메뉴 건너뛰기




Volumn 11, Issue 2, 2016, Pages

Subcellular fractionation analysis of the extraction of ubiquitinated polytopic membrane substrate during ER-associated degradation

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; MEMBRANE PROTEIN; PROTEIN CDC48; PROTEIN STE6; UNCLASSIFIED DRUG; ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; CDC48 PROTEIN; DNA BINDING PROTEIN; DSK2 PROTEIN, S CEREVISIAE; RAD23 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; STE6 PROTEIN, S CEREVISIAE; UBIQUITIN;

EID: 84959431880     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0148327     Document Type: Article
Times cited : (17)

References (80)
  • 1
    • 79851515002 scopus 로고    scopus 로고
    • Protein dislocation from the ER
    • 20599420 Epub 2010/07/06
    • Bagola K, Mehnert M, Jarosch E, Sommer T. Protein dislocation from the ER. Biochim Biophys Acta. 2011; 1808(3):925-36. Epub 2010/07/06. doi: 10.1016/j.bbamem.2010.06.025 PMID: 20599420.
    • (2011) Biochim Biophys Acta. , vol.1808 , Issue.3 , pp. 925-936
    • Bagola, K.1    Mehnert, M.2    Jarosch, E.3    Sommer, T.4
  • 2
    • 77952555674 scopus 로고    scopus 로고
    • ERAD substrate recognition in budding yeast
    • 20178855 Epub 2010/02/25
    • Xie W, Ng DT. ERAD substrate recognition in budding yeast. Semin Cell Dev Biol. 2010; 21(5):533-9. Epub 2010/02/25. doi: 10.1016/j.semcdb.2010.02.007 PMID: 20178855.
    • (2010) Semin Cell Dev Biol. , vol.21 , Issue.5 , pp. 533-539
    • Xie, W.1    Ng, D.T.2
  • 3
    • 84865298998 scopus 로고    scopus 로고
    • Finding the will and the way of ERAD substrate retrotranslocation
    • 22854296 Epub 2012/08/03
    • Hampton RY, Sommer T. Finding the will and the way of ERAD substrate retrotranslocation. Current opinion in cell biology. 2012; 24(4):460-6. Epub 2012/08/03. doi: 10.1016/j.ceb.2012.05.010 PMID: 22854296.
    • (2012) Current Opinion in Cell Biology. , vol.24 , Issue.4 , pp. 460-466
    • Hampton, R.Y.1    Sommer, T.2
  • 4
    • 84855188325 scopus 로고    scopus 로고
    • The Cdc48 machine in endoplasmic reticulum associated protein degradation
    • 21945179 Epub 2011/09/29
    • Wolf DH, Stolz A. The Cdc48 machine in endoplasmic reticulum associated protein degradation. Biochim Biophys Acta. 2012; 1823(1):117-24. Epub 2011/09/29. doi: 10.1016/j.bbamcr.2011.09.002 PMID: 21945179.
    • (2012) Biochim Biophys Acta. , vol.1823 , Issue.1 , pp. 117-124
    • Wolf, D.H.1    Stolz, A.2
  • 5
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • 23217703 Epub 2012/12/12; PubMed Central PMCID: PMC3521611
    • Brodsky JL. Cleaning up: ER-associated degradation to the rescue. Cell. 2012; 151(6):1163-7. Epub 2012/12/12. doi: 10.1016/j.cell.2012.11.012 PMID: 23217703; PubMed Central PMCID: PMC3521611.
    • (2012) Cell. , vol.151 , Issue.6 , pp. 1163-1167
    • Brodsky, J.L.1
  • 6
    • 84948567055 scopus 로고    scopus 로고
    • Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: Lessons from yeast
    • 26362128 Epub 2015/09/13
    • Nakatsukasa K, Okumura F, Kamura T. Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast. Critical reviews in biochemistry and molecular biology. 2015; 50 (6):489-502. Epub 2015/09/13. doi: 10.3109/10409238.2015.1081869 PMID: 26362128.
    • (2015) Critical Reviews in Biochemistry and Molecular Biology. , vol.50 , Issue.6 , pp. 489-502
    • Nakatsukasa, K.1    Okumura, F.2    Kamura, T.3
  • 7
    • 34548202772 scopus 로고    scopus 로고
    • Visiting the ER: The endoplasmic reticulum as a target for therapeutics in traffic related diseases
    • 17681635 Epub 2007/08/08
    • Aridor M. Visiting the ER: the endoplasmic reticulum as a target for therapeutics in traffic related diseases. Adv Drug Deliv Rev. 2007; 59(8):759-81. Epub 2007/08/08. doi: 10.1016/j.addr.2007.06.002 PMID: 17681635.
    • (2007) Adv Drug Deliv Rev. , vol.59 , Issue.8 , pp. 759-781
    • Aridor, M.1
  • 8
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • 22535891 Epub 2012/ 04/27
    • Guerriero CJ, Brodsky JL. The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiol Rev. 2012; 92(2):537-76. Epub 2012/ 04/27. doi: 10.1152/physrev.00027.2011 PMID: 22535891.
    • (2012) Physiol Rev. , vol.92 , Issue.2 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 9
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • 15078901 Epub 2004/04/14; PubMed Central PMCID: PMC2172089
    • Vashist S, Ng DT. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. The Journal of cell biology. 2004; 165(1):41-52. Epub 2004/04/14. doi: 10.1083/jcb.200309132 PMID: 15078901; PubMed Central PMCID: PMC2172089.
    • (2004) The Journal of Cell Biology. , vol.165 , Issue.1 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 10
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • 16873066 Epub 2006/07/29
    • Carvalho P, Goder V, Rapoport TA. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell. 2006; 126(2):361-73. Epub 2006/07/29. doi: 10.1016/j.cell.2006. 05.043 PMID: 16873066.
