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Volumn 23, Issue 5, 2012, Pages 896-907

Design Principles of Protein Biosynthesis-Coupled Quality Control

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; MEMBRANE PROTEIN; MESSENGER RNA; POLYPEPTIDE;

EID: 84869065405     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2012.10.012     Document Type: Review
Times cited : (37)

References (123)
  • 1
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • Alberti S., Demand J., Esser C., Emmerich N., Schild H., Hohfeld J. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 2002, 277:45920-45927.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 2
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be-molecular chaperones in protein degradation
    • Arndt V., Rogon C., Höhfeld J. To be, or not to be-molecular chaperones in protein degradation. Cell. Mol. Life Sci. 2007, 64:2525-2541.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Höhfeld, J.3
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 4
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 1999, 19:4535-4545.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 6
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson M.H., Joazeiro C.A. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 2010, 467:470-473.
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 7
    • 41649116014 scopus 로고    scopus 로고
    • Derlin-1 facilitates the retro-translocation of cholera toxin
    • Bernardi K.M., Forster M.L., Lencer W.I., Tsai B. Derlin-1 facilitates the retro-translocation of cholera toxin. Mol. Biol. Cell 2008, 19:877-884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 877-884
    • Bernardi, K.M.1    Forster, M.L.2    Lencer, W.I.3    Tsai, B.4
  • 8
    • 60849096653 scopus 로고    scopus 로고
    • A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel
    • Berndt U., Oellerer S., Zhang Y., Johnson A.E., Rospert S. A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc. Natl. Acad. Sci. USA 2009, 106:1398-1403.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1398-1403
    • Berndt, U.1    Oellerer, S.2    Zhang, Y.3    Johnson, A.E.4    Rospert, S.5
  • 10
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A., Bukau B., Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 2010, 40:238-252.
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 11
    • 0030067832 scopus 로고    scopus 로고
    • Coding sequence-dependent ribosomal arrest at termination of translation
    • Cao J., Geballe A.P. Coding sequence-dependent ribosomal arrest at termination of translation. Mol. Cell. Biol. 1996, 16:603-608.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 603-608
    • Cao, J.1    Geballe, A.P.2
  • 13
    • 4344684215 scopus 로고    scopus 로고
    • Neuronal DnaJ proteins HSJ1a and HSJ1b: a role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system?
    • Chapple J.P., van der Spuy J., Poopalasundaram S., Cheetham M.E. Neuronal DnaJ proteins HSJ1a and HSJ1b: a role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system?. Biochem. Soc. Trans. 2004, 32:640-642.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 640-642
    • Chapple, J.P.1    van der Spuy, J.2    Poopalasundaram, S.3    Cheetham, M.E.4
  • 14
    • 0028099817 scopus 로고
    • Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b
    • Cheetham M.E., Jackson A.P., Anderton B.H. Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur. J. Biochem. 1994, 226:99-107.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 99-107
    • Cheetham, M.E.1    Jackson, A.P.2    Anderton, B.H.3
  • 15
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10:272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 17
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic V., Quan E.M., Weissman J.S. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006, 126:349-359.
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 19
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • Dimitrova L.N., Kuroha K., Tatematsu T., Inada T. Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J. Biol. Chem. 2009, 284:10343-10352.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 20
    • 79958766636 scopus 로고    scopus 로고
    • Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands
    • Dolan B.P., Bennink J.R., Yewdell J.W. Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands. Cell. Mol. Life Sci. 2011, 68:1481-1489.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1481-1489
    • Dolan, B.P.1    Bennink, J.R.2    Yewdell, J.W.3
  • 21
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
    • Doma M.K., Parker R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 2006, 440:561-564.
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.K.1    Parker, R.2
  • 22
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser C., Alberti S., Höhfeld J. Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim. Biophys. Acta 2004, 1695:171-188.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Höhfeld, J.3
  • 23
    • 46749104133 scopus 로고    scopus 로고
    • Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
    • Favaloro V., Spasic M., Schwappach B., Dobberstein B. Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J. Cell Sci. 2008, 121:1832-1840.
    • (2008) J. Cell Sci. , vol.121 , pp. 1832-1840
    • Favaloro, V.1    Spasic, M.2    Schwappach, B.3    Dobberstein, B.4
  • 24
    • 79956149556 scopus 로고    scopus 로고
    • SmpB as the handyman of tmRNA during trans-translation
    • Felden B., Gillet R. SmpB as the handyman of tmRNA during trans-translation. RNA Biol. 2011, 8:440-449.
