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Volumn 71, Issue 17, 2014, Pages 3311-3325

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

Author keywords

Disaggregase; GroEL; Holdase; Hsp110; Hsp40; Hsp70; Polypeptide unfoldase; Translocase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; ALPHA SYNUCLEIN; CHAPERONE; CHAPERONIN 60; GLUCOSE 6 PHOSPHATE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN B2B3; HEAT SHOCK PROTEIN B5; HEAT SHOCK TRANSCRIPTION FACTOR 1; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN CLPB; PROTEIN DNAJ; PROTEIN DNAK; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84906096557     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-014-1627-y     Document Type: Review
Times cited : (95)

References (164)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181(4096):223-230
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • doi:10.1038/nature02261
    • Dobson CM (2003) Protein folding and misfolding. Nature 426(6968):884-890. doi:10.1038/nature02261
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 84875212796 scopus 로고    scopus 로고
    • Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates
    • doi:10.1016/j.jmb.2012.12.025
    • Natalello A, Mattoo RU, Priya S, Sharma SK, Goloubinoff P, Doglia SM (2013) Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. J Mol Biol 425(7):1158-1171. doi:10.1016/j.jmb.2012.12.025
    • (2013) J Mol Biol , vol.425 , Issue.7 , pp. 1158-1171
    • Natalello, A.1    Mattoo, R.U.2    Priya, S.3    Sharma, S.K.4    Goloubinoff, P.5    Doglia, S.M.6
  • 4
    • 34147102801 scopus 로고    scopus 로고
    • Chaperones and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging
    • DOI 10.1385/JMN:30:3:249, PII JMN303249
    • Hinault MP, Ben-Zvi A, Goloubinoff P (2006) Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. J Mol Neurosci 30(3):249-265. doi:10.1385/JMN:30:3:249 (Pubitemid 46568344)
    • (2006) Journal of Molecular Neuroscience , vol.30 , Issue.3 , pp. 249-265
    • Hinault, M.-P.1    Ben-Zvi, A.2    Goloubinoff, P.3
  • 5
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • doi:10.1038/nature10317
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475(7356):324-332. doi:10.1038/nature10317
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 6
    • 40949124274 scopus 로고    scopus 로고
    • GroEL stimulates protein folding through forced unfolding
    • DOI 10.1038/nsmb.1394, PII NSMB1394
    • Lin Z, Madan D, Rye HS (2008) GroEL stimulates protein folding through forced unfolding. Nat Struct Mol Biol 15(3):303-311. doi:10.1038/nsmb.1394 (Pubitemid 351654048)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.3 , pp. 303-311
    • Lin, Z.1    Madan, D.2    Rye, H.S.3
  • 7
    • 4944221602 scopus 로고    scopus 로고
    • Expansion and compression of a protein folding intermediate by GroEL
    • DOI 10.1016/j.molcel.2004.09.003, PII S1097276504005210
    • Lin Z, Rye HS (2004) Expansion and compression of a protein folding intermediate by GroEL. Mol Cell 16(1):23-34. doi:10.1016/j.molcel.2004.09.003 (Pubitemid 39330149)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 23-34
    • Lin, Z.1    Rye, H.S.2
  • 8
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • (pii:0014-5793(90)81469-5)
    • Rassow J, Hartl FU, Guiard B, Pfanner N, Neupert W (1990) Polypeptides traverse the mitochondrial envelope in an extended state. FEBS Lett 275(1-2):190-194 (pii:0014-5793(90)81469-5)
    • (1990) FEBS Lett , vol.275 , Issue.1-2 , pp. 190-194
    • Rassow, J.1    Hartl, F.U.2    Guiard, B.3    Pfanner, N.4    Neupert, W.5
  • 9
    • 0033617338 scopus 로고    scopus 로고
    • The structure of precursor proteins during import into mitochondria
    • Schwartz MP, Huang S, Matouschek A (1999) The structure of precursor proteins during import into mitochondria. J Biol Chem 274(18):12759-12764
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12759-12764
    • Schwartz, M.P.1    Huang, S.2    Matouschek, A.3
  • 10
    • 41149089882 scopus 로고    scopus 로고
    • Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding
    • DOI 10.1016/j.cell.2008.01.048, PII S0092867408002134
    • Sharma S, Chakraborty K, Muller BK, Astola N, Tang YC, Lamb DC, Hayer-Hartl M, Hartl FU (2008) Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 133(1):142-153. doi:10.1016/j.cell.2008. 01.048 (Pubitemid 351442991)
    • (2008) Cell , vol.133 , Issue.1 , pp. 142-153
    • Sharma, S.1    Chakraborty, K.2    Muller, B.K.3    Astola, N.4    Tang, Y.-C.5    Lamb, D.C.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 11
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • DOI 10.1126/science.284.5415.822
    • Shtilerman M, Lorimer GH, Englander SW (1999) Chaperonin function: folding by forced unfolding. Science 284(5415):822-825 (Pubitemid 29291351)
    • (1999) Science , vol.284 , Issue.5415 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 12
    • 84876926597 scopus 로고    scopus 로고
    • GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP
    • doi:10.1073/pnas.1219867110
    • Priya S, Sharma SK, Sood V, Mattoo RU, Finka A, Azem A, De Los Rios P, Goloubinoff P (2013) GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP. Proc Natl Acad Sci USA 110(18):7199-7204. doi:10.1073/pnas.1219867110
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.18 , pp. 7199-7204
    • Priya, S.1    Sharma, S.K.2    Sood, V.3    Mattoo, R.U.4    Finka, A.5    Azem, A.6    De Los Rios, P.7    Goloubinoff, P.8
  • 13
    • 78649309029 scopus 로고    scopus 로고
    • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
    • doi:10.1038/Nchembio.455
    • Sharma SK, De Los Rios P, Christen P, Lustig A, Goloubinoff P (2010) The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat Chem Biol 6(12):914-920. doi:10.1038/Nchembio.455
    • (2010) Nat Chem Biol , vol.6 , Issue.12 , pp. 914-920
    • Sharma, S.K.1    De Los Rios, P.2    Christen, P.3    Lustig, A.4    Goloubinoff, P.5
  • 14
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • doi:10.1016/j.tem.2006.06.003
    • Picard D (2006) Chaperoning steroid hormone action. Trends Endocrinol Metab 17(6):229-235. doi:10.1016/j.tem.2006.06.003
    • (2006) Trends Endocrinol Metab , vol.17 , Issue.6 , pp. 229-235
    • Picard, D.1
  • 15
    • 84934440933 scopus 로고    scopus 로고
    • Chaperone regulation of the heat shock protein response
    • doi:10.1007/978-0-387-39975-1-9
    • Voellmy R, Boellmann F (2007) Chaperone regulation of the heat shock protein response. Adv Exp Med Biol 594:89-99. doi:10.1007/978-0-387-39975-1-9
    • (2007) Adv Exp Med Biol , vol.594 , pp. 89-99
    • Voellmy, R.1    Boellmann, F.2
  • 16
    • 34548292474 scopus 로고    scopus 로고
    • Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome
    • DOI 10.1097/01.CCM.0000278915.78030.74, PII 0000324620070900000017
    • Weiss YG, Bromberg Z, Raj N, Raphael J, Goloubinoff P, Ben-Neriah Y, Deutschman CS (2007) Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Crit Care Med 35(9):2128-2138 (Pubitemid 47326450)
    • (2007) Critical Care Medicine , vol.35 , Issue.9 , pp. 2128-2138