    • (2006) Cell. , vol.126 , Issue.2 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 11
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • 19394298 Epub 2009/04/28; PubMed Central PMCID: PMC2710143
    • Sato BK, Schulz D, Do PH, Hampton RY. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Molecular cell. 2009; 34(2):212-22. Epub 2009/04/28. doi: 10.1016/j.molcel.2009.03.010 PMID: 19394298; PubMed Central PMCID: PMC2710143.
    • (2009) Molecular Cell. , vol.34 , Issue.2 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 12
    • 84864022349 scopus 로고    scopus 로고
    • Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase
    • 22689655 Epub 2012/06/13; PubMed Central PMCID: PMC3373407
    • Rubenstein EM, Kreft SG, Greenblatt W, Swanson R, Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. The Journal of cell biology. 2012; 197(6):761-73. Epub 2012/06/13. doi: 10.1083/jcb.201203061 PMID: 22689655; PubMed Central PMCID: PMC3373407.
    • (2012) The Journal of Cell Biology. , vol.197 , Issue.6 , pp. 761-773
    • Rubenstein, E.M.1    Kreft, S.G.2    Greenblatt, W.3    Swanson, R.4    Hochstrasser, M.5
  • 13
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • 11641273 Epub 2001/10/20; PubMed Central PMCID: PMC312819
    • Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 2001; 15(20):2660-74. Epub 2001/10/20. doi: 10.1101/gad.933301 PMID: 11641273; PubMed Central PMCID: PMC312819.
    • (2001) Genes Dev. , vol.15 , Issue.20 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 14
    • 84980051722 scopus 로고    scopus 로고
    • The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
    • 25918226 Epub 2015/04/29; PubMed Central PMCID: PMC4411271
    • Habeck G, Ebner FA, Shimada-Kreft H, Kreft SG. The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron. The Journal of cell biology. 2015; 209(2):261-73. Epub 2015/04/29. doi: 10.1083/jcb.201408088 PMID: 25918226; PubMed Central PMCID: PMC4411271.
    • (2015) The Journal of Cell Biology. , vol.209 , Issue.2 , pp. 261-273
    • Habeck, G.1    Ebner, F.A.2    Shimada-Kreft, H.3    Kreft, S.G.4
  • 15
    • 34548496285 scopus 로고    scopus 로고
    • Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal
    • 17615300 Epub 2007/07/07; PubMed Central PMCID: PMC1951769
    • Pagant S, Kung L, Dorrington M, Lee MC, Miller EA. Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Molecular biology of the cell. 2007; 18(9):3398-413. Epub 2007/07/07. doi: 10.1091/mbc.E07-01-0046 PMID: 17615300; PubMed Central PMCID: PMC1951769.
    • (2007) Molecular Biology of the Cell. , vol.18 , Issue.9 , pp. 3398-3413
    • Pagant, S.1    Kung, L.2    Dorrington, M.3    Lee, M.C.4    Miller, E.A.5
  • 16
    • 33847375937 scopus 로고    scopus 로고
    • Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD
    • 17325204 Epub 2007/02/28; PubMed Central PMCID: PMC2064020
    • Kota J, Gilstring CF, Ljungdahl PO. Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD. The Journal of cell biology. 2007; 176(5):617-28. Epub 2007/02/28 doi: 10.1083/jcb.200612100 PMID: 17325204; PubMed Central PMCID: PMC2064020.
    • (2007) The Journal of Cell Biology. , vol.176 , Issue.5 , pp. 617-628
    • Kota, J.1    Gilstring, C.F.2    Ljungdahl, P.O.3
  • 17
    • 84909962081 scopus 로고    scopus 로고
    • Quality control of inner nuclear membrane proteins by the Asi complex
    • 25236469 Epub 2014/09/23
    • Foresti O, Rodriguez-Vaello V, Funaya C, Carvalho P. Quality control of inner nuclear membrane proteins by the Asi complex. Science. 2014. Epub 2014/09/23. doi: 10.1126/science.1255638 PMID: 25236469.
    • (2014) Science
    • Foresti, O.1    Rodriguez-Vaello, V.2    Funaya, C.3    Carvalho, P.4
  • 18
    • 84922218720 scopus 로고    scopus 로고
    • Protein quality control at the inner nuclear membrane
    • 25519137 Epub 2014/12/19
    • Khmelinskii A, Blaszczak E, Pantazopoulou M, Fischer B, Omnus DJ, Le Dez G, et al. Protein quality control at the inner nuclear membrane. Nature. 2014; 516(7531):410-3. Epub 2014/12/19. doi: 10.1038/nature14096 PMID: 25519137.
    • (2014) Nature , vol.516 , Issue.7531 , pp. 410-413
    • Khmelinskii, A.1    Blaszczak, E.2    Pantazopoulou, M.3    Fischer, B.4    Omnus, D.J.5    Le Dez, G.6
  • 19
    • 84896270715 scopus 로고    scopus 로고
    • Quality control: ER-associated degradation: Protein quality control and beyond
    • 24637321 Epub 2014/03/19; PubMed Central PMCID: PMC3998802
    • Ruggiano A, Foresti O, Carvalho P. Quality control: ER-associated degradation: protein quality control and beyond. The Journal of cell biology. 2014; 204(6):869-79. Epub 2014/03/19. doi: 10.1083/jcb. 201312042 PMID: 24637321; PubMed Central PMCID: PMC3998802.
    • (2014) The Journal of Cell Biology. , vol.204 , Issue.6 , pp. 869-879
    • Ruggiano, A.1    Foresti, O.2    Carvalho, P.3
  • 20
    • 77952860536 scopus 로고    scopus 로고
    • Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase
    • 20482385 Epub 2010/05/21; PubMed Central PMCID: PMC2937355
    • Jo Y, Debose-Boyd RA. Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase. Critical reviews in biochemistry and molecular biology. 2010; 45(3):185-98. Epub 2010/05/21. doi: 10.3109/10409238.2010.485605 PMID: 20482385; PubMed Central PMCID: PMC2937355.
