proteins. J Cell Biochem 72, 119-34 (1999)
    • (1999) J Cell Biochem , vol.72 , pp. 119-134
    • Wang, Y.1    Yeung, Y.G.2    Stanley, E.R.3
  • 153
    • 0036039649 scopus 로고    scopus 로고
    • Negative regulation of EphA2 receptor by Cbl
    • Wang, Y. et al. Negative regulation of EphA2 receptor by Cbl. Biochem Biophys Res Commun 296, 214-20. (2002)
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 214-220
    • Wang, Y.1
  • 154
    • 0034638634 scopus 로고    scopus 로고
    • Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes
    • Watanabe, S. et al. Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes. Biochem Biophys Res Commun 278, 167-74 (2000)
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 167-174
    • Watanabe, S.1
  • 155
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • Waterman, H. et al. A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. Embo J 21, 303-13 (2002)
    • (2002) Embo J , vol.21 , pp. 303-313
    • Waterman, H.1
  • 156
    • 0033525759 scopus 로고    scopus 로고
    • EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake
    • Wilde, A. et al. EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake. Cell 96, 677-87 (1999)
    • (1999) Cell , vol.96 , pp. 677-687
    • Wilde, A.1
  • 157
    • 0034798985 scopus 로고    scopus 로고
    • Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
    • Wilkinson, C. R. et al. Proteins containing the UBA domain are able to bind to multi-ubiquitin chains. Nat Cell Biol 3, 939-43 (2001)
    • (2001) Nat Cell Biol , vol.3 , pp. 939-943
    • Wilkinson, C.R.1
  • 158
    • 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. Semin Cell Dev Biol 11, 141-8. (2000)
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 159
    • 0037076329 scopus 로고    scopus 로고
    • FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl
    • Wong, A. et al. FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl. Proc Natl Acad Sci U S A 99, 6684-9. (2002)
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6684-6689
    • Wong, A.1
  • 160
    • 0037248944 scopus 로고    scopus 로고
    • Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter
    • Wood, A. et al. Bre1, an E3 ubiquitin ligase required for recruitment and substrate selection of Rad6 at a promoter. Mol Cell 11, 267-74 (2003)
    • (2003) Mol Cell , vol.11 , pp. 267-274
    • Wood, A.1
  • 161
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi, M. et al. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J Biol Chem 274, 31707-12. (1999)
    • (1999) J Biol Chem , vol.274 , pp. 31707-31712
    • Yokouchi, M.1
  • 162
    • 0035860713 scopus 로고    scopus 로고
    • Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins
    • Yokouchi, M. et al. Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins. J Biol Chem 276, 35185-93. (2001)
    • (2001) J Biol Chem , vol.276 , pp. 35185-35193
    • Yokouchi, M.1
  • 163
    • 0033002197 scopus 로고    scopus 로고
    • Bridging the gap: Composition, regulation, and physiological function of the IkappaB kinase complex
    • Zandi, E., Karin, M. Bridging the gap: composition, regulation, and physiological function of the IkappaB kinase complex. Mol Cell Biol 19, 4547-51 (1999)
    • (1999) Mol Cell Biol , vol.19 , pp. 4547-4551
    • Zandi, E.1    Karin, M.2


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