    • Weiss, Y.G.1    Bromberg, Z.2    Raj, N.3    Raphael, J.4    Goloubinoff, P.5    Ben-Neriah, Y.6    Deutschman, C.S.7
  • 17
    • 0035400710 scopus 로고    scopus 로고
    • Molecular chaperones and the regulation of neurotransmitter exocytosis
    • pii:S0006-2952(01)00648-7
    • Zinsmaier KE, Bronk P (2001) Molecular chaperones and the regulation of neurotransmitter exocytosis. Biochem Pharmacol 62(1):1-11 (pii:S0006-2952(01) 00648-7)
    • (2001) Biochem Pharmacol , vol.62 , Issue.1 , pp. 1-11
    • Zinsmaier, K.E.1    Bronk, P.2
  • 18
    • 19644387113 scopus 로고    scopus 로고
    • Evidence for regulation of ER/Golgi SNARE complex formation by hsc70 chaperones
    • DOI 10.1016/j.ejcb.2004.12.028, PII S0171933505000208
    • Joglekar AP, Hay JC (2005) Evidence for regulation of ER/Golgi SNARE complex formation by hsc70 chaperones. Eur J Cell Biol 84(5):529-542. doi:10.1016/j.ejcb.2004.12.028 (Pubitemid 40740425)
    • (2005) European Journal of Cell Biology , vol.84 , Issue.5 , pp. 529-542
    • Joglekar, A.P.1    Hay, J.C.2
  • 19
    • 78650505099 scopus 로고    scopus 로고
    • CSPalpha promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity
    • doi:10.1038/ncb2131
    • Sharma M, Burre J, Sudhof TC (2011) CSPalpha promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity. Nat Cell Biol 13(1):30-39. doi:10.1038/ncb2131
    • (2011) Nat Cell Biol , vol.13 , Issue.1 , pp. 30-39
    • Sharma, M.1    Burre, J.2    Sudhof, T.C.3
  • 20
    • 33750996168 scopus 로고    scopus 로고
    • Keep the traffic moving: Mechanism of the Hsp70 motor
    • DOI 10.1111/j.1600-0854.2006.00497.x
    • Sousa R, Lafer EM (2006) Keep the traffic moving: mechanism of the Hsp70 motor. Traffic 7(12):1596-1603. doi:10.1111/j.1600-0854.2006.00497.x (Pubitemid 44742362)
    • (2006) Traffic , vol.7 , Issue.12 , pp. 1596-1603
    • Sousa, R.1    Lafer, E.M.2
  • 21
    • 79951681576 scopus 로고    scopus 로고
    • Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
    • doi:10.1007/s12192-010-0216-8
    • Finka A, Mattoo RU, Goloubinoff P (2011) Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 16(1):15-31. doi:10.1007/s12192-010-0216-8
    • (2011) Cell Stress Chaperones , vol.16 , Issue.1 , pp. 15-31
    • Finka, A.1    Mattoo, R.U.2    Goloubinoff, P.3
  • 22
    • 84863533791 scopus 로고    scopus 로고
    • The stress of protein misfolding: From single cells to multicellular organisms
    • doi:10.1101/cshperspect.a009704
    • Gidalevitz T, Prahlad V, Morimoto RI (2011) The stress of protein misfolding: from single cells to multicellular organisms. Cold Spring Harb Perspect Biol 3(6). doi:10.1101/cshperspect.a009704
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.6
    • Gidalevitz, T.1    Prahlad, V.2    Morimoto, R.I.3
  • 23
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • doi:10.1038/nrm2993
    • Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11(11):777-788. doi:10.1038/nrm2993
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 24
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • doi:10.1016/j.molcel.2010.10.006
    • Richter K, Haslbeck M, Buchner J (2010) The heat shock response: life on the verge of death. Mol Cell 40(2):253-266. doi:10.1016/j.molcel.2010.10.006
    • (2010) Mol Cell , vol.40 , Issue.2 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 27
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • doi:10.1007/s12192-013-0413-3
    • Finka A, Goloubinoff P (2013) Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress Chaperones 18(5):591-605. doi:10.1007/s12192-013-0413-3
    • (2013) Cell Stress Chaperones , vol.18 , Issue.5 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 29
    • 0036846119 scopus 로고    scopus 로고
    • TorsinA and heat shock proteins act as molecular chaperones: Suppression of alpha-synuclein aggregation
    • pii:1190
    • McLean PJ, Kawamata H, Shariff S, Hewett J, Sharma N, Ueda K, Breakefield XO, Hyman BT (2002) TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation. J Neurochem 83(4):846-854 (pii:1190)
    • (2002) J Neurochem , vol.83 , Issue.4 , pp. 846-854
    • McLean, P.J.1    Kawamata, H.2    Shariff, S.3    Hewett, J.4    Sharma, N.5    Ueda, K.6    Breakefield, X.O.7    Hyman, B.T.8
  • 31
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • DOI 10.1126/science.1067389
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295(5556):865-868. doi:10.1126/science.1067389389 (Pubitemid 34118369)
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4    Bonini, N.M.5
  • 33
    • 0037237358 scopus 로고    scopus 로고
    • The mouse MPTP model: Gene expression changes in dopaminergic neurons
    • pii:2408
    • Kuhn K, Wellen J, Link N, Maskri L, Lubbert H, Stichel CC (2003) The mouse MPTP model: gene expression changes in dopaminergic neurons. Eur J Neurosci 17(1):1-12 (pii:2408)
    • (2003) Eur J Neurosci , vol.17 , Issue.1 , pp. 1-12
    • Kuhn, K.1    Wellen, J.2    Link, N.3    Maskri, L.4    Lubbert, H.5    Stichel, C.C.6
  • 35
    • 85005900833 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies
    • doi:10.1186/2051-5960-1-79
    • Ebrahimi-Fakhari D, Saidi LJ, Wahlster L (2013) Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies. Acta Neuropathol Commun 1(1):79. doi:10.1186/2051-5960-1-79
    • (2013) Acta Neuropathol Commun , vol.1 , Issue.1 , pp. 79
    • Ebrahimi-Fakhari, D.1    Saidi, L.J.2    Wahlster, L.3
  • 36
    • 78649640867 scopus 로고    scopus 로고
    • Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones
    • doi:10.1074/jbc.M110.127753
    • Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P (2010) Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. J Biol Chem 285(49):38173-38182. doi:10.1074/jbc.M110.127753
    • (2010) J Biol Chem , vol.285 , Issue.49 , pp. 38173-38182
    • Hinault, M.P.1    Cuendet, A.F.2    Mattoo, R.U.3    Mensi, M.4    Dietler, G.5    Lashuel, H.A.6    Goloubinoff, P.7
  • 38
    • 84863683967 scopus 로고    scopus 로고
    • Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
    • doi:10.1371/journal.pbio.1001346
    • Duennwald ML, Echeverria A, Shorter J (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346. doi:10.1371/journal.pbio.1001346
    • (2012) PLoS Biol , vol.10 , Issue.6
    • Duennwald, M.L.1    Echeverria, A.2    Shorter, J.3
  • 39
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • doi:10.1371/journal.pone.0026319
    • Shorter J (2011) The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6(10):e26319. doi:10.1371/journal.pone.0026319
    • (2011) PLoS One , vol.6 , Issue.10
    • Shorter, J.1
  • 40
    • 0037147221 scopus 로고    scopus 로고
    • Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones
    • DOI 10.1074/jbc.M209163200
    • Ben-Zvi AP, Goloubinoff P (2002) Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones. J Biol Chem 277(51):49422-49427. doi:10.1074/jbc.M209163200 (Pubitemid 36014376)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49422-49427
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 41
    • 70349484861 scopus 로고    scopus 로고
    • Disaggregating chaperones: An unfolding story
    • pii:CPPS-4