    • (2010) Critical Reviews in Biochemistry and Molecular Biology. , vol.45 , Issue.3 , pp. 185-198
    • Jo, Y.1    Debose-Boyd, R.A.2
  • 21
    • 64749083589 scopus 로고    scopus 로고
    • Protein quality control as a strategy for cellular regulation: Lessons from ubiquitin-mediated regulation of the sterol pathway
    • 19243134 Epub 2009/02/27
    • Hampton RY, Garza RM. Protein quality control as a strategy for cellular regulation: lessons from ubiquitin-mediated regulation of the sterol pathway. Chem Rev. 2009; 109(4):1561-74. Epub 2009/02/27. doi: 10.1021/cr800544v PMID: 19243134.
    • (2009) Chem Rev. , vol.109 , Issue.4 , pp. 1561-1574
    • Hampton, R.Y.1    Garza, R.M.2
  • 22
    • 84880707873 scopus 로고    scopus 로고
    • Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4
    • 23898401 Epub 2013/07/31; PubMed Central PMCID: PMC3721249
    • Foresti O, Ruggiano A, Hannibal-Bach HK, Ejsing CS, Carvalho P. Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4. eLife. 2013; 2: e00953. Epub 2013/07/31. doi: 10.7554/eLife.00953 PMID: 23898401; PubMed Central PMCID: PMC3721249.
    • (2013) ELife. , vol.2
    • Foresti, O.1    Ruggiano, A.2    Hannibal-Bach, H.K.3    Ejsing, C.S.4    Carvalho, P.5
  • 23
    • 84908072286 scopus 로고    scopus 로고
    • Key steps in ERAD of luminal ER proteins reconstituted with purified components
    • 25215493 Epub 2014/09/13; PubMed Central PMCID: PMC4163015
    • Stein A, Ruggiano A, Carvalho P, Rapoport TA. Key Steps in ERAD of Luminal ER Proteins Reconstituted with Purified Components. Cell. 2014; 158(6):1375-88. Epub 2014/09/13. doi: 10.1016/j.cell. 2014.07.050 PMID: 25215493; PubMed Central PMCID: PMC4163015.
    • (2014) Cell , vol.158 , Issue.6 , pp. 1375-1388
    • Stein, A.1    Ruggiano, A.2    Carvalho, P.3    Rapoport, T.A.4
  • 24
    • 0035875921 scopus 로고    scopus 로고
    • Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
    • 11406589 Epub 2001/06/19; PubMed Central PMCID: PMC150204
    • Walter J, Urban J, Volkwein C, Sommer T. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. EMBO J. 2001; 20(12):3124-31. Epub 2001/06/19. doi: 10.1093/emboj/20. 12.3124 PMID: 11406589; PubMed Central PMCID: PMC150204.
    • (2001) EMBO J. , vol.20 , Issue.12 , pp. 3124-3131
    • Walter, J.1    Urban, J.2    Volkwein, C.3    Sommer, T.4
  • 25
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • 16845392 Epub 2006/07/18
    • Piwko W, Jentsch S. Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site. Nat Struct Mol Biol. 2006; 13(8):691-7. Epub 2006/07/18. doi: 10.1038/nsmb1122 PMID: 16845392.
    • (2006) Nat Struct Mol Biol. , vol.13 , Issue.8 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 26
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ERtransmembrane protein
    • 9628862 Epub 1998/06/17; PubMed Central PMCID: PMC1170663
    • Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ERtransmembrane protein. EMBO J. 1998; 17(12):3251-7. Epub 1998/06/17. doi: 10.1093/emboj/17.12. 3251 PMID: 9628862; PubMed Central PMCID: PMC1170663.
    • (1998) EMBO J. , vol.17 , Issue.12 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 27
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • 18191224 Epub 2008/01/15; PubMed Central PMCID: PMC2219389
    • Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell. 2008; 132(1):101-12. Epub 2008/01/15. doi: 10.1016/j.cell. 2007.11.023 PMID: 18191224; PubMed Central PMCID: PMC2219389.
    • (2008) Cell. , vol.132 , Issue.1 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 28
    • 67649371174 scopus 로고    scopus 로고
    • In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase
    • 19324879 Epub 2009/03/28; PubMed Central PMCID: PMC2685653
    • Garza RM, Sato BK, Hampton RY. In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase. The Journal of biological chemistry. 2009; 284(22):14710-22. Epub 2009/03/28. doi: 10.1074/jbc.M809607200 PMID: 19324879; PubMed Central PMCID: PMC2685653.
    • (2009) The Journal of Biological Chemistry. , vol.284 , Issue.22 , pp. 14710-14722
    • Garza, R.M.1    Sato, B.K.2    Hampton, R.Y.3
  • 29
    • 77953530388 scopus 로고    scopus 로고
    • Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets
    • 20406816 Epub 2010/04/22; PubMed Central PMCID: PMC2885207
    • Hartman IZ, Liu P, Zehmer JK, Luby-Phelps K, Jo Y, Anderson RG, et al. Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets. The Journal of biological chemistry. 2010; 285(25):19288-98. Epub 2010/04/22. doi: 10.1074/jbc.M110.134213 PMID: 20406816; PubMed Central PMCID: PMC2885207.
    • (2010) The Journal of Biological Chemistry. , vol.285 , Issue.25 , pp. 19288-19298
    • Hartman, I.Z.1    Liu, P.2    Zehmer, J.K.3    Luby-Phelps, K.4    Jo, Y.5    Anderson, R.G.6
  • 30
    • 79953687692 scopus 로고    scopus 로고
    • Enzymatic blockade of the ubiquitin-proteasome pathway
    • 21468303 Epub 2011/04/07; PubMed Central PMCID: PMC3066133
    • Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, et al. Enzymatic blockade of the ubiquitin-proteasome pathway. PLoS Biol. 2011; 8(3):e1000605. Epub 2011/04/07. doi: 10.1371/ journal.pbio.1000605 PMID: 21468303; PubMed Central PMCID: PMC3066133.
