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Volumn 8, Issue SUPPL. 1, 2007, Pages

Ubiquitin domain proteins in disease

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 3; CARRIER PROTEIN; ELONGIN B; PARKIN; UBIQUILIN; UBIQUITIN;

EID: 38449101038     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-8-S1-S1     Document Type: Review
Times cited : (26)

References (74)
  • 1
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • 11917093
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. MH Glickman A Ciechanover, Physiol Rev 2002 82 373 428 11917093
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • 10.1146/annurev.biochem.70.1.503. 11395416
    • Mechanisms underlying ubiquitination. CM Pickart, Annu Rev Biochem 2001 70 503 533 10.1146/annurev.biochem.70.1.503 11395416
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • 10.1016/S0092-8674(00)80574-7. 10089879
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. M Koegl T Hoppe S Schlenker HD Ulrich TU Mayer S Jentsch, Cell 1999 96 635 644 10.1016/S0092-8674(00)80574-7 10089879
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 4
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • 10.1006/scdb.2000.0164. 10906270
    • Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. KD Wilkinson, Semin Cell Dev Biol 2000 11 141 148 10.1006/scdb.2000.0164 10906270
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 5
    • 0028235965 scopus 로고
    • A 26 S protease subunit that binds ubiquitin conjugates
    • 8125911
    • A 26 S protease subunit that binds ubiquitin conjugates. Q Deveraux V Ustrell C Pickart M Rechsteiner, J Biol Chem 1994 269 7059 7061 8125911
    • (1994) J Biol Chem , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 6
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • 10619848. 10.1093/emboj/19.1.94
    • Recognition of the polyubiquitin proteolytic signal. JS Thrower L Hoffman M Rechsteiner CM Pickart, Embo J 2000 19 94 102 10619848 10.1093/emboj/19.1.94
    • (2000) Embo J , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 7
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • 10.1016/S0092-8674(00)00126-4. 11057907
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. L Deng C Wang E Spencer L Yang A Braun J You C Slaughter C Pickart ZJ Chen, Cell 2000 103 351 361 10.1016/S0092-8674(00)00126-4 11057907
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 9
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • 10.1038/35056583. 11265249
    • Protein regulation by monoubiquitin. L Hicke, Nat Rev Mol Cell Biol 2001 2 195 201 10.1038/35056583 11265249
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 10
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • 10.1016/0022-2836(87)90679-6. 3041007
    • Structure of ubiquitin refined at 1.8 Å resolution. S Vijay-Kumar CE Bugg WJ Cook, J Mol Biol 1987 194 531 544 10.1016/0022-2836(87)90679-6 3041007
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 11
    • 1342300578 scopus 로고    scopus 로고
    • Integral UBL domain proteins: A family of proteasome interacting proteins
    • 10.1016/j.semcdb.2003.12.006. 15209385
    • Integral UBL domain proteins: a family of proteasome interacting proteins. R Hartmann-Petersen C Gordon, Semin Cell Dev Biol 2004 15 247 259 10.1016/j.semcdb.2003.12.006 15209385
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 247-259
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 12
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • 10.1016/S0962-8924(00)01785-2. 10884686
    • Ubiquitin and its kin: how close are the family ties? S Jentsch G Pyrowolakis, Trends Cell Biol 2000 10 335 342 10.1016/S0962-8924(00)01785-2 10884686
    • (2000) Trends Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 15
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway
    • 10.1016/j.jmb.2005.10.020. 16289116