    • Sharma SK, Christen P, Goloubinoff P (2009) Disaggregating chaperones: an unfolding story. Curr Protein Pept Sci 10(5):432-446 (pii:CPPS-4)
    • (2009) Curr Protein Pept Sci , vol.10 , Issue.5 , pp. 432-446
    • Sharma, S.K.1    Christen, P.2    Goloubinoff, P.3
  • 43
    • 44649091898 scopus 로고    scopus 로고
    • Heavy metal ions are potent inhibitors of protein folding
    • doi:10.1016/j.bbrc.2008.05.052
    • Sharma SK, Goloubinoff P, Christen P (2008) Heavy metal ions are potent inhibitors of protein folding. Biochem Biophys Res Commun 372(2):341-345. doi:10.1016/j.bbrc.2008.05.052
    • (2008) Biochem Biophys Res Commun , vol.372 , Issue.2 , pp. 341-345
    • Sharma, S.K.1    Goloubinoff, P.2    Christen, P.3
  • 44
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler R, Zou J, Voellmy R (1996) Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1(1):33-39 (Pubitemid 126672887)
    • (1996) Cell Stress and Chaperones , vol.1 , Issue.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 46
    • 0025266685 scopus 로고
    • Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B
    • doi:10.1038/344678a0
    • Ghosh S, Baltimore D (1990) Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature 344(6267):678-682. doi:10.1038/344678a0
    • (1990) Nature , vol.344 , Issue.6267 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 47
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran SK, Wisniewski J, Li L, Li GC, Wu C (1994) Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol Cell Biol 14(10):6552-6560 (Pubitemid 24299724)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.10 , pp. 6552-6560
    • Rabindran, S.K.1    Wisniewski, J.2    Li, L.3    Li, G.C.4    Wu, C.5
  • 48
    • 0032571320 scopus 로고    scopus 로고
    • The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 Heterocomplex assembly by the reconstituted hsp90.p60.hsp70 Foldosome complex
    • DOI 10.1074/jbc.273.13.7358
    • Dittmar KD, Banach M, Galigniana MD, Pratt WB (1998) The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex. J Biol Chem 273(13):7358-7366 (Pubitemid 28152756)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.13 , pp. 7358-7366
    • Dittmar, K.D.1    Banach, M.2    Galigniana, M.D.3    Pratt, W.B.4
  • 49
    • 17544384391 scopus 로고    scopus 로고
    • Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate
    • DOI 10.1074/jbc.271.22.12833
    • Dittmar KD, Hutchison KA, Owens-Grillo JK, Pratt WB (1996) Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J Biol Chem 271(22):12833-12839 (Pubitemid 26175857)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.22 , pp. 12833-12839
    • Dittmar, K.D.1    Hutchison, K.A.2    Owens-Grillo, J.K.3    Pratt, W.B.4
  • 50
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 228(2):111-133 (Pubitemid 36187918)
    • (2003) Experimental Biology and Medicine , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 51
    • 84857187885 scopus 로고    scopus 로고
    • Protein folding: Chaperoning protein evolution
    • doi:10.1038/nchembio.791
    • De Los Rios P, Goloubinoff P (2012) Protein folding: chaperoning protein evolution. Nat Chem Biol 8(3):226-228. doi:10.1038/nchembio.791
    • (2012) Nat Chem Biol , vol.8 , Issue.3 , pp. 226-228
    • De Los Rios, P.1    Goloubinoff, P.2
  • 52
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418(6895):291. doi:10.1038/418291a (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 53
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295(5561):1852-1858. doi:10.1126/science.1068408 (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 54
    • 84878901297 scopus 로고    scopus 로고
    • Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
    • doi:10.1016/j.febslet.2013.05.014
    • Priya S, Sharma SK, Goloubinoff P (2013) Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett 587(13):1981-1987. doi:10.1016/j.febslet.2013.05.014
    • (2013) FEBS Lett , vol.587 , Issue.13 , pp. 1981-1987
    • Priya, S.1    Sharma, S.K.2    Goloubinoff, P.3
  • 55
    • 0024578552 scopus 로고
    • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • DOI 10.1038/337044a0
    • Goloubinoff P, Gatenby AA, Lorimer GH (1989) GroE heatshock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337(6202):44-47. doi:10.1038/337044a0 (Pubitemid 19022550)
    • (1989) Nature , vol.337 , Issue.6202 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 56
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • doi:10.1038/358169a0
    • Wiech H, Buchner J, Zimmermann R, Jakob U (1992) Hsp90 chaperones protein folding in vitro. Nature 358(6382):169-170. doi:10.1038/358169a0
    • (1992) Nature , vol.358 , Issue.6382 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 57
    • 0025034590 scopus 로고
    • Folding pathway enigma
    • doi:10.1038/343601b0
    • Buchner J, Kiefhaber T (1990) Folding pathway enigma. Nature 343(6259):601-602. doi:10.1038/343601b0
    • (1990) Nature , vol.343 , Issue.6259 , pp. 601-602
    • Buchner, J.1    Kiefhaber, T.2
  • 58
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96(24):13732-13737
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.24 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 59
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • DOI 10.1093/emboj/16.2.221
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16(2):221-229. doi:10.1093/emboj/16.2.221 (Pubitemid 27049380)
    • (1997) EMBO Journal , vol.16 , Issue.2 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 60
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • DOI 10.1093/emboj/16.3.659
    • Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 16(3):659-671. doi:10.1093/emboj/16.3.659 (Pubitemid 27067794)
    • (1997) EMBO Journal , vol.16 , Issue.3 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 61
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • DOI 10.1074/jbc.273.18.11032
    • Veinger L, Diamant S, Buchner J, Goloubinoff P (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 273(18):11032-11037 (Pubitemid 28204946)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 62
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • DOI 10.1074/jbc.271.12.7218
    • Chang Z, Primm TP, Jakana J, Lee IH, Serysheva I, Chiu W, Gilbert HF, Quiocho FA (1996) Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J Biol Chem 271(12):7218-7223 (Pubitemid 26104163)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.12 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 63
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J (1992) Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89(21):10449-10453
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.21 , pp. 10449-10453
    • Horwitz, J.1
  • 65
    • 0028859629 scopus 로고
    • Characterization and physiological function of class I low-molecular-mass, heat-shock protein complex in soybean
    • pii:108/2/693
    • Jinn TL, Chen YM, Lin CY (1995) Characterization and physiological function of class I low-molecular-mass, heat-shock protein complex in soybean. Plant Physiol 108(2):693-701 (pii:108/2/693)
    • (1995) Plant Physiol , vol.108 , Issue.2 , pp. 693-701
    • Jinn, T.L.1    Chen, Y.M.2    Lin, C.Y.3