    • (2011) PLoS Biol. , vol.8 , Issue.3
    • Ernst, R.1    Claessen, J.H.2    Mueller, B.3    Sanyal, S.4    Spooner, E.5    Van Der Veen, A.G.6
  • 31
    • 84884308471 scopus 로고    scopus 로고
    • Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation
    • 23988329 Epub 2013/08/31; PubMed Central PMCID: PMC3780849
    • Stolz A, Besser S, Hottmann H, Wolf DH. Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation. Proceedings of the National Academy of Sciences of the United States of America. 2013; 110(38):15271-6. Epub 2013/08/31. doi: 10.1073/pnas. 1304928110 PMID: 23988329; PubMed Central PMCID: PMC3780849.
    • (2013) Proceedings of the National Academy of Sciences of the United States of America. , vol.110 , Issue.38 , pp. 15271-15276
    • Stolz, A.1    Besser, S.2    Hottmann, H.3    Wolf, D.H.4
  • 32
    • 84873355211 scopus 로고    scopus 로고
    • Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes
    • 23223569 Epub 2012/12/12; PubMed Central PMCID: PMC3564538
    • Jo Y, Hartman IZ, DeBose-Boyd RA. Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes. Molecular biology of the cell. 2013; 24(3):169-83. Epub 2012/12/12. doi: 10.1091/mbc. E12-07-0564 PMID: 23223569; PubMed Central PMCID: PMC3564538.
    • (2013) Molecular Biology of the Cell. , vol.24 , Issue.3 , pp. 169-183
    • Jo, Y.1    Hartman, I.Z.2    DeBose-Boyd, R.A.3
  • 33
    • 67749116062 scopus 로고    scopus 로고
    • Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation
    • 19458199 Epub 2009/05/22. PubMed Central PMCID: PMC2710830
    • Leichner GS, Avner R, Harats D, Roitelman J. Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation. Molecular biology of the cell. 2009; 20(14):3330-41. Epub 2009/05/22. doi: 10.1091/mbc.E08-09-0953 PMID: 19458199; PubMed Central PMCID: PMC2710830.
    • (2009) Molecular Biology of the Cell. , vol.20 , Issue.14 , pp. 3330-3341
    • Leichner, G.S.1    Avner, R.2    Harats, D.3    Roitelman, J.4
  • 34
    • 84887107942 scopus 로고    scopus 로고
    • Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from membranes of permeabilized cells
    • 24025715 Epub 2013/09/13 PubMed Central PMCID: PMC3814148
    • Elsabrouty R, Jo Y, Dinh TT, DeBose-Boyd RA. Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from membranes of permeabilized cells. Molecular biology of the cell. 2013; 24(21):3300-8. Epub 2013/09/13. doi: 10.1091/mbc.E13-03-0157 PMID: 24025715; PubMed Central PMCID: PMC3814148.
    • (2013) Molecular Biology of the Cell. , vol.24 , Issue.21 , pp. 3300-3308
    • Elsabrouty, R.1    Jo, Y.2    Dinh, T.T.3    DeBose-Boyd, R.A.4
  • 35
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • 11740563 Epub 2001/12/12
    • Ye Y, Meyer HH, Rapoport TA. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 2001; 414(6864):652-6. Epub 2001/12/12. doi: 10.1038/414652a PMID: 11740563.
    • (2001) Nature , vol.414 , Issue.6864 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 36
    • 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
    • 12847084 Epub 2003/07/09; PubMed Central PMCID: PMC2172719
    • Ye Y, Meyer HH, Rapoport TA. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. The Journal of cell biology. 2003; 162(1):71-84. Epub 2003/07/09. doi: 10.1083/jcb.200302169 PMID: 12847084; PubMed Central PMCID: PMC2172719.
    • (2003) The Journal of Cell Biology. , vol.162 , Issue.1 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 37
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • 11813000 Epub 2002/01/29
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, Wolf DH, et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nature cell biology. 2002; 4(2):134-9. Epub 2002/01/29. doi: 10.1038/ncb746 PMID: 11813000.
    • (2002) Nature Cell Biology. , vol.4 , Issue.2 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5    Wolf, D.H.6
  • 38
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • 16179952 Epub 2005/09/24
    • Schuberth C, Buchberger A. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nature cell biology. 2005; 7(10):999-1006. Epub 2005/09/24. doi: 10.1038/ncb1299 PMID: 16179952.
    • (2005) Nature Cell Biology. , vol.7 , Issue.10 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 39
    • 27144535945 scopus 로고    scopus 로고
    • Ubx2 links the Cdc48 complex to ER-associated protein degradation
    • 16179953 Epub 2005/09/24
    • Neuber O, Jarosch E, Volkwein C, Walter J, Sommer T. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nature cell biology. 2005; 7(10):993-8. Epub 2005/09/24. doi: 10.1038/ ncb1298 PMID: 16179953.
    • (2005) Nature Cell Biology. , vol.7 , Issue.10 , pp. 993-998
    • Neuber, O.1    Jarosch, E.2    Volkwein, C.3    Walter, J.4    Sommer, T.5
  • 40
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • 21074049 Epub 2010/11/16; PubMed Central PMCID: PMC3026631
    • Carvalho P, Stanley AM, Rapoport TA. Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell. 2010; 143(4):579-91. Epub 2010/11/16. doi: 10.1016/j.cell.2010.10.028 PMID: 21074049; PubMed Central PMCID: PMC3026631.
    • (2010) Cell. , vol.143 , Issue.4 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 41
    • 33646552435 scopus 로고    scopus 로고
    • The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
    • 16619026 Epub 2006/04/19; PubMed Central PMCID: PMC1456945
    • Gauss R, Sommer T, Jarosch E. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. EMBO J. 2006; 25(9):1827-35. Epub 2006/04/19. doi: 10.1038/sj.emboj.7601088 PMID: 16619026; PubMed Central PMCID: PMC1456945.
