메뉴 건너뛰기




Volumn 36, Issue 1, 2010, Pages 1-10

Molecular chaperones

Author keywords

Heat shock proteins; Molecular chaperones; Remodeling of proteins

Indexed keywords


EID: 77649123895     PISSN: 10681620     EISSN: None     Source Type: Journal    
DOI: 10.1134/S1068162010010012     Document Type: Review
Times cited : (6)

References (71)
  • 1
    • 0029566336 scopus 로고
    • 1:CAS:528:DyaK28XhsVCksA%3D%3D 8529835
    • J.P. Hendrick F.U. Hartl 1995 FASEB J. 9 1559 1569 1:CAS:528: DyaK28XhsVCksA%3D%3D 8529835
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 3
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • DOI 10.1146/annurev.biochem.70.1.603
    • J. Frydman 2001 Annu. Rev. Biochem. 70 603 647 10.1146/annurev.biochem. 70.1.603 1:CAS:528:DC%2BD3MXlsVehtLo%3D 11395418 (Pubitemid 32662220)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 603-648
    • Frydman, J.1
  • 4
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • F.U. Hartl M. Hayer-Hartl 2002 Science 295 1852 1858 10.1126/science. 1068408 1:CAS:528:DC%2BD38XhvFClsL4%3D 11884745 (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 5
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • DOI 10.1016/j.semcdb.2003.12.008
    • C.M. Dobson 2004 Semin. Cell. Dev. Biol. 15 3 16 10.1016/j.semcdb.2003. 12.008 1:CAS:528:DC%2BD2cXptVansg%3D%3D 15036202 (Pubitemid 38177363)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.1 , pp. 3-16
    • Dobson, C.M.1
  • 6
    • 77649163232 scopus 로고    scopus 로고
    • St.-Peterb. Univ. St. Petersburg. (Protein Folding)
    • Myul'berg, A.A., Folding belka (Protein Folding), St. Petersburg: St.-Peterb. Univ., 2004, 155.
    • (2004) Folding Belka , pp. 155
    • Myul'Berg, A.A.1
  • 7
    • 51749114237 scopus 로고    scopus 로고
    • 10.1111/j.1742-4658.2008.06590.x 1:CAS:528:DC%2BD1cXht1SnsbrL 18680510
    • Ch. Christis N.H. Lubsen I. Braakman 2008 FEBS J. 275 4700 4727 10.1111/j.1742-4658.2008.06590.x 1:CAS:528:DC%2BD1cXht1SnsbrL 18680510
    • (2008) FEBS J. , vol.275 , pp. 4700-4727
    • Christis, Ch.1    Lubsen, N.H.2    Braakman, I.3
  • 8
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • DOI 10.1016/S0959-440X(00)00172-X
    • R.J. Ellis 2001 Curr. Opin. Struct. Biol. 11 114 119 10.1016/S0959- 440X(00)00172-X 1:CAS:528:DC%2BD3MXhs1Kis7o%3D 11179900 (Pubitemid 32155560)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.1 , pp. 114-119
    • Ellis, R.J.1
  • 9
    • 77649083967 scopus 로고    scopus 로고
    • Problema belka
    • Nauka Moscow. (Protein Problem)
    • Popov, E.M., et al., Problema belka (Protein Problem), vol. 2: Prostranstvennoe stroenie belka (Protein Spatial Structure), Moscow: Nauka, 1996, pp. 406-430.
    • (1996) Prostranstvennoe Stroenie Belka , pp. 406-430
    • Popov, E.M.1
  • 10
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C.M. Dobson 2003 Nature 426 884 890 10.1038/nature02261 1:CAS:528:DC%2BD3sXpvVGmtbk%3D 14685248 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 11
    • 59649108278 scopus 로고    scopus 로고
    • 10.1002/iub.117 1:CAS:528:DC%2BD1cXhsFSnsbjL
    • H. Ecroyd J.A. Carver 2008 IUMBM Life 60 769 774 10.1002/iub.117 1:CAS:528:DC%2BD1cXhsFSnsbjL