  • 66
    • 84880515581 scopus 로고    scopus 로고
    • Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
    • doi:10.1074/jbc.M113.479253
    • Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P (2013) Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem. doi:10.1074/jbc.M113.479253
    • (2013) J Biol Chem
    • Mattoo, R.U.1    Sharma, S.K.2    Priya, S.3    Finka, A.4    Goloubinoff, P.5
  • 67
    • 0032478091 scopus 로고    scopus 로고
    • On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase
    • DOI 10.1021/bi972069y
    • Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR (1998) On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry 37(9):2759-2767. doi:10.1021/bi972069y (Pubitemid 28145728)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 2759-2767
    • Cosgrove, M.S.1    Naylor, C.2    Paludan, S.3    Adams, M.J.4    Levy, H.R.5
  • 68
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee GJ, Pokala N, Vierling E (1995) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J Biol Chem 270(18):10432-10438
    • (1995) J Biol Chem , vol.270 , Issue.18 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 69
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
    • DOI 10.1074/jbc.M405627200
    • Ben-Zvi A, De Los Rios P, Dietler G, Goloubinoff P (2004) Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J Biol Chem 279(36):37298-37303. doi:10.1074/jbc.M405627200 (Pubitemid 39195436)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los, R.P.2    Dietler, G.3    Goloubinoff, P.4
  • 70
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • DOI 10.1074/jbc.M001293200
    • Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P (2000) Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem 275(28):21107-21113. doi:10.1074/jbc.M001293200 (Pubitemid 30481803)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21107-21113
    • Diamant, S.1    Peres B.-Zvi, A.2    Bukau, B.3    Goloubinoff, P.4
  • 71
    • 0024988094 scopus 로고
    • The E. Coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
    • pii:0092-8674(90)90268-J
    • Skowyra D, Georgopoulos C, Zylicz M (1990) The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62(5):939-944 (pii:0092-8674(90)90268-J)
    • (1990) Cell , vol.62 , Issue.5 , pp. 939-944
    • Skowyra, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 72
    • 78649285172 scopus 로고    scopus 로고
    • Chaperones: A story of thrift unfolds
    • doi:10.1038/nchembio.468
    • Baneyx F, Nannenga BL (2010) Chaperones: a story of thrift unfolds. Nat Chem Biol 6(12):880-881. doi:10.1038/nchembio.468
    • (2010) Nat Chem Biol , vol.6 , Issue.12 , pp. 880-881
    • Baneyx, F.1    Nannenga, B.L.2
  • 73
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • doi:10.1038/nsmb.2006
    • Schlecht R, Erbse AH, Bukau B, Mayer MP (2011) Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol 18(3):345-351. doi:10.1038/nsmb.2006
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.3 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 74
    • 33646557371 scopus 로고    scopus 로고
    • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
    • doi:10.1073/pnas.0510496103
    • De Los Rios P, Ben-Zvi A, Slutsky O, Azem A, Goloubinoff P (2006) Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc Natl Acad Sci USA 103(16):6166-6171. doi:10.1073/pnas.0510496103
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.16 , pp. 6166-6171
    • De Los Rios, P.1    Ben-Zvi, A.2    Slutsky, O.3    Azem, A.4    Goloubinoff, P.5
  • 76
    • 17844378217 scopus 로고    scopus 로고
    • Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
    • DOI 10.1038/nsmb901
    • Rivenzon-Segal D, Wolf SG, Shimon L, Willison KR, Horovitz A (2005) Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 12(3):233-237. doi:10.1038/nsmb901 (Pubitemid 43079364)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.3 , pp. 233-237
    • Rivenzon-Segal, D.1    Wolf, S.G.2    Shimon, L.3    Willison, K.R.4    Horovitz, A.5
  • 77
    • 77957804652 scopus 로고    scopus 로고
    • ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein
    • doi:10.1074/jbc.M110.112110
    • Walerych D, Gutkowska M, Klejman MP, Wawrzynow B, Tracz Z, Wiech M, Zylicz M, Zylicz A (2010) ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein. J Biol Chem 285(42):32020-32028. doi:10.1074/jbc.M110.112110
    • (2010) J Biol Chem , vol.285 , Issue.42 , pp. 32020-32028
    • Walerych, D.1    Gutkowska, M.2    Klejman, M.P.3    Wawrzynow, B.4    Tracz, Z.5    Wiech, M.6    Zylicz, M.7    Zylicz, A.8
  • 79
    • 79957730170 scopus 로고    scopus 로고
    • Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
    • doi:10.1073/pnas.1104703108
    • Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S (2011) Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci USA 108(20):8206-8211. doi:10.1073/pnas.1104703108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.20 , pp. 8206-8211
    • Genest, O.1    Hoskins, J.R.2    Camberg, J.L.3    Doyle, S.M.4    Wickner, S.5
  • 80
    • 79955724860 scopus 로고    scopus 로고
    • Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate
    • doi:10.1002/prot.23024
    • Sharma SK, De Los Rios P, Goloubinoff P (2011) Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins 79(6):1991-1998. doi:10.1002/prot.23024
    • (2011) Proteins , vol.79 , Issue.6 , pp. 1991-1998
    • Sharma, S.K.1    De Los Rios, P.2    Goloubinoff, P.3
  • 81
    • 34247589657 scopus 로고    scopus 로고
    • Activation of the heat shock response in plants by chlorophenols: Transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants
    • DOI 10.1111/j.1365-3040.2007.01664.x
    • Saidi Y, Domini M, Choy F, Zryd JP, Schwitzguebel JP, Goloubinoff P (2007) Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant Cell Environ 30(6):753-763. doi:10.1111/j.1365-3040.2007. 01664.x (Pubitemid 46674422)
    • (2007) Plant, Cell and Environment , vol.30 , Issue.6 , pp. 753-763
    • Saidi, Y.1    Domini, M.2    Choy, F.3    Zryd, J.-P.4    Schwitzguebel, J.-P.5    Goloubinoff, P.6
  • 82
    • 0031589203 scopus 로고    scopus 로고
    • GroES binding regulates GroEL chaperonin activity under heat shock
    • pii:S0014-5793(97)00348-7
    • Goloubinoff P, Diamant S, Weiss C, Azem A (1997) GroES binding regulates GroEL chaperonin activity under heat shock. FEBS Lett 407(2):215-219 (pii:S0014-5793(97)00348-7)
    • (1997) FEBS Lett , vol.407 , Issue.2 , pp. 215-219
    • Goloubinoff, P.1    Diamant, S.2    Weiss, C.3    Azem, A.4
  • 83
    • 0032493416 scopus 로고    scopus 로고
    • Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: Protein- folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration
    • DOI 10.1021/bi980338u
    • Diamant S, Goloubinoff P (1998) Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. Biochemistry 37(27):9688-9694. doi:10.1021/bi980338u (Pubitemid 28319613)
    • (1998) Biochemistry , vol.37 , Issue.27 , pp. 9688-9694
    • Diamant, S.1    Goloubinoff, P.2
  • 84
    • 74549165678 scopus 로고    scopus 로고
    • Biochemistry: Tackling unintelligent design
    • doi:10.1038/463164a