    • (2011) RNA Biol. , vol.8 , pp. 440-449
    • Felden, B.1    Gillet, R.2
  • 25
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 28
    • 84858309380 scopus 로고    scopus 로고
    • Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome
    • Gagnon M.G., Seetharaman S.V., Bulkley D., Steitz T.A. Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science 2012, 335:1370-1372.
    • (2012) Science , vol.335 , pp. 1370-1372
    • Gagnon, M.G.1    Seetharaman, S.V.2    Bulkley, D.3    Steitz, T.A.4
  • 29
    • 84655163784 scopus 로고    scopus 로고
    • Emerging roles of molecular chaperones and co-chaperones in selective autophagy: focus on BAG proteins
    • Gamerdinger M., Carra S., Behl C. Emerging roles of molecular chaperones and co-chaperones in selective autophagy: focus on BAG proteins. J. Mol. Med. 2011, 89:1175-1182.
    • (2011) J. Mol. Med. , vol.89 , pp. 1175-1182
    • Gamerdinger, M.1    Carra, S.2    Behl, C.3
  • 30
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • Garrison J.L., Kunkel E.J., Hegde R.S., Taunton J. A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 2005, 436:285-289.
    • (2005) Nature , vol.436 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 32
    • 70350236409 scopus 로고    scopus 로고
    • Mechanisms for rescue of correctable folding defects in CFTRDelta F508
    • Grove D.E., Rosser M.F., Ren H.Y., Naren A.P., Cyr D.M. Mechanisms for rescue of correctable folding defects in CFTRDelta F508. Mol. Biol. Cell 2009, 20:4059-4069.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4059-4069
    • Grove, D.E.1    Rosser, M.F.2    Ren, H.Y.3    Naren, A.P.4    Cyr, D.M.5
  • 33
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M., Grassucci R.A., Frank J., Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 2004, 427:808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 34
    • 84865298998 scopus 로고    scopus 로고
    • Finding the will and the way of ERAD substrate retrotranslocation
    • Hampton R.Y., Sommer T. Finding the will and the way of ERAD substrate retrotranslocation. Curr. Opin. Cell Biol. 2012, 24:460-466.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 460-466
    • Hampton, R.Y.1    Sommer, T.2
  • 35
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • Hegde R.S., Keenan R.J. Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 2011, 12:787-798.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 787-798
    • Hegde, R.S.1    Keenan, R.J.2
  • 37
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E., Hegde R.S. Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 2011, 475:394-397.
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 38
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld J., Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 1997, 16:6209-6216.
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 39
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: molecular chaperones that may choose between folding and degradation
    • Höhfeld J., Cyr D.M., Patterson C. From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep. 2001, 2:885-890.
    • (2001) EMBO Rep. , vol.2 , pp. 885-890
    • Höhfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 40
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K. Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J. Biol. Chem. 2008, 283:20914-20924.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 42
    • 70249141564 scopus 로고    scopus 로고
    • Co-translational mRNA decay in Saccharomyces cerevisiae
    • Hu W., Sweet T.J., Chamnongpol S., Baker K.E., Coller J. Co-translational mRNA decay in Saccharomyces cerevisiae. Nature 2009, 461:225-229.
    • (2009) Nature , vol.461 , pp. 225-229
    • Hu, W.1    Sweet, T.J.2    Chamnongpol, S.3    Baker, K.E.4    Coller, J.5
  • 43
    • 46249121083 scopus 로고    scopus 로고
    • Protein trafficking to plastids: one theme, many variations
    • Inaba T., Schnell D.J. Protein trafficking to plastids: one theme, many variations. Biochem. J. 2008, 413:15-28.
    • (2008) Biochem. J. , vol.413 , pp. 15-28
    • Inaba, T.1    Schnell, D.J.2
  • 44
    • 33947159090 scopus 로고    scopus 로고
    • Translation of the poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast
    • Ito-Harashima S., Kuroha K., Tatematsu T., Inada T. Translation of the poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast. Genes Dev. 2007, 21:519-524.
    • (2007) Genes Dev. , vol.21 , pp. 519-524
    • Ito-Harashima, S.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 45
    • 0032855355 scopus 로고    scopus 로고
    • Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate
    • Iwamuro S., Saeki M., Kato S. Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate. J. Biochem. 1999, 126:48-53.