    • (2006) EMBO J. , vol.25 , Issue.9 , pp. 1827-1835
    • Gauss, R.1    Sommer, T.2    Jarosch, E.3
  • 42
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • 17653186 Epub 2007/07/27
    • Ploegh HL. A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature. 2007; 448(7152):435-8. Epub 2007/07/27. doi: 10.1038/nature06004 PMID: 17653186.
    • (2007) Nature , vol.448 , Issue.7152 , pp. 435-438
    • Ploegh, H.L.1
  • 43
    • 80054801259 scopus 로고    scopus 로고
    • Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control
    • 21857022 Epub 2011/08/23; PubMed Central PMCID: PMC3199505
    • Klemm EJ, Spooner E, Ploegh HL. Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control. The Journal of biological chemistry. 2011; 286(43):37602-14. Epub 2011/08/23. doi: 10.1074/jbc.M111.284794 PMID: 21857022; PubMed Central PMCID: PMC3199505.
    • (2011) The Journal of Biological Chemistry. , vol.286 , Issue.43 , pp. 37602-37614
    • Klemm, E.J.1    Spooner, E.2    Ploegh, H.L.3
  • 44
    • 0031690373 scopus 로고    scopus 로고
    • Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae
    • 9763443 Epub 1998/10/08; PubMed Central PMCID: PMC25553
    • Loayza D, Tam A, Schmidt WK, Michaelis S. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Molecular biology of the cell. 1998; 9(10):2767-84. Epub 1998/10/08. PMID: 9763443; PubMed Central PMCID: PMC25553.
    • (1998) Molecular Biology of the Cell. , vol.9 , Issue.10 , pp. 2767-2784
    • Loayza, D.1    Tam, A.2    Schmidt, W.K.3    Michaelis, S.4
  • 45
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • 11673477 Epub 2001/10/24; PubMed Central PMCID: PMC2150856
    • Vashist S, Kim W, Belden WJ, Spear ED, Barlowe C, Ng DT. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. The Journal of cell biology. 2001; 155(3):355-68. Epub 2001/10/24. doi: 10.1083/jcb.200106123 PMID: 11673477; PubMed Central PMCID: PMC2150856.
    • (2001) The Journal of Cell Biology. , vol.155 , Issue.3 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 46
    • 84878730933 scopus 로고    scopus 로고
    • A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation
    • 23536702 S1-8 Epub 2013/03/29; PubMed Central PMCID: PMC3667728
    • Nakatsukasa K, Brodsky JL, Kamura T. A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation. Molecular biology of the cell. 2013; 24(11):1765-75, S1-8. Epub 2013/03/29. doi: 10.1091/mbc.E12-12-0907 PMID: 23536702; PubMed Central PMCID: PMC3667728.
    • (2013) Molecular Biology of the Cell. , vol.24 , Issue.11 , pp. 1765-1775
    • Nakatsukasa, K.1    Brodsky, J.L.2    Kamura, T.3
  • 48
    • 84937161989 scopus 로고    scopus 로고
    • The Ubiquitin Ligase SCF(Ucc1) Acts as a Metabolic Switch for the Glyoxylate Cycle
    • 25982115 Epub 2015/05/20
    • Nakatsukasa K, Nishimura T, Byrne SD, Okamoto M, Takahashi-Nakaguchi A, Chibana H, et al. The Ubiquitin Ligase SCF(Ucc1) Acts as a Metabolic Switch for the Glyoxylate Cycle. Molecular cell. 2015; 59(1):22-34. Epub 2015/05/20. doi: 10.1016/j.molcel.2015.04.013 PMID: 25982115.
    • (2015) Molecular Cell. , vol.59 , Issue.1 , pp. 22-34
    • Nakatsukasa, K.1    Nishimura, T.2    Byrne, S.D.3    Okamoto, M.4    Takahashi-Nakaguchi, A.5    Chibana, H.6
  • 49
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • 11359923 Epub 2001/05/22; PubMed Central PMCID: PMC34585
    • Zhang Y, Nijbroek G, Sullivan ML, McCracken AA, Watkins SC, Michaelis S, et al. Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Molecular biology of the cell. 2001; 12(5):1303-14. Epub 2001/05/22. PMID: 11359923; PubMed Central PMCID: PMC34585.
    • (2001) Molecular Biology of the Cell. , vol.12 , Issue.5 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3    McCracken, A.A.4    Watkins, S.C.5    Michaelis, S.6
  • 50
    • 57749116223 scopus 로고    scopus 로고
    • Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
    • 18812321 Epub 2008/09/25 PubMed Central PMCID: PMC2583311
    • Metzger MB, Maurer MJ, Dancy BM, Michaelis S. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. The Journal of biological chemistry. 2008; 283 (47):32302-16. Epub 2008/09/25. doi: 10.1074/jbc.M806424200 PMID: 18812321; PubMed Central PMCID: PMC2583311.
    • (2008) The Journal of Biological Chemistry. , vol.283 , Issue.47 , pp. 32302-32316
    • Metzger, M.B.1    Maurer, M.J.2    Dancy, B.M.3    Michaelis, S.4
  • 51
    • 80051998695 scopus 로고    scopus 로고
    • The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23
    • 21807993 Epub 2011/08/03; PubMed Central PMCID: PMC3158229
    • Baek GH, Kim I, Rao H. The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23. Proceedings of the National Academy of Sciences of the United States of America. 2011; 108(33):13558-63. Epub 2011/08/03. doi: 10.1073/pnas.1104051108 PMID: 21807993; PubMed Central PMCID: PMC3158229.