    • Ellis RJ (2010) Biochemistry: tackling unintelligent design. Nature 463(7278):164-165. doi:10.1038/463164a
    • (2010) Nature , vol.463 , Issue.7278 , pp. 164-165
    • Ellis, R.J.1
  • 85
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • DOI 10.1146/annurev.arplant.53.100301.135233
    • Spreitzer RJ, Salvucci ME (2002) RuBisCO: structure, regulatory interactions, and possibilities for a better enzyme. Annu Rev Plant Biol 53:449-475. doi:10.1146/annurev.arplant.53.100301.135233 (Pubitemid 36257503)
    • (2002) Annual Review of Plant Biology , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 86
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • pii:S0092-8674(00)81223-4
    • Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82 (pii:S0092-8674(00)81223-4)
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 88
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
    • doi:10.1038/nsmb.2442
    • Seyffer F, Kummer E, Oguchi Y, Winkler J, Kumar M, Zahn R, Sourjik V, Bukau B, Mogk A (2012) Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat Struct Mol Biol 19(12):1347-1355. doi:10.1038/nsmb.2442
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.12 , pp. 1347-1355
    • Seyffer, F.1    Kummer, E.2    Oguchi, Y.3    Winkler, J.4    Kumar, M.5    Zahn, R.6    Sourjik, V.7    Bukau, B.8    Mogk, A.9
  • 89
    • 84891905978 scopus 로고    scopus 로고
    • Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation
    • doi:10.1074/jbc.M113.520759
    • Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, Wendler P, Shorter J (2014) Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J Biol Chem 289(2):848-867. doi:10.1074/jbc.M113.520759
    • (2014) J Biol Chem , vol.289 , Issue.2 , pp. 848-867
    • Desantis, M.E.1    Sweeny, E.A.2    Snead, D.3    Leung, E.H.4    Go, M.S.5    Gupta, K.6    Wendler, P.7    Shorter, J.8
  • 90
    • 84878143436 scopus 로고    scopus 로고
    • Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor
    • doi:10.1073/pnas.1217988110
    • Lee J, Kim JH, Biter AB, Sielaff B, Lee S, Tsai FT (2013) Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc Natl Acad Sci USA 110(21):8513-8518. doi:10.1073/pnas.1217988110
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.21 , pp. 8513-8518
    • Lee, J.1    Kim, J.H.2    Biter, A.B.3    Sielaff, B.4    Lee, S.5    Tsai, F.T.6
  • 92
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • DOI 10.1038/sj.emboj.7601138, PII 7601138
    • Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25(11):2519-2528. doi:10.1038/sj.emboj.7601138 (Pubitemid 44012234)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 93
    • 44649110104 scopus 로고    scopus 로고
    • Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
    • DOI 10.1016/j.cell.2008.05.022, PII S0092867408006788
    • Polier S, Dragovic Z, Hartl FU, Bracher A (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133(6):1068-1079. doi:10.1016/j.cell.2008.05.022 (Pubitemid 351787748)
    • (2008) Cell , vol.133 , Issue.6 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 94
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • DOI 10.1038/sj.emboj.7601139, PII 7601139
    • Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B (2006) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 25(11):2510-2518. doi:10.1038/sj.emboj.7601139 (Pubitemid 44012233)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 95
  • 96
    • 84893855426 scopus 로고    scopus 로고
    • The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins
    • Torrente MP, Shorter J (2013) The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion 7(6):457-463
    • (2013) Prion , vol.7 , Issue.6 , pp. 457-463
    • Torrente, M.P.1    Shorter, J.2
  • 97
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. Coli: Interaction of SRP and trigger factor with nascent polypeptides
    • Valent QA, Kendall DA, High S, Kusters R, Oudega B, Luirink J (1995) Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J 14(22):5494-5505
    • (1995) EMBO J , vol.14 , Issue.22 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 98
    • 0030805752 scopus 로고    scopus 로고
    • Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor
    • Valent QA, de Gier JW, von Heijne G, Kendall DA, ten Hagen-Jongman CM, Oudega B, Luirink J (1997) Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor. Mol Microbiol 25(1):53-64 (Pubitemid 27316121)
    • (1997) Molecular Microbiology , vol.25 , Issue.1 , pp. 53-64
    • Valent, Q.A.1    De Gier, J.-W.L.2    Von Heijne, G.3    Kendall, D.A.4    Ten H.-Jongman, C.M.5    Oudega, B.6    Luirink, J.7
  • 99
    • 0034820026 scopus 로고    scopus 로고
    • Functional dissection of trigger factor and DnaK: Interactions with nascent polypeptides and thermally denatured proteins
    • DOI 10.1515/BC.2001.154
    • Schaffitzel E, Rudiger S, Bukau B, Deuerling E (2001) Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins. Biol Chem 382(8):1235-1243. doi:10.1515/BC.2001.154 (Pubitemid 32894030)
    • (2001) Biological Chemistry , vol.382 , Issue.8 , pp. 1235-1243
    • Schaffitzel, E.1    Rudiger, S.2    Bukau, B.3    Deuerling, E.4
  • 100
    • 11244280828 scopus 로고    scopus 로고
    • Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat-mediated export
    • DOI 10.1111/j.1432-1033.2004.04442.x
    • Jong WSP, ten Hagen-Jongman CM, Genevaux P, Brunner J, Oudega B, Luirink J (2004) Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat-mediated export. Eur J Biochem 271(23-24):4779-4787 (Pubitemid 40065580)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.23-24 , pp. 4779-4787
    • Jong, W.S.P.1    Ten H.-Jongman, C.M.2    Genevaux, P.3    Brunner, J.4    Oudega, B.5    Luirink, J.6
  • 102
    • 0038360877 scopus 로고    scopus 로고
    • Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome
    • DOI 10.1083/jcb.200302130
    • Ullers RS, Houben EN, Raine A, ten Hagen-Jongman CM, Ehrenberg M, Brunner J, Oudega B, Harms N, Luirink J (2003) Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome. J Cell Biol 161(4):679-684. doi:10.1083/jcb.200302130 (Pubitemid 36648750)
    • (2003) Journal of Cell Biology , vol.161 , Issue.4 , pp. 679-684
    • Ullers, R.S.1    Houben, E.N.G.2    Raine, A.3    Ten H.-Jongman, C.M.4    Ehrenberg, M.5    Brunner, J.6    Oudega, B.7    Harms, N.8    Luirink, J.9
  • 103
    • 33744925719 scopus 로고    scopus 로고
    • Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle
    • DOI 10.1074/jbc.M600638200
    • Ullers RS, Houben EN, Brunner J, Oudega B, Harms N, Luirink J (2006) Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle. J Biol Chem 281(20):13999-14005. doi:10.1074/jbc.M600638200 (Pubitemid 43848326)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 13999-14005
    • Ullers, R.S.1    Houben, E.N.G.2    Brunner, J.3    Oudega, B.4    Harms, N.5    Luirink, J.6
  • 104
    • 79953106751 scopus 로고    scopus 로고
    • The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
    • doi:10.1016/j.sbi.2011.01.007
    • Wilson DN, Beckmann R (2011) The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling. Curr Opin Struct Biol 21(2):274-282. doi:10.1016/j.sbi.2011.01.007