    • (1999) J. Biochem. , vol.126 , pp. 48-53
    • Iwamuro, S.1    Saeki, M.2    Kato, S.3
  • 49
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation
    • Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Höhfeld J., Patterson C. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 2001, 276:42938-42944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Höhfeld, J.6    Patterson, C.7
  • 51
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga H.H., Craig E.A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 2010, 11:579-592.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 52
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang S.W., Rane N.S., Kim S.J., Garrison J.L., Taunton J., Hegde R.S. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 2006, 127:999-1013.
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 53
    • 75649148551 scopus 로고    scopus 로고
    • Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis
    • Lee S., Lee D.W., Lee Y., Mayer U., Stierhof Y.D., Lee S., Jürgens G., Hwang I. Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis. Plant Cell 2009, 21:3984-4001.
    • (2009) Plant Cell , vol.21 , pp. 3984-4001
    • Lee, S.1    Lee, D.W.2    Lee, Y.3    Mayer, U.4    Stierhof, Y.D.5    Lee, S.6    Jürgens, G.7    Hwang, I.8
  • 54
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • Levine C.G., Mitra D., Sharma A., Smith C.L., Hegde R.S. The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 2005, 16:279-291.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5
  • 55
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki P., Clancy A., Schwappach B., High S. Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 2010, 123:2170-2178.
    • (2010) J. Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 56
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao S., Lin J., Do H., Johnson A.E. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 1997, 90:31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 57
    • 0009461277 scopus 로고
    • Interference of nonsense mutations with eukaryotic messenger RNA stability
    • Losson R., Lacroute F. Interference of nonsense mutations with eukaryotic messenger RNA stability. Proc. Natl. Acad. Sci. USA 1979, 76:5134-5137.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5134-5137
    • Losson, R.1    Lacroute, F.2
  • 58
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu J., Deutsch C. Electrostatics in the ribosomal tunnel modulate chain elongation rates. J. Mol. Biol. 2008, 384:73-86.
    • (2008) J. Mol. Biol. , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 59
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Lüders J., Demand J., Höhfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 2000, 275:4613-4617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Lüders, J.1    Demand, J.2    Höhfeld, J.3
  • 60
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: matrix and membrane protein biogenesis
    • Ma C., Agrawal G., Subramani S. Peroxisome assembly: matrix and membrane protein biogenesis. J. Cell Biol. 2011, 193:7-16.
    • (2011) J. Cell Biol. , vol.193 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 61
    • 0019733025 scopus 로고
    • Unstable beta-globin mRNA in mRNA-deficient beta o thalassemia
    • Maquat L.E., Kinniburgh A.J., Rachmilewitz E.A., Ross J. Unstable beta-globin mRNA in mRNA-deficient beta o thalassemia. Cell 1981, 27:543-553.
    • (1981) Cell , vol.27 , pp. 543-553
    • Maquat, L.E.1    Kinniburgh, A.J.2    Rachmilewitz, E.A.3    Ross, J.4
  • 62
    • 77955326776 scopus 로고    scopus 로고
    • The pioneer round of translation: features and functions
    • Maquat L.E., Tarn W.Y., Isken O. The pioneer round of translation: features and functions. Cell 2010, 142:368-374.
    • (2010) Cell , vol.142 , pp. 368-374
    • Maquat, L.E.1    Tarn, W.Y.2    Isken, O.3
  • 65
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • May T., Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell 2000, 12:53-64.
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 66
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 2005, 62:670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 67
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan A.J., Scott M.D., Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005, 121:739-748.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 69
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham G.C., Patterson C., Zhang W., Younger J.M., Cyr D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 2001, 3:100-105.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 70
    • 77957189436 scopus 로고    scopus 로고
    • ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum
    • Mehnert M., Sommer T., Jarosch E. ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 2010, 32:905-913.
    • (2010) Bioessays , vol.32 , pp. 905-913
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 72
    • 84879417885 scopus 로고    scopus 로고
    • C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
    • Muller P., Ruckova E., Halada P., Coates P.J., Hrstka R., Lane D.P., Vojtesek B. C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances. Oncogene 2012.
    • (2012) Oncogene
    • Muller, P.1    Ruckova, E.2    Halada, P.3    Coates, P.J.4    Hrstka, R.5    Lane, D.P.6    Vojtesek, B.7
  • 73
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S., Minami Y., Minami M., Chiba T., Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2001, 2:1133-1138.