    • (2011) Proceedings of the National Academy of Sciences of the United States of America. , vol.108 , Issue.33 , pp. 13558-13563
    • Baek, G.H.1    Kim, I.2    Rao, H.3
  • 52
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • 15167887 Epub 2004/05/29; PubMed Central PMCID: PMC1299090
    • Medicherla B, Kostova Z, Schaefer A, Wolf DH. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 2004; 5(7):692-7. Epub 2004/05/29. doi: 10.1038/sj.embor.7400164 PMID: 15167887; PubMed Central PMCID: PMC1299090.
    • (2004) EMBO Rep. , vol.5 , Issue.7 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 53
    • 80051540452 scopus 로고    scopus 로고
    • Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation
    • 21693705 Epub 2011/06/23; PubMed Central PMCID: PMC3151032
    • Olzmann JA, Kopito RR. Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation. The Journal of biological chemistry. 2011; 286(32):27872-4. Epub 2011/06/23. doi: 10.1074/jbc.C111.266452 PMID: 21693705; PubMed Central PMCID: PMC3151032.
    • (2011) The Journal of Biological Chemistry. , vol.286 , Issue.32 , pp. 27872-27874
    • Olzmann, J.A.1    Kopito, R.R.2
  • 54
    • 71449099158 scopus 로고    scopus 로고
    • Sterol and diacylglycerol acyltransferase deficiency triggers fatty acid-mediated cell death
    • 19690167 Epub 2009/08/20; PubMed Central PMCID: PMC2781500
    • Garbarino J, Padamsee M, Wilcox L, Oelkers PM, D'Ambrosio D, Ruggles KV, et al. Sterol and diacylglycerol acyltransferase deficiency triggers fatty acid-mediated cell death. The Journal of biological chemistry. 2009; 284(45):30994-1005. Epub 2009/08/20. doi: 10.1074/jbc.M109.050443 PMID: 19690167; PubMed Central PMCID: PMC2781500.
    • (2009) The Journal of Biological Chemistry. , vol.284 , Issue.45 , pp. 30994-31005
    • Garbarino, J.1    Padamsee, M.2    Wilcox, L.3    Oelkers, P.M.4    D'Ambrosio, D.5    Ruggles, K.V.6
  • 55
    • 71449102613 scopus 로고    scopus 로고
    • Good fat, essential cellular requirements for triacylglycerol synthesis to maintain membrane homeostasis in yeast
    • 19608739 Epub 2009/07/18; PubMed Central PMCID: PMC2781499
    • Petschnigg J, Wolinski H, Kolb D, Zellnig G, Kurat CF, Natter K, et al. Good fat, essential cellular requirements for triacylglycerol synthesis to maintain membrane homeostasis in yeast. The Journal of biological chemistry. 2009; 284(45):30981-93. Epub 2009/07/18. doi: 10.1074/jbc.M109.024752 PMID: 19608739; PubMed Central PMCID: PMC2781499.
    • (2009) The Journal of Biological Chemistry. , vol.284 , Issue.45 , pp. 30981-30993
    • Petschnigg, J.1    Wolinski, H.2    Kolb, D.3    Zellnig, G.4    Kurat, C.F.5    Natter, K.6
  • 56
    • 3843131947 scopus 로고    scopus 로고
    • A yeast strain lacking lipid particles bears a defect in ergosterol formation
    • 15155725 Epub 2004/05/25
    • Sorger D, Athenstaedt K, Hrastnik C, Daum G. A yeast strain lacking lipid particles bears a defect in ergosterol formation. The Journal of biological chemistry. 2004; 279(30):31190-6. Epub 2004/05/25. doi: 10.1074/jbc.M403251200 PMID: 15155725.
    • (2004) The Journal of Biological Chemistry. , vol.279 , Issue.30 , pp. 31190-31196
    • Sorger, D.1    Athenstaedt, K.2    Hrastnik, C.3    Daum, G.4
  • 57
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • 8045256 Epub 1994/07/15; PubMed Central PMCID: PMC395222
    • Kolling R, Hollenberg CP. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 1994; 13(14):3261-71. Epub 1994/07/15. PMID: 8045256; PubMed Central PMCID: PMC395222.
    • (1994) EMBO J. , vol.13 , Issue.14 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 58
    • 40949101672 scopus 로고    scopus 로고
    • Overview of subcellular fractionation procedures for the yeast Saccharomyces cerevisiae
    • 18228359 [et al].;Chapter 3:Unit 3.7. Epub 2008/01/30
    • Rieder SE, Emr SD. Overview of subcellular fractionation procedures for the yeast Saccharomyces cerevisiae. Current protocols in cell biology / editorial board, Juan S Bonifacino [et al]. 2001;Chapter 3:Unit 3.7. Epub 2008/01/30. doi: 10.1002/0471143030.cb0307s07 PMID: 18228359.
    • (2001) Current Protocols in Cell Biology / Editorial Board, Juan S Bonifacino
    • Rieder, S.E.1    Emr, S.D.2
  • 59
    • 0038010388 scopus 로고    scopus 로고
    • Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation
    • 12711700 Epub 2003/04/25
    • Palmer EA, Kruse KB, Fewell SW, Buchanan SM, Brodsky JL, McCracken AA. Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation. Journal of cell science. 2003; 116(Pt 11):2361-73. Epub 2003/04/25. doi: 10.1242/jcs.00439 PMID: 12711700.
    • (2003) Journal of Cell Science. , vol.116 , pp. 2361-2373
    • Palmer, E.A.1    Kruse, K.B.2    Fewell, S.W.3    Buchanan, S.M.4    Brodsky, J.L.5    McCracken, A.A.6
  • 60
    • 27644554700 scopus 로고    scopus 로고
    • A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes
    • 16251969 Epub 2005/10/28
    • Hirano Y, Hendil KB, Yashiroda H, Iemura S, Nagane R, Hioki Y, et al. A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature. 2005; 437(7063):1381-5. Epub 2005/10/28. doi: 10.1038/nature04106 PMID: 16251969.