    • (2008) IUMBM Life , vol.60 , pp. 769-774
    • Ecroyd, H.1    Carver, J.A.2
  • 13
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • DOI 10.1038/317267a0
    • J.C. Edman L. Ellis R.W. Blacher R.A. Roth W.J. Rutter 1985 Nature 317 267 270 10.1038/317267a0 1:CAS:528:DyaL2MXmtVOru7Y%3D 3840230 (Pubitemid 16246506)
    • (1985) Nature , vol.317 , Issue.6034 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3
  • 15
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trams isomerases, a superfamily of ubiquitous folding catalysts
    • DOI 10.1007/s000180050299
    • S.F. Göthel M.A. Marahiel 1999 Cell. Mol. Life Sci. 55 423 436 10.1007/s000180050299 10228556 (Pubitemid 29178881)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.3 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 16
    • 0023668329 scopus 로고
    • 10.1038/328378a0 1:STN:280:DyaL2s3oslWqtQ%3D%3D 3112578
    • R.J. Ellis 1987 Nature 328 378 379 10.1038/328378a0 1:STN:280: DyaL2s3oslWqtQ%3D%3D 3112578
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, R.J.1
  • 17
    • 0024314918 scopus 로고
    • 10.1016/0968-0004(89)90168-0 1:CAS:528:DyaL1MXlvV2ltrk%3D 2572080
    • R.J. Ellis S.M. Hemmingsen 1989 Trends Biochem. Sci. 14 339 342 10.1016/0968-0004(89)90168-0 1:CAS:528:DyaL1MXlvV2ltrk%3D 2572080
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 18
    • 0025382818 scopus 로고
    • 1:STN:280:DyaK3MzjvVOntg%3D%3D 1983265
    • R.J. Ellis 1990 Semin. Cell. Biol. 1 1 9 1:STN:280:DyaK3MzjvVOntg%3D%3D 1983265
    • (1990) Semin. Cell. Biol. , vol.1 , pp. 1-9
    • Ellis, R.J.1
  • 19
    • 0018221572 scopus 로고
    • 10.1038/275416a0 1:CAS:528:DyaE1MXhvVWktbs%3D 692721
    • R.A. Laskey B.M. Honda A.D. Mills J.T. Finch 1978 Nature 275 416 420 10.1038/275416a0 1:CAS:528:DyaE1MXhvVWktbs%3D 692721
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 20
    • 33745829795 scopus 로고    scopus 로고
    • Molecular chaperones: Assisting assembly in addition to folding
    • DOI 10.1016/j.tibs.2006.05.001, PII S0968000406001228
    • R.J. Ellis 2006 Trends Biochem. Sci. 31 395 401 10.1016/j.tibs.2006.05. 001 1:CAS:528:DC%2BD28XntFWrsL0%3D 16716593 (Pubitemid 44038913)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.7 , pp. 395-401
    • Ellis, R.J.1
  • 21
    • 25444522227 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD2MXlt1ygsb0%3D 15943899
    • S. Lee F.T. Tsai 2005 J. Biochem. Mol. Biol. 38 259 265 1:CAS:528:DC%2BD2MXlt1ygsb0%3D 15943899
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 259-265
    • Lee, S.1    Tsai, F.T.2
  • 22
    • 33646127577 scopus 로고    scopus 로고
    • 10.1016/j.cell.2006.04.014 1:CAS:528:DC%2BD28XkslCjtLw%3D 16678092
    • B. Bukau J. Weissman A. Horwich 2006 Cell 125 443 451 10.1016/j.cell.2006.04.014 1:CAS:528:DC%2BD28XkslCjtLw%3D 16678092
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 23
    • 39449097830 scopus 로고    scopus 로고
    • Common and specific mechanisms of AAA+ proteins involved in protein quality control
    • DOI 10.1042/BST0360120
    • A. Mogk T. Haslberger P. Tessarz B. Bukau 2008 Biochem. Soc. Trans. 36 120 125 10.1042/BST0360120 1:CAS:528:DC%2BD1cXht1aju7w%3D 18208398 (Pubitemid 351