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 74
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund A.M., Pellegrino M.W., Fiorese C.J., Baker B.M., Haynes C.M. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 2012, 337:587-590.
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 75
    • 84858321922 scopus 로고    scopus 로고
    • Decoding in the absence of a codon by tmRNA and SmpB in the ribosome
    • Neubauer C., Gillet R., Kelley A.C., Ramakrishnan V. Decoding in the absence of a codon by tmRNA and SmpB in the ribosome. Science 2012, 335:1366-1369.
    • (2012) Science , vol.335 , pp. 1366-1369
    • Neubauer, C.1    Gillet, R.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 76
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003, 299:1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 79
    • 79955626576 scopus 로고    scopus 로고
    • Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
    • Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J. 2011, 30:1804-1817.
    • (2011) EMBO J. , vol.30 , pp. 1804-1817
    • Pisareva, V.P.1    Skabkin, M.A.2    Hellen, C.U.3    Pestova, T.V.4    Pisarev, A.V.5
  • 80
    • 33646593202 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64
    • Qbadou S., Becker T., Mirus O., Tews I., Soll J., Schleiff E. The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J. 2006, 25:1836-1847.
    • (2006) EMBO J. , vol.25 , pp. 1836-1847
    • Qbadou, S.1    Becker, T.2    Mirus, O.3    Tews, I.4    Soll, J.5    Schleiff, E.6
  • 81
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • Rane N.S., Yonkovich J.L., Hegde R.S. Protection from cytosolic prion protein toxicity by modulation of protein translocation. EMBO J. 2004, 23:4550-4559.
    • (2004) EMBO J. , vol.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 82
    • 77949568225 scopus 로고    scopus 로고
    • DNA polymerase proofreading: Multiple roles maintain genome stability
    • Reha-Krantz L.J. DNA polymerase proofreading: Multiple roles maintain genome stability. Biochim. Biophys. Acta 2010, 1804:1049-1063.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1049-1063
    • Reha-Krantz, L.J.1
  • 85
    • 84864022349 scopus 로고    scopus 로고
    • Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase
    • Rubenstein E.M., Kreft S.G., Greenblatt W., Swanson R., Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J. Cell Biol. 2012, 197:761-773.
    • (2012) J. Cell Biol. , vol.197 , pp. 761-773
    • Rubenstein, E.M.1    Kreft, S.G.2    Greenblatt, W.3    Swanson, R.4    Hochstrasser, M.5
  • 86
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 1997, 16:1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 87
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato B.K., Schulz D., Do P.H., Hampton R.Y. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol. Cell 2009, 34:212-222.
    • (2009) Mol. Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 88
    • 0032571366 scopus 로고    scopus 로고
    • Cotranslational ubiquitination of cystic fibrosis transmembrane conductance regulator in vitro
    • Sato S., Ward C.L., Kopito R.R. Cotranslational ubiquitination of cystic fibrosis transmembrane conductance regulator in vitro. J. Biol. Chem. 1998, 273:7189-7192.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7189-7192
    • Sato, S.1    Ward, C.L.2    Kopito, R.R.3
  • 89
    • 79952304472 scopus 로고    scopus 로고
    • Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs
    • Schaeffer D., van Hoof A. Different nuclease requirements for exosome-mediated degradation of normal and nonstop mRNAs. Proc. Natl. Acad. Sci. USA 2011, 108:2366-2371.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2366-2371
    • Schaeffer, D.1    van Hoof, A.2
  • 90
    • 37549040609 scopus 로고    scopus 로고
    • The tetratricopeptide repeats of receptors involved in protein translocation across membranes
    • Schlegel T., Mirus O., von Haeseler A., Schleiff E. The tetratricopeptide repeats of receptors involved in protein translocation across membranes. Mol. Biol. Evol. 2007, 24:2763-2774.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 2763-2774
    • Schlegel, T.1    Mirus, O.2    von Haeseler, A.3    Schleiff, E.4
  • 92
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • Shan S.O., Walter P. Co-translational protein targeting by the signal recognition particle. FEBS Lett. 2005, 579:921-926.
    • (2005) FEBS Lett. , vol.579 , pp. 921-926
    • Shan, S.O.1    Walter, P.2
  • 93
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao S., Hegde R.S. Membrane protein insertion at the endoplasmic reticulum. Annu. Rev. Cell Dev. Biol. 2011, 10:25-56.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.10 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 94
  • 95
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • Shoemaker C.J., Eyler D.E., Green R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 2010, 330:369-372.