    • (2005) Nature , vol.437 , Issue.7063 , pp. 1381-1385
    • Hirano, Y.1    Hendil, K.B.2    Yashiroda, H.3    Iemura, S.4    Nagane, R.5    Hioki, Y.6
  • 61
    • 33845681479 scopus 로고    scopus 로고
    • Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes
    • 17189198 Epub 2006/12/26
    • Hirano Y, Hayashi H, Iemura S, Hendil KB, Niwa S, Kishimoto T, et al. Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Molecular cell. 2006; 24(6):977-84. Epub 2006/12/26. doi: 10.1016/j.molcel.2006.11.015 PMID: 17189198.
    • (2006) Molecular Cell. , vol.24 , Issue.6 , pp. 977-984
    • Hirano, Y.1    Hayashi, H.2    Iemura, S.3    Hendil, K.B.4    Niwa, S.5    Kishimoto, T.6
  • 62
    • 34247617365 scopus 로고    scopus 로고
    • Beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint
    • 17431397 Epub 2007/04/14; PubMed Central PMCID: PMC1864979
    • Li X, Kusmierczyk AR, Wong P, Emili A, Hochstrasser M. beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 2007; 26(9):2339-49. Epub 2007/04/14. doi: 10.1038/sj.emboj.7601681 PMID: 17431397; PubMed Central PMCID: PMC1864979.
    • (2007) EMBO J. , vol.26 , Issue.9 , pp. 2339-2349
    • Li, X.1    Kusmierczyk, A.R.2    Wong, P.3    Emili, A.4    Hochstrasser, M.5
  • 63
    • 34948897990 scopus 로고    scopus 로고
    • ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly
    • 17634286 Epub 2007/07/20; PubMed Central PMCID: PMC1995736
    • Scott CM, Kruse KB, Schmidt BZ, Perlmutter DH, McCracken AA, Brodsky JL. ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly. Molecular biology of the cell. 2007; 18(10):3776-87. Epub 2007/07/20. doi: 10.1091/mbc.E07-01-0034 PMID: 17634286; PubMed Central PMCID: PMC1995736.
    • (2007) Molecular Biology of the Cell. , vol.18 , Issue.10 , pp. 3776-3787
    • Scott, C.M.1    Kruse, K.B.2    Schmidt, B.Z.3    Perlmutter, D.H.4    McCracken, A.A.5    Brodsky, J.L.6
  • 64
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • 12353037 Epub 2002/09/28
    • Yao T, Cohen RE. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature. 2002; 419(6905):403-7. Epub 2002/09/28. doi: 10.1038/nature01071 PMID: 12353037.
    • (2002) Nature , vol.419 , Issue.6905 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 65
    • 0347087494 scopus 로고    scopus 로고
    • Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome
    • 14581483 Epub 2003/10/29
    • Guterman A, Glickman MH. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. The Journal of biological chemistry. 2004; 279(3):1729-38. Epub 2003/10/29. doi: 10.1074/jbc.M307050200 PMID: 14581483.
    • (2004) The Journal of Biological Chemistry. , vol.279 , Issue.3 , pp. 1729-1738
    • Guterman, A.1    Glickman, M.H.2
  • 66
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation
    • 17018280 Epub 2006/10/05
    • Hanna J, Hathaway NA, Tone Y, Crosas B, Elsasser S, Kirkpatrick DS, et al. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell. 2006; 127(1):99-111. Epub 2006/10/05. doi: 10.1016/j.cell.2006.07.038 PMID: 17018280.
    • (2006) Cell. , vol.127 , Issue.1 , pp. 99-111
    • Hanna, J.1    Hathaway, N.A.2    Tone, Y.3    Crosas, B.4    Elsasser, S.5    Kirkpatrick, D.S.6
  • 67
    • 0742270608 scopus 로고    scopus 로고
    • A striking quality control subcompartment in Saccharomyces cerevisiae: The endoplasmic reticulum-associated compartment
    • 14668485 Epub 2003/12/12; PubMed Central PMCID: PMC329403
    • Huyer G, Longsworth GL, Mason DL, Mallampalli MP, McCaffery JM, Wright RL, et al. A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment. Molecular biology of the cell. 2004; 15(2):908-21. Epub 2003/12/12. doi: 10.1091/mbc.E03-07-0546 PMID: 14668485; PubMed Central PMCID: PMC329403.
    • (2004) Molecular Biology of the Cell. , vol.15 , Issue.2 , pp. 908-921
    • Huyer, G.1    Longsworth, G.L.2    Mason, D.L.3    Mallampalli, M.P.4    McCaffery, J.M.5    Wright, R.L.6
  • 68
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • 18756251 Epub 2008/08/30; PubMed Central PMCID: PMC2746971
    • Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature. 2008; 454(7208):1088-95. Epub 2008/08/30. doi: 10.1038/nature07195 PMID: 18756251; PubMed Central PMCID: PMC2746971.
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 69
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • 24036477 Epub 2013/09/17; PubMed Central PMCID: PMC4121856
    • Escusa-Toret S, Vonk WI, Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nature cell biology. 2013; 15(10):1231-43. Epub 2013/09/17. doi: 10.1038/ncb2838 PMID: 24036477; PubMed Central PMCID: PMC4121856.
    • (2013) Nature Cell Biology. , vol.15 , Issue.10 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 70
    • 33947301163 scopus 로고    scopus 로고
    • Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum
    • 17264153 Epub 2007/02/01
    • Ng W, Sergeyenko T, Zeng N, Brown JD, Romisch K. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. Journal of cell science. 2007; 120(Pt 4):682-91. Epub 2007/02/01. doi: 10.1242/jcs.03351 PMID: 17264153.
    • (2007) Journal of Cell Science. , vol.120 , pp. 682-691
    • Ng, W.1    Sergeyenko, T.2    Zeng, N.3    Brown, J.D.4    Romisch, K.5
  • 71
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • 21636303 Epub 2011/06/04; PubMed Central PMCID: PMC3138499
    • Wang Q, Liu Y, Soetandyo N, Baek K, Hegde R, Ye Y. A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Molecular cell. 2011; 42(6):758-70. Epub 2011/06/04. doi: 10.1016/j.molcel.2011.05.010 PMID: 21636303; PubMed Central PMCID: PMC3138499.