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. A Schulze S Standera E Buerger M Kikkert S van Voorden E Wiertz F Koning PM Kloetzel M Seeger, J Mol Biol 2005 354 1021 1027 10.1016/j.jmb.2005.10.020 16289116
    • (2005) J Mol Biol , vol.354 , pp. 1021-1027
    • Schulze, A.1    Standera, S.2    Buerger, E.3    Kikkert, M.4    Van Voorden, S.5    Wiertz, E.6    Koning, F.7    Kloetzel, P.M.8    Seeger, M.9
  • 16
    • 0037221535 scopus 로고    scopus 로고
    • Transferring substrates to the 26S proteasome
    • 10.1016/S0968-0004(02)00002-6. 12517449
    • Transferring substrates to the 26S proteasome. R Hartmann-Petersen M Seeger C Gordon, Trends Biochem Sci 2003 28 26 31 10.1016/S0968-0004(02)00002-6 12517449
    • (2003) Trends Biochem Sci , vol.28 , pp. 26-31
    • Hartmann-Petersen, R.1    Seeger, M.2    Gordon, C.3
  • 17
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • 10.1016/j.cell.2004.06.014. 15242647
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. R Verma R Oania J Graumann RJ Deshaies, Cell 2004 118 99 110 10.1016/j.cell.2004.06.014 15242647
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 18
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. the ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • 10.1074/jbc.274.39.28019. 10488153
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. H Hiyama M Yokoi C Masutani K Sugasawa T Maekawa K Tanaka JH Hoeijmakers F Hanaoka, J Biol Chem 1999 274 28019 28025 10.1074/jbc.274.39.28019 10488153
    • (1999) J Biol Chem , vol.274 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3    Sugasawa, K.4    Maekawa, T.5    Tanaka, K.6    Hoeijmakers, J.H.7    Hanaoka, F.8
  • 19
    • 0033636785 scopus 로고    scopus 로고
    • The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome
    • 10.1016/S1097-2765(00)00040-X. 10983987
    • The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. MF Kleijnen AH Shih P Zhou S Kumar RE Soccio NL Kedersha G Gill PM Howley, Mol Cell 2000 6 409 419 10.1016/S1097-2765(00)00040-X 10983987
    • (2000) Mol Cell , vol.6 , pp. 409-419
    • Kleijnen, M.F.1    Shih, A.H.2    Zhou, P.3    Kumar, S.4    Soccio, R.E.5    Kedersha, N.L.6    Gill, G.7    Howley, P.M.8
  • 21
    • 0038268188 scopus 로고    scopus 로고
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins
    • 10.1074/jbc.M208281200. 12615927
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. M Seeger R Hartmann-Petersen CR Wilkinson M Wallace I Samejima MS Taylor C Gordon, J Biol Chem 2003 278 16791 16796 10.1074/jbc.M208281200 12615927
    • (2003) J Biol Chem , vol.278 , pp. 16791-16796
    • Seeger, M.1    Hartmann-Petersen, R.2    Wilkinson, C.R.3    Wallace, M.4    Samejima, I.5    Taylor, M.S.6    Gordon, C.7
  • 22
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • 15121879. 10.1091/mbc.E03-11-0835
    • Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. I Kim K Mi H Rao, Mol Biol Cell 2004 15 3357 3365 15121879 10.1091/mbc.E03-11-0835
    • (2004) Mol Biol Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 23
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • 10.1016/j.cell.2004.11.013. 15652483
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. H Richly M Rape S Braun S Rumpf C Hoege S Jentsch, Cell 2005 120 73 84 10.1016/j.cell.2004.11.013 15652483
    • (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
  • 24
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • 10.1093/hmg/9.12.1795. 10915768
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. G Wang N Sawai S Kotliarova I Kanazawa N Nukina, Hum Mol Genet 2000 9 1795 1803 10.1093/hmg/9.12.1795 10915768
    • (2000) Hum Mol Genet , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3    Kanazawa, I.4    Nukina, N.5
  • 25
    • 23044515498 scopus 로고    scopus 로고
    • The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition
    • 16020535. 10.1073/pnas.0501732102
    • The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition. G Nicastro RP Menon L Masino PP Knowles NQ McDonald A Pastore, Proc Natl Acad Sci U S A 2005 102 10493 10498 16020535 10.1073/pnas.0501732102