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 96
    • 0029042422 scopus 로고
    • BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
    • Simons J.F., Ferro-Novick S., Rose M.D., Helenius A. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol. 1995, 130:41-49.
    • (1995) J. Cell Biol. , vol.130 , pp. 41-49
    • Simons, J.F.1    Ferro-Novick, S.2    Rose, M.D.3    Helenius, A.4
  • 97
    • 77955257617 scopus 로고    scopus 로고
    • CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates
    • Stankiewicz M., Nikolay R., Rybin V., Mayer M.P. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates. FEBS J. 2010, 277:3353-3367.
    • (2010) FEBS J. , vol.277 , pp. 3353-3367
    • Stankiewicz, M.1    Nikolay, R.2    Rybin, V.3    Mayer, M.P.4
  • 98
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • Stefanovic S., Hegde R.S. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 2007, 128:1147-1159.
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 99
    • 70549111391 scopus 로고    scopus 로고
    • RNA polymerase fidelity and transcriptional proofreading
    • Sydow J.F., Cramer P. RNA polymerase fidelity and transcriptional proofreading. Curr. Opin. Struct. Biol. 2009, 19:732-739.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 732-739
    • Sydow, J.F.1    Cramer, P.2
  • 101
    • 0033534588 scopus 로고    scopus 로고
    • An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators
    • Takayama S., Xie Z., Reed J.C. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J. Biol. Chem. 1999, 274:781-786.
    • (1999) J. Biol. Chem. , vol.274 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 102
    • 80053352130 scopus 로고    scopus 로고
    • Mitochondrial quality control by the ubiquitin-proteasome system
    • Taylor E.B., Rutter J. Mitochondrial quality control by the ubiquitin-proteasome system. Biochem. Soc. Trans. 2011, 39:1509-1513.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1509-1513
    • Taylor, E.B.1    Rutter, J.2
  • 103
    • 84863615329 scopus 로고    scopus 로고
    • A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast
    • Theodoraki M.A., Nillegoda N.B., Saini J., Caplan A.J. A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast. J. Biol. Chem. 2012, 287:23911-23922.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23911-23922
    • Theodoraki, M.A.1    Nillegoda, N.B.2    Saini, J.3    Caplan, A.J.4
  • 104
    • 84861456756 scopus 로고    scopus 로고
    • Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3' end of aberrant mRNA
    • Tsuboi T., Kuroha K., Kudo K., Makino S., Inoue E., Kashima I., Inada T. Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3' end of aberrant mRNA. Mol. Cell 2012, 46:518-529.
    • (2012) Mol. Cell , vol.46 , pp. 518-529
    • Tsuboi, T.1    Kuroha, K.2    Kudo, K.3    Makino, S.4    Inoue, E.5    Kashima, I.6    Inada, T.7
  • 105
    • 29344464782 scopus 로고    scopus 로고
    • Protein synthesis upon acute nutrient restriction relies on proteasome function
    • Vabulas R.M., Hartl F.U. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 2005, 310:1960-1963.
    • (2005) Science , vol.310 , pp. 1960-1963
    • Vabulas, R.M.1    Hartl, F.U.2
  • 106
    • 80755140606 scopus 로고    scopus 로고
    • A brief survey of mRNA surveillance
    • van Hoof A., Wagner E.J. A brief survey of mRNA surveillance. Trends Biochem. Sci. 2011, 36:585-592.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 585-592
    • van Hoof, A.1    Wagner, E.J.2
  • 107
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof A., Frischmeyer P.A., Dietz H.C., Parker R. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 2002, 295:2262-2264.
    • (2002) Science , vol.295 , pp. 2262-2264
    • van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 108
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011, 10.1002/pro.666.
    • (2011) Protein Sci.
    • Varshavsky, A.1
  • 109
    • 77954604855 scopus 로고    scopus 로고
    • J domain co-chaperone specificity defines the role of BiP during protein translocation
    • Vembar S.S., Jonikas M.C., Hendershot L.M., Weissman J.S., Brodsky J.L. J domain co-chaperone specificity defines the role of BiP during protein translocation. J. Biol. Chem. 2010, 285:22484-22494.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22484-22494
    • Vembar, S.S.1    Jonikas, M.C.2    Hendershot, L.M.3    Weissman, J.S.4    Brodsky, J.L.5
  • 110
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang F., Brown E.C., Mak G., Zhuang J., Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 2010, 40:159-171.