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.2 , pp. 274-282
    • Wilson, D.N.1    Beckmann, R.2
  • 105
    • 84867379923 scopus 로고    scopus 로고
    • Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding
    • doi:10.1016/j.molcel.2012.07.018
    • Hoffmann A, Becker AH, Zachmann-Brand B, Deuerling E, Bukau B, Kramer G (2012) Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. Mol Cell 48(1):63-74. doi:10.1016/j.molcel.2012.07.018
    • (2012) Mol Cell , vol.48 , Issue.1 , pp. 63-74
    • Hoffmann, A.1    Becker, A.H.2    Zachmann-Brand, B.3    Deuerling, E.4    Bukau, B.5    Kramer, G.6
  • 106
    • 84867364077 scopus 로고    scopus 로고
    • You got to know when to hold (or unfold) 'em
    • doi:10.1016/j.molcel.2012.09.022
    • Hebert DN, Chandrasekhar KD, Gierasch LM (2012) You got to know when to hold (or unfold) 'em. Mol Cell 48(1):3-4. doi:10.1016/j.molcel.2012.09.022
    • (2012) Mol Cell , vol.48 , Issue.1 , pp. 3-4
    • Hebert, D.N.1    Chandrasekhar, K.D.2    Gierasch, L.M.3
  • 107
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • DOI 10.1038/nature02899
    • Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N (2004) Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431(7008):590-596. doi:10.1038/nature02899 (Pubitemid 39336342)
    • (2004) Nature , vol.431 , Issue.7008 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 108
    • 33845984939 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
    • DOI 10.1074/jbc.M605164200
    • Merz F, Hoffmann A, Rutkowska A, Zachmann-Brand B, Bukau B, Deuerling E (2006) The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J Biol Chem 281(42):31963-31971. doi:10.1074/jbc.M605164200 (Pubitemid 46041458)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31963-31971
    • Merz, F.1    Hoffmann, A.2    Rutkowska, A.3    Zachmann-Brand, B.4    Bukau, B.5    Deuerling, E.6
  • 110
    • 0033918740 scopus 로고    scopus 로고
    • Assisted folding of d-glyceraldehyde-3-phosphate dehydrogenase by trigger factor
    • doi:10.1110/ps.9.6.1254
    • Huang GC, Li ZY, Zhou JM, Fischer G (2000) Assisted folding of d-glyceraldehyde-3-phosphate dehydrogenase by trigger factor. Protein Sci 9(6):1254-1261. doi:10.1110/ps.9.6.1254
    • (2000) Protein Sci , vol.9 , Issue.6 , pp. 1254-1261
    • Huang, G.C.1    Li, Z.Y.2    Zhou, J.M.3    Fischer, G.4
  • 111
    • 22144451849 scopus 로고    scopus 로고
    • Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
    • DOI 10.1111/j.1365-2958.2005.04690.x
    • Rauch T, Hundley HA, Pfund C, Wegrzyn RD, Walter W, Kramer G, Kim SY, Craig EA, Deuerling E (2005) Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Mol Microbiol 57(2):357-365. doi:10.1111/j.1365-2958.2005.04690.x (Pubitemid 40979338)
    • (2005) Molecular Microbiology , vol.57 , Issue.2 , pp. 357-365
    • Rauch, T.1    Hundley, H.A.2    Pfund, C.3    Wegrzyn, R.D.4    Walter, W.5    Kramer, G.6    Kim, S.-Y.7    Craig, E.A.8    Deuerling, E.9
  • 113
    • 84862848780 scopus 로고    scopus 로고
    • Ribosome-associated chaperones as key players in proteostasis
    • doi:10.1016/j.tibs.2012.03.002
    • Preissler S, Deuerling E (2012) Ribosome-associated chaperones as key players in proteostasis. Trends Biochem Sci 37(7):274-283. doi:10.1016/j.tibs. 2012.03.002
    • (2012) Trends Biochem Sci , vol.37 , Issue.7 , pp. 274-283
    • Preissler, S.1    Deuerling, E.2
  • 114
    • 22444439361 scopus 로고    scopus 로고
    • The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuol
    • DOI 10.1038/nsmb942, PII NSMB942
    • Huang P, Gautschi M, Walter W, Rospert S, Craig EA (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504. doi:10.1038/nsmb942 (Pubitemid 43085879)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.6 , pp. 497-504
    • Huang, P.1    Gautschi, M.2    Walter, W.3    Rospert, S.4    Craig, E.A.5
  • 115
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • doi:10.1016/j.cell.2009.08.005
    • Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138(4):628-644. doi:10.1016/j.cell.2009.08.005
    • (2009) Cell , vol.138 , Issue.4 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 116
    • 0032728066 scopus 로고    scopus 로고
    • Posttranslational protein translocation across the membrane of the endoplasmic reticulum
    • DOI 10.1515/BC.1999.145
    • Rapoport TA, Matlack KE, Plath K, Misselwitz B, Staeck O (1999) Posttranslational protein translocation across the membrane of the endoplasmic reticulum. Biol Chem 380(10):1143-1150. doi:10.1515/BC.1999.145 (Pubitemid 29516402)
    • (1999) Biological Chemistry , vol.380 , Issue.10 , pp. 1143-1150
    • Rapoport, T.A.1    Matlack, K.E.S.2    Plath, K.3    Misselwitz, B.4    Staeck, O.5
  • 117
    • 80052576118 scopus 로고    scopus 로고
    • The motors of protein import into chloroplasts
    • doi:10.4161/psb.6.9.16916
    • Shi LX, Theg SM (2011) The motors of protein import into chloroplasts. Plant Signal Behav 6(9):1397-1401. doi:10.4161/psb.6.9.16916
    • (2011) Plant Signal Behav , vol.6 , Issue.9 , pp. 1397-1401
    • Shi, L.X.1    Theg, S.M.2
  • 118
    • 78650517733 scopus 로고    scopus 로고
    • Common ground for protein translocation: Access control for mitochondria and chloroplasts
    • doi:10.1038/nrm3027
    • Schleiff E, Becker T (2011) Common ground for protein translocation: access control for mitochondria and chloroplasts. Nat Rev Mol Cell Biol 12(1):48-59. doi:10.1038/nrm3027
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.1 , pp. 48-59
    • Schleiff, E.1    Becker, T.2
  • 119
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • pii:S0092-8674(00)81320-3
    • Bauer MF, Sirrenberg C, Neupert W, Brunner M (1996) Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87(1):33-41 (pii:S0092-8674(00)81320-3)
    • (1996) Cell , vol.87 , Issue.1 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 120
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import: Delta psi Drives the movement of presequences
    • Martin J, Mahlke K, Pfanner N (1991) Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J Biol Chem 266(27):18051-18057 (Pubitemid 21908046)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.27 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 121
    • 0028132179 scopus 로고
    • Mitochondrial Hsp70/MIM44 complex facilitates protein import
    • DOI 10.1038/371768a0
    • Schneider HC, Berthold J, Bauer MF, Dietmeier K, Guiard B, Brunner M, Neupert W (1994) Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature 371(6500):768-774. doi:10.1038/371768a0 (Pubitemid 24333863)
    • (1994) Nature , vol.371 , Issue.6500 , pp. 768-774
    • Schneider, H.-C.1    Berthold, J.2    Bauer, M.F.3    Dietmeier, K.4    Guiard, B.5    Brunner, M.6    Neupert, W.7
  • 122
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann C, Neupert W, Cyr DM (1994) The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266(5188):1250-1253 (Pubitemid 24371284)
    • (1994) Science , vol.266 , Issue.5188 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 123
    • 0029070886 scopus 로고
    • The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system