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 10493-10498
    • Nicastro, G.1    Menon, R.P.2    Masino, L.3    Knowles, P.P.4    McDonald, N.Q.5    Pastore, A.6
  • 26
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • 12944474. 10.1128/MCB.23.18.6469-6483.2003
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. EW Doss-Pepe ES Stenroos WG Johnson K Madura, Mol Cell Biol 2003 23 6469 6483 12944474 10.1128/MCB.23.18.6469-6483. 2003
    • (2003) Mol Cell Biol , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 28
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • 10.1083/jcb.151.4.847. 11076969
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. AL Mah G Perry MA Smith MJ Monteiro, J Cell Biol 2000 151 847 862 10.1083/jcb.151.4.847 11076969
    • (2000) J Cell Biol , vol.151 , pp. 847-862
    • Mah, A.L.1    Perry, G.2    Smith, M.A.3    Monteiro, M.J.4
  • 30
    • 33746310315 scopus 로고    scopus 로고
    • Alzheimer's disease
    • 10.1016/S0140-6736(06)69113-7. 16876668
    • Alzheimer's disease. K Blennow MJ de Leon H Zetterberg, Lancet 2006 368 387 403 10.1016/S0140-6736(06)69113-7 16876668
    • (2006) Lancet , vol.368 , pp. 387-403
    • Blennow, K.1    De Leon, M.J.2    Zetterberg, H.3
  • 31
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • 10.1038/ncb1104-1054. 15516999
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. DJ Selkoe, Nat Cell Biol 2004 6 1054 1061 10.1038/ncb1104-1054 15516999
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 34
    • 0034310719 scopus 로고    scopus 로고
    • Constitutive endocytosis of GABAA receptors by an association with the adaptin AP2 complex modulates inhibitory synaptic currents in hippocampal neurons
    • 11050117
    • Constitutive endocytosis of GABAA receptors by an association with the adaptin AP2 complex modulates inhibitory synaptic currents in hippocampal neurons. JT Kittler P Delmas JN Jovanovic DA Brown TG Smart SJ Moss, J Neurosci 2000 20 7972 7977 11050117
    • (2000) J Neurosci , vol.20 , pp. 7972-7977
    • Kittler, J.T.1    Delmas, P.2    Jovanovic, J.N.3    Brown, D.A.4    Smart, T.G.5    Moss, S.J.6
  • 38
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • 10.1074/jbc.M508786200. 16192271
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. A Iwata BE Riley JA Johnston RR Kopito, J Biol Chem 2005 280 40282 40292 10.1074/jbc.M508786200 16192271
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 39
    • 0034703397 scopus 로고    scopus 로고
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein
    • 11001934
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein. JD Davidson B Riley EN Burright LA Duvick HY Zoghbi HT Orr, Hum Mol Genet 2000 9 2305 2312 11001934
    • (2000) Hum Mol Genet , vol.9 , pp. 2305-2312
    • Davidson, J.D.1    Riley, B.2    Burright, E.N.3    Duvick, L.A.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 40
    • 4744372012 scopus 로고    scopus 로고
    • The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up
    • 10.1074/jbc.M406284200. 15280365
    • The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up. BE Riley Y Xu HY Zoghbi HT Orr, J Biol Chem 2004 279 42290 42301 10.1074/jbc.M406284200 15280365
    • (2004) J Biol Chem , vol.279 , pp. 42290-42301
    • Riley, B.E.1    Xu, Y.2    Zoghbi, H.Y.3    Orr, H.T.4
  • 43
    • 1542285483 scopus 로고    scopus 로고
    • Genetics of parkin-linked disease
    • 10.1007/s00439-003-1074-6. 14727181
    • Genetics of parkin-linked disease. AB West NT Maidment, Hum Genet 2004 114 327 336 10.1007/s00439-003-1074-6 14727181
    • (2004) Hum Genet , vol.114 , pp. 327-336
    • West, A.B.1    Maidment, N.T.2
  • 44
    • 0142074728 scopus 로고    scopus 로고
    • Parkin is recruited to the centrosome in response to inhibition of proteasomes
    • 10.1242/jcs.00700. 12928331