    • (2010) Mol. Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 111
    • 0037166282 scopus 로고    scopus 로고
    • A quality control pathway that down-regulates aberrant T-cell receptor (TCR) transcripts by a mechanism requiring UPF2 and translation
    • Wang J., Vock V.M., Li S., Olivas O.R., Wilkinson M.F. A quality control pathway that down-regulates aberrant T-cell receptor (TCR) transcripts by a mechanism requiring UPF2 and translation. J. Biol. Chem. 2002, 277:18489-18493.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18489-18493
    • Wang, J.1    Vock, V.M.2    Li, S.3    Olivas, O.R.4    Wilkinson, M.F.5
  • 112
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff B., Chapple J.P., van der Spuy J., Höhfeld J., Cheetham M.E. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 2005, 15:1058-1064.
    • (2005) Curr. Biol. , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3    Höhfeld, J.4    Cheetham, M.E.5
  • 113
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 1999, 286:1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 114
    • 79953106751 scopus 로고    scopus 로고
    • The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
    • Wilson D.N., Beckmann R. The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling. Curr. Opin. Struct. Biol. 2011, 21:274-282.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 274-282
    • Wilson, D.N.1    Beckmann, R.2
  • 115
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler J., Tyedmers J., Bukau B., Mogk A. Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 2012, 179:152-160.
    • (2012) J. Struct. Biol. , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 116
    • 33745934813 scopus 로고    scopus 로고
    • Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest
    • Winnefeld M., Grewenig A., Schnölzer M., Spring H., Knoch T.A., Gan E.C., Rommelaere J., Cziepluch C. Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest. Exp. Cell Res. 2006, 312:2500-2514.
    • (2006) Exp. Cell Res. , vol.312 , pp. 2500-2514
    • Winnefeld, M.1    Grewenig, A.2    Schnölzer, M.3    Spring, H.4    Knoch, T.A.5    Gan, E.C.6    Rommelaere, J.7    Cziepluch, C.8
  • 117
    • 84855892823 scopus 로고    scopus 로고
    • Quality control in aminoacyl-tRNA synthesis its role in translational fidelity
    • Yadavalli S.S., Ibba M. Quality control in aminoacyl-tRNA synthesis its role in translational fidelity. Adv. Protein Chem. Struct. Biol. 2012, 86:1-43.
    • (2012) Adv. Protein Chem. Struct. Biol. , vol.86 , pp. 1-43
    • Yadavalli, S.S.1    Ibba, M.2
  • 118
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J.C., Hoogenraad N.J., Hartl F.U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 2003, 112:41-50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 119
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTRDeltaF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • Younger J.M., Ren H.Y., Chen L., Fan C.Y., Fields A., Patterson C., Cyr D.M. A foldable CFTRDeltaF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J. Cell Biol. 2004, 167:1075-1085.
    • (2004) J. Cell Biol. , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 120
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: lessons from protein synthesis
    • Zaher H.S., Green R. Fidelity at the molecular level: lessons from protein synthesis. Cell 2009, 136:746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 121
    • 81855227611 scopus 로고    scopus 로고
    • Motility and segregation of Hsp104-associated protein aggregates in budding yeast
    • Zhou C., Slaughter B.D., Unruh J.R., Eldakak A., Rubinstein B., Li R. Motility and segregation of Hsp104-associated protein aggregates in budding yeast. Cell 2011, 147:1186-1196.
    • (2011) Cell , vol.147 , pp. 1186-1196
    • Zhou, C.1    Slaughter, B.D.2    Unruh, J.R.3    Eldakak, A.4    Rubinstein, B.5    Li, R.6
  • 122
    • 0032544634 scopus 로고    scopus 로고
    • Regulated Co-translational ubiquitination of apolipoprotein B100. A new paradigm for proteasomal degradation of a secretory protein
    • Zhou M., Fisher E.A., Ginsberg H.N. Regulated Co-translational ubiquitination of apolipoprotein B100. A new paradigm for proteasomal degradation of a secretory protein. J. Biol. Chem. 1998, 273:24649-24653.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24649-24653
    • Zhou, M.1    Fisher, E.A.2    Ginsberg, H.N.3
  • 123
    • 0031923127 scopus 로고    scopus 로고
    • The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum
    • Zimmermann R. The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum. Biol. Chem. 1998, 379:275-282.
    • (1998) Biol. Chem. , vol.379 , pp. 275-282
    • Zimmermann, R.1


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