    • (2011) Molecular Cell. , vol.42 , Issue.6 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 72
    • 84871682623 scopus 로고    scopus 로고
    • SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation
    • 23246001 Epub 2012/12/19; PubMed Central PMCID: PMC3534891
    • Xu Y, Cai M, Yang Y, Huang L, Ye Y. SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation. Cell reports. 2012; 2(6):1633-44. Epub 2012/12/19. doi: 10.1016/j.celrep.2012.11.010 PMID: 23246001; PubMed Central PMCID: PMC3534891.
    • (2012) Cell Reports. , vol.2 , Issue.6 , pp. 1633-1644
    • Xu, Y.1    Cai, M.2    Yang, Y.3    Huang, L.4    Ye, Y.5
  • 73
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • 21743475 Epub 2011/ 07/12; PubMed Central PMCID: PMC3150218
    • Hessa T, Sharma A, Mariappan M, Eshleman HD, Gutierrez E, Hegde RS. Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature. 2011; 475(7356):394-7. Epub 2011/ 07/12. doi: 10.1038/nature10181 PMID: 21743475; PubMed Central PMCID: PMC3150218.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 74
    • 84878191743 scopus 로고    scopus 로고
    • BAG6/BAT3: Emerging roles in quality control for nascent polypeptides
    • 23275523 Epub 2013/01/01
    • Kawahara H, Minami R, Yokota N. BAG6/BAT3: emerging roles in quality control for nascent polypeptides. Journal of biochemistry. 2013; 153(2):147-60. Epub 2013/01/01. doi: 10.1093/jb/mvs149 PMID: 23275523.
    • (2013) Journal of Biochemistry. , vol.153 , Issue.2 , pp. 147-160
    • Kawahara, H.1    Minami, R.2    Yokota, N.3
  • 75
    • 84869065405 scopus 로고    scopus 로고
    • Design principles of protein biosynthesis-coupled quality control
    • 23153486 Epub 2012/11/17
    • Rodrigo-Brenni MC, Hegde RS. Design principles of protein biosynthesis-coupled quality control. Developmental cell. 2012; 23(5):896-907. Epub 2012/11/17. doi: 10.1016/j.devcel.2012.10.012 PMID: 23153486.
    • (2012) Developmental Cell. , vol.23 , Issue.5 , pp. 896-907
    • Rodrigo-Brenni, M.C.1    Hegde, R.S.2
  • 76
    • 84913593958 scopus 로고    scopus 로고
    • SGTA regulates the cytosolic quality control of hydrophobic substrates
    • 25179605 Epub 2014/09/03; PubMed Central PMCID: PMC4215715
    • Wunderley L, Leznicki P, Payapilly A, High S. SGTA regulates the cytosolic quality control of hydrophobic substrates. Journal of cell science. 2014; 127(Pt 21):4728-39. Epub 2014/09/03. doi: 10.1242/jcs. 155648 PMID: 25179605; PubMed Central PMCID: PMC4215715.
    • (2014) Journal of Cell Science. , vol.127 , pp. 4728-4739
    • Wunderley, L.1    Leznicki, P.2    Payapilly, A.3    High, S.4
  • 77
    • 80053210242 scopus 로고    scopus 로고
    • A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex
    • 21832041 Epub 2011/08/13; PubMed Central PMCID: PMC3190793
    • Chartron JW, Gonzalez GM, ClemonsWMJr. A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. The Journal of biological chemistry. 2011; 286 (39):34325-34. Epub 2011/08/13. doi: 10.1074/jbc.M111.277798 PMID: 21832041; PubMed Central PMCID: PMC3190793.
    • (2011) The Journal of Biological Chemistry. , vol.286 , Issue.39 , pp. 34325-34334
    • Chartron, J.W.1    Gonzalez, G.M.2    Clemons, W.M.3
  • 78
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • 20850366 Epub 2010/09/21; PubMed Central PMCID: PMC3652556
    • Wang F, Brown EC, Mak G, Zhuang J, Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Molecular cell. 2010; 40(1):159-71. Epub 2010/09/21. doi: 10.1016/j.molcel.2010.08.038 PMID: 20850366; PubMed Central PMCID: PMC3652556.
    • (2010) Molecular Cell. , vol.40 , Issue.1 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 79
    • 77951209587 scopus 로고    scopus 로고
    • Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1
    • 20106980 Epub 2010/01/29
    • Chang YW, Chuang YC, Ho YC, Cheng MY, Sun YJ, Hsiao CD, et al. Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1. The Journal of biological chemistry. 2010; 285 (13):9962-70. Epub 2010/01/29. doi: 10.1074/jbc.M109.087098 PMID: 20106980; PubMed Central PMCID: PMC2843242.
    • (2010) The Journal of Biological Chemistry. , vol.285 , Issue.13 , pp. 9962-9970
    • Chang, Y.W.1    Chuang, Y.C.2    Ho, Y.C.3    Cheng, M.Y.4    Sun, Y.J.5    Hsiao, C.D.6
  • 80
    • 79959440698 scopus 로고    scopus 로고
    • Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
    • 21619481 Epub 2011/05/31
    • Kohl C, Tessarz P, von der Malsburg K, Zahn R, Bukau B, Mogk A. Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. Biological chemistry. 2011; 392(7):601-8. Epub 2011/05/31. doi: 10.1515/BC.2011.066 PMID: 21619481.
    • (2011) Biological Chemistry. , vol.392 , Issue.7 , pp. 601-608
    • Kohl, C.1    Tessarz, P.2    Von Der Malsburg, K.3    Zahn, R.4    Bukau, B.5    Mogk, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.