    • Parkin is recruited to the centrosome in response to inhibition of proteasomes. J Zhao Y Ren Q Jiang J Feng, J Cell Sci 2003 116 4011 4019 10.1242/jcs.00700 12928331
    • (2003) J Cell Sci , vol.116 , pp. 4011-4019
    • Zhao, J.1    Ren, Y.2    Jiang, Q.3    Feng, J.4
  • 46
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • 11078524. 10.1073/pnas.240347797
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Y Zhang J Gao KK Chung H Huang VL Dawson TM Dawson, Proc Natl Acad Sci U S A 2000 97 13354 13359 11078524 10.1073/pnas.240347797
    • (2000) Proc Natl Acad Sci U S a , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 47
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • 10.1074/jbc.C000447200. 10973942
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. Y Imai M Soda R Takahashi, J Biol Chem 2000 275 35661 35664 10.1074/jbc.C000447200 10973942
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 48
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • 10.1038/nm1001-1144. 11590439
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. KK Chung Y Zhang KL Lim Y Tanaka H Huang J Gao CA Ross VL Dawson TM Dawson, Nat Med 2001 7 1144 1150 10.1038/nm1001-1144 11590439
    • (2001) Nat Med , vol.7 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 49
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • 10.1016/S0092-8674(01)00407-X. 11439185
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Y Imai M Soda H Inoue N Hattori Y Mizuno R Takahashi, Cell 2001 105 891 902 10.1016/S0092-8674(01)00407- X 11439185
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 51
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • 10.1016/S0896-6273(03)00084-9. 12628165
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. JF Staropoli C McDermott C Martinat B Schulman E Demireva A Abeliovich, Neuron 2003 37 735 749 10.1016/S0896-6273(03)00084-9 12628165
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 53
    • 33344456519 scopus 로고    scopus 로고
    • Parkin-mediated lysine 63-linked polyubiquitination: A link to protein inclusions formation in Parkinson's and other conformational diseases?
    • 10.1016/j.neurobiolaging.2005.07.023. 16213628
    • Parkin-mediated lysine 63-linked polyubiquitination: A link to protein inclusions formation in Parkinson's and other conformational diseases? KL Lim VL Dawson TM Dawson, Neurobiol Aging 2006 27 524 529 10.1016/j.neurobiolaging. 2005.07.023 16213628
    • (2006) Neurobiol Aging , vol.27 , pp. 524-529
    • Lim, K.L.1    Dawson, V.L.2    Dawson, T.M.3
  • 54
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • 10.1074/jbc.M103378200. 11369780
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains. RM Hofmann CM Pickart, J Biol Chem 2001 276 27936 27943 10.1074/jbc.M103378200 11369780
    • (2001) J Biol Chem , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 55
    • 17144417404 scopus 로고    scopus 로고
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
    • 10.1016/j.jmb.2005.03.007. 15826667
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. Q Wang P Young KJ Walters, J Mol Biol 2005 348 727 739 10.1016/j.jmb.2005.03.007 15826667
    • (2005) J Mol Biol , vol.348 , pp. 727-739
    • Wang, Q.1    Young, P.2    Walters, K.J.3
  • 56
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • 10.1038/35056563. 11265246
    • Themes and variations on ubiquitylation. AM Weissman, Nat Rev Mol Cell Biol 2001 2 169 178 10.1038/35056563 11265246
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 58
    • 13244257325 scopus 로고    scopus 로고
    • Pathogenic mutations inactivate parkin by distinct mechanisms
    • 10.1111/j.1471-4159.2004.02854.x. 15606901
    • Pathogenic mutations inactivate parkin by distinct mechanisms. IH Henn JM Gostner P Lackner J Tatzelt KF Winklhofer, J Neurochem 2005 92 114 122 10.1111/j.1471-4159.2004.02854.x 15606901
    • (2005) J Neurochem , vol.92 , pp. 114-122
    • Henn, I.H.1    Gostner, J.M.2    Lackner, P.3    Tatzelt, J.4    Winklhofer, K.F.5