    • pii:S0092-8674(05)80013-3
    • Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W, Brunner M (1995) The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system. Cell 81(7):1085-1093 (pii:S0092-8674(05)80013-3)
    • (1995) Cell , vol.81 , Issue.7 , pp. 1085-1093
    • Berthold, J.1    Bauer, M.F.2    Schneider, H.C.3    Klaus, C.4    Dietmeier, K.5    Neupert, W.6    Brunner, M.7
  • 124
    • 0035854691 scopus 로고    scopus 로고
    • Modular structure of the TIM23 preprotein translocase of mitochondria
    • doi:10.1074/jbc.M102132200
    • Milisav I, Moro F, Neupert W, Brunner M (2001) Modular structure of the TIM23 preprotein translocase of mitochondria. J Biol Chem 276(28):25856-25861. doi:10.1074/jbc.M102132200
    • (2001) J Biol Chem , vol.276 , Issue.28 , pp. 25856-25861
    • Milisav, I.1    Moro, F.2    Neupert, W.3    Brunner, M.4
  • 125
    • 0033168677 scopus 로고    scopus 로고
    • The TIM17.23 preprotein translocase of mitochondria: Composition and function in protein transport into the matrix
    • DOI 10.1093/emboj/18.13.3667
    • Moro F, Sirrenberg C, Schneider HC, Neupert W, Brunner M (1999) The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix. EMBO J 18(13):3667-3675. doi:10.1093/emboj/ 18.13.3667 (Pubitemid 29308846)
    • (1999) EMBO Journal , vol.18 , Issue.13 , pp. 3667-3675
    • Moro, F.1    Sirrenberg, C.2    Schneider, H.-C.3    Neupert, W.4    Brunner, M.5
  • 126
    • 0029856628 scopus 로고    scopus 로고
    • The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
    • Schneider HC, Westermann B, Neupert W, Brunner M (1996) The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J 15(21):5796-5803 (Pubitemid 26375501)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5796-5803
    • Schneider, H.-C.1    Westermann, B.2    Neupert, W.3    Brunner, M.4
  • 127
    • 0038889171 scopus 로고    scopus 로고
    • Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins
    • DOI 10.1093/emboj/17.15.4226
    • Bomer U, Maarse AC, Martin F, Geissler A, Merlin A, Schonfisch B, Meijer M, Pfanner N, Rassow J (1998) Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins. EMBO J 17(15):4226-4237. doi:10.1093/emboj/17.15.4226 (Pubitemid 28362613)
    • (1998) EMBO Journal , vol.17 , Issue.15 , pp. 4226-4237
    • Bomer, U.1    Maarse, A.C.2    Martin, F.3    Geissler, A.4    Merlin, A.5    Schonfisch, B.6    Meijer, M.7    Pfanner, N.8    Rassow, J.9
  • 128
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • pii:S0092-8674(00)80928-9
    • Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92(3):351-366 (pii:S0092-8674(00)80928-9)
    • (1998) Cell , vol.92 , Issue.3 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 129
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • pii:0092-8674(95)90444-1
    • Glick BS (1995) Can Hsp70 proteins act as force-generating motors? Cell 80(1):11-14 (pii:0092-8674(95)90444-1)
    • (1995) Cell , vol.80 , Issue.1 , pp. 11-14
    • Glick, B.S.1
  • 130
    • 0033592642 scopus 로고    scopus 로고
    • Protein translocation: Is Hsp70 pulling my chain?
    • DOI 10.1016/S0960-9822(00)80012-3
    • Jensen RE, Johnson AE (1999) Protein translocation: is Hsp70 pulling my chain? Curr Biol 9(20):R779-R782. doi:10.1016/S0960-9822(00)80012-3 (Pubitemid 29527095)
    • (1999) Current Biology , vol.9 , Issue.20
    • Jensen, R.E.1    Johnson, A.E.2
  • 131
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • DOI 10.1038/35073006
    • Pfanner N, Geissler A (2001) Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2(5):339-349. doi:10.1038/35073006 (Pubitemid 33674046)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.5 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 132
    • 0029240213 scopus 로고
    • Protein sorting. Pulling in the proteins
    • pii:S0960-9822(95)00033-9
    • Pfanner N, Meijer M (1995) Protein sorting. Pulling in the proteins. Curr Biol 5(2):132-135 (pii:S0960-9822(95)00033-9)
    • (1995) Curr Biol , vol.5 , Issue.2 , pp. 132-135
    • Pfanner, N.1    Meijer, M.2
  • 133
    • 0035715285 scopus 로고    scopus 로고
    • Hsp70 proteins in protein translocation
    • DOI 10.1016/S0065-3233(01)59007-5
    • Ryan MT, Pfanner N (2001) Hsp70 proteins in protein translocation. Adv Protein Chem 59:223-242 (Pubitemid 34169306)
    • (2001) Advances in Protein Chemistry , vol.59 , pp. 223-242
    • Ryan, M.T.1    Pfanner, N.2
  • 134
    • 34547146401 scopus 로고    scopus 로고
    • The mechanism of Hsp70 chaperones: (entropic) pulling the models together
    • DOI 10.1016/j.tibs.2007.06.008, PII S0968000407001685
    • Goloubinoff P, De Los Rios P (2007) The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem Sci 32(8):372-380. doi:10.1016/j.tibs.2007.06.008 (Pubitemid 47126861)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.8 , pp. 372-380
    • Goloubinoff, P.1    Rios, P.D.L.2
  • 135
    • 62449229531 scopus 로고    scopus 로고
    • Chaperone effects on prion and nonprion aggregates
    • pii:5058
    • Rikhvanov EG, Romanova NV, Chernoff YO (2007) Chaperone effects on prion and nonprion aggregates. Prion 1(4):217-222 (pii:5058)
    • (2007) Prion , vol.1 , Issue.4 , pp. 217-222
    • Rikhvanov, E.G.1    Romanova, N.V.2    Chernoff, Y.O.3
  • 136
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • DOI 10.1038/76819
    • Mayer MP, Schroder H, Rudiger S, Paal K, Laufen T, Bukau B (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol 7(7):586-593. doi:10.1038/76819 (Pubitemid 30445917)
    • (2000) Nature Structural Biology , vol.7 , Issue.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 140
    • 0033575256 scopus 로고    scopus 로고
    • Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
    • Misselwitz B, Staeck O, Matlack KE, Rapoport TA (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274(29):20110-20115
    • (1999) J Biol Chem , vol.274 , Issue.29 , pp. 20110-20115
    • Misselwitz, B.1    Staeck, O.2    Matlack, K.E.3    Rapoport, T.A.4
  • 141
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • doi:10.1016/j.cell.2012.11.002
    • Zhuravleva A, Clerico EM, Gierasch LM (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151(6):1296-1307. doi:10.1016/j.cell.2012.11.002
    • (2012) Cell , vol.151 , Issue.6 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 142
    • 79955565642 scopus 로고    scopus 로고
    • Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
    • doi:10.1073/pnas.1014448108
    • Zhuravleva A, Gierasch LM (2011) Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci USA 108(17):6987-6992. doi:10.1073/pnas. 1014448108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.17 , pp. 6987-6992
    • Zhuravleva, A.1    Gierasch, L.M.2
  • 144
    • 84873684893 scopus 로고    scopus 로고
    • Unique structural modulation of a non-native substrate by cochaperone Dna
    • doi:10.1021/bi301543g
    • Tiwari S, Kumar V, Jayaraj GG, Maiti S, Mapa K (2013) Unique structural modulation of a non-native substrate by cochaperone DnaJ. Biochemistry 52(6):1011-1018. doi:10.1021/bi301543g
    • (2013) J. Biochemistry , vol.52 , Issue.6 , pp. 1011-1018
    • Tiwari, S.1    Kumar, V.2    Jayaraj, G.G.3    Maiti, S.4    Mapa, K.5
  • 145
    • 35649024724 scopus 로고    scopus 로고
    • Structural Basis of J Cochaperone Binding and Regulation of Hsp70
    • DOI 10.1016/j.molcel.2007.08.022, PII S1097276507005928
    • Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R (2007) Structural basis of J cochaperone binding and regulation of Hsp70. Mol Cell 28(3):422-433. doi:10.1016/j.molcel.2007.08.022 (Pubitemid 350030560)
    • (2007) Molecular Cell , vol.28 , Issue.3 , pp. 422-433
    • Jiang, J.1    Maes, E.G.2    Taylor, A.B.3    Wang, L.4    Hinck, A.P.5    Lafer, E.M.6    Sousa, R.7
  • 146
    • 0025949426 scopus 로고
    • Light-chain-independent binding of adaptors, AP180, and auxilin to clathrin
    • Lindner R, Ungewickell E (1991) Light-chain-independent binding of adaptors, AP180, and auxilin to clathrin. Biochemistry 30(37):9097-9101
    • (1991) Biochemistry , vol.30 , Issue.37 , pp. 9097-9101
    • Lindner, R.1    Ungewickell, E.2
  • 147
    • 0038290383 scopus 로고    scopus 로고
    • Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface
    • DOI 10.1021/bi034270g
    • Jiang J, Taylor AB, Prasad K, Ishikawa-Brush Y, Hart PJ, Lafer EM, Sousa R (2003) Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface. Biochemistry 42(19):5748-5753. doi:10.1021/bi034270g (Pubitemid 36582866)
    • (2003) Biochemistry , vol.42 , Issue.19 , pp. 5748-5753
    • Jiang, J.1    Taylor, A.B.2    Prasad, K.3    Ishikawa-Brush, Y.4    Hart, P.J.5    Lafer, E.M.6    Sousa, R.7
  • 148
    • 0037147292 scopus 로고    scopus 로고
    • Identification of domain required for catalytic activity of auxilin in supporting clathrin uncoating by Hsc70
    • DOI 10.1074/jbc.M203695200
    • Ma Y, Greener T, Pacold ME, Kaushal S, Greene LE, Eisenberg E (2002) Identification of domain required for catalytic activity of auxilin in supporting clathrin uncoating by Hsc70. J Biol Chem 277(51):49267-49274. doi:10.1074/jbc.M203695200 (Pubitemid 36014355)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.51 , pp. 49267-49274
    • Ma, Y.1    Greener, T.2    Pacold, M.E.3    Kaushal, S.4    Greene, L.E.5    Eisenberg, E.6
  • 150
    • 0033020519 scopus 로고    scopus 로고
    • Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy
    • DOI 10.1006/jmbi.1999.2844
    • Mayer MP, Laufen T, Paal K, McCarty JS, Bukau B (1999) Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. J Mol Biol 289(4):1131-1144. doi:10.1006/jmbi.1999.2844 (Pubitemid 29306675)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.4 , pp. 1131-1144
    • Mayer, M.P.1    Laufen, T.2    Paal, K.3    McCarty, J.S.4    Bukau, B.5
  • 152
    • 38749083424 scopus 로고    scopus 로고
    • Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane
    • DOI 10.1091/mbc.E07-08-0748
    • D'Silva PR, Schilke B, Hayashi M, Craig EA (2008) Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane. Mol Biol Cell 19(1):424-432. doi:10.1091/mbc.E07-08-0748 (Pubitemid 351186165)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 424-432
    • D'Silva, P.R.1    Schilke, B.2    Hayashi, M.3    Craig, E.A.4
  • 153
    • 33644816759 scopus 로고    scopus 로고
    • Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
    • DOI 10.1016/j.tibs.2006.01.002, PII S0968000406000235
    • Soto C, Estrada L, Castilla J (2006) Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem Sci 31(3):150-155. doi:10.1016/j.tibs.2006.01.002 (Pubitemid 43357995)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.3 , pp. 150-155
    • Soto, C.1    Estrada, L.2    Castilla, J.3
  • 154
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes
    • DOI 10.1021/bi971843e
    • Terzi E, Holzemann G, Seelig J (1997) Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry 36(48):14845-14852. doi:10.1021/bi971843e (Pubitemid 27524407)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14845-14852
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 155
    • 0141891097 scopus 로고    scopus 로고
    • The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation
    • DOI 10.1074/jbc.M305326200
    • Zhu M, Li J, Fink AL (2003) The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation. J Biol Chem 278(41):40186-40197. doi:10.1074/jbc.M305326200 (Pubitemid 37248587)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 157
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • DOI 10.1038/nsmb993, PII N993
    • Haslbeck M, Franzmann T, Weinfurtner D, Buchner J (2005) Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 12(10):842-846. doi:10.1038/nsmb993 (Pubitemid 41486706)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 158
    • 1642361660 scopus 로고    scopus 로고
    • The ClpB/Hsp104 molecular chaperone - A protein disaggregating machine
    • DOI 10.1016/j.jsb.2003.11.016, PII S104784770300282X
    • Lee S, Sowa ME, Choi JM, Tsai FT (2004) The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine. J Struct Biol 146(1-2):99-105. doi:10.1016/j.jsb.2003.11.016 (Pubitemid 38369022)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 99-105
    • Lee, S.1    Sowa, M.E.2    Choi, J.-M.3    Tsai, F.T.F.4
  • 159
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • doi:10.1038/348137a0
    • Kang PJ, Ostermann J, Shilling J, Neupert W, Craig EA, Pfanner N (1990) Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348(6297):137-143. doi:10.1038/348137a0
    • (1990) Nature , vol.348 , Issue.6297 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 160
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • DOI 10.1038/342884a0
    • Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342(6252):884-889. doi:10.1038/342884a0 (Pubitemid 20021332)
    • (1989) Nature , vol.342 , Issue.6252 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 161
    • 56249135270 scopus 로고    scopus 로고
    • Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
    • doi:10.1073/pnas.0809794105
    • Apetri AC, Horwich AL (2008) Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc Natl Acad Sci USA 105(45):17351-17355. doi:10.1073/pnas.0809794105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.45 , pp. 17351-17355
    • Apetri, A.C.1    Horwich, A.L.2
  • 162
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • pii:S0968-0004(99)01373-0
    • Buchner J (1999) Hsp90 & Co. - a holding for folding. Trends Biochem Sci 24(4):136-141 (pii:S0968-0004(99)01373-0)
    • (1999) Trends Biochem Sci , vol.24 , Issue.4 , pp. 136-141
    • Buchner, J.1
  • 163
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • DOI 10.1038/nsmb.1425, PII NSMB1425
    • Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B (2008) Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol 15(6):641-650. doi:10.1038/nsmb.1425 (Pubitemid 351799133)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.6 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6    Bukau, B.7
  • 164
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B (1999) Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18(24):6934-6949. doi:10.1093/emboj/18.24.6934 (Pubitemid 30000447)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7


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