  • 59
    • 0038121031 scopus 로고    scopus 로고
    • The cellular protein level of parkin is regulated by its ubiquitin-like domain
    • 10.1074/jbc.C300051200. 12621021
    • The cellular protein level of parkin is regulated by its ubiquitin-like domain. N Finney F Walther PY Mantel D Stauffer G Rovelli KK Dev, J Biol Chem 2003 278 16054 16058 10.1074/jbc.C300051200 12621021
    • (2003) J Biol Chem , vol.278 , pp. 16054-16058
    • Finney, N.1    Walther, F.2    Mantel, P.Y.3    Stauffer, D.4    Rovelli, G.5    Dev, K.K.6
  • 61
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • 10.1038/nrc885. 12209156
    • Molecular basis of the VHL hereditary cancer syndrome. WG Kaelin Jr, Nat Rev Cancer 2002 2 673 682 10.1038/nrc885 12209156
    • (2002) Nat Rev Cancer , vol.2 , pp. 673-682
    • Kaelin, W.G.1    Jr2
  • 64
    • 0035839577 scopus 로고    scopus 로고
    • Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase
    • 10.1074/jbc.M103093200. 11384984
    • Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase. T Kamura D Burian Q Yan SL Schmidt WS Lane E Querido PE Branton A Shilatifard RC Conaway JW Conaway, J Biol Chem 2001 276 29748 29753 10.1074/jbc.M103093200 11384984
    • (2001) J Biol Chem , vol.276 , pp. 29748-29753
    • Kamura, T.1    Burian, D.2    Yan, Q.3    Schmidt, S.L.4    Lane, W.S.5    Querido, E.6    Branton, P.E.7    Shilatifard, A.8    Conaway, R.C.9    Conaway, J.W.10
  • 68
    • 1842441089 scopus 로고    scopus 로고
    • It's a double knock-out! the quaking mouse is a spontaneous deletion of parkin and parkin co-regulated gene (PACRG)
    • 10.1002/mds.20000. 14743368
    • It's a double knock-out! The quaking mouse is a spontaneous deletion of parkin and parkin co-regulated gene (PACRG). PJ Lockhart CA O'Farrell MJ Farrer, Mov Disord 2004 19 101 104 10.1002/mds.20000 14743368
    • (2004) Mov Disord , vol.19 , pp. 101-104
    • Lockhart, P.J.1    O'Farrell, C.A.2    Farrer, M.J.3
  • 69
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • 10.1242/dev.01095. 15073152
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Y Pesah T Pham H Burgess B Middlebrooks P Verstreken Y Zhou M Harding H Bellen G Mardon, Development 2004 131 2183 2194 10.1242/dev.01095 15073152
    • (2004) Development , vol.131 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5    Zhou, Y.6    Harding, M.7    Bellen, H.8    Mardon, G.9
  • 70
    • 32944469894 scopus 로고    scopus 로고
    • Bortezomib: Proteasome inhibition as an effective anticancer therapy
    • 10.1146/annurev.med.57.042905.122625. 16409135
    • Bortezomib: proteasome inhibition as an effective anticancer therapy. PG Richardson C Mitsiades T Hideshima KC Anderson, Annu Rev Med 2006 57 33 47 10.1146/annurev.med.57.042905.122625 16409135
    • (2006) Annu Rev Med , vol.57 , pp. 33-47
    • Richardson, P.G.1    Mitsiades, C.2    Hideshima, T.3    Anderson, K.C.4
  • 72
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • 10.1074/jbc.M204733200. 12052835
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. JS Isaacs YJ Jung EG Mimnaugh A Martinez F Cuttitta LM Neckers, J Biol Chem 2002 277 29936 29944 10.1074/jbc.M204733200 12052835
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 73
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • 10.1016/S1535-6108(03)00029-1. 12676580
    • Heat shock protein 90 as a molecular target for cancer therapeutics. JS Isaacs W Xu L Neckers, Cancer Cell 2003 3 213 217 10.1016/S1535-6108(03)00029-1 12676580
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 74
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • 10.1517/14712598.2.1.3. 11772336
    • HSP90 as a new therapeutic target for cancer therapy: the story unfolds. A Maloney P Workman, Expert Opin Biol Ther 2002 2 3 24 10.1517/14712598.2.1.3 11772336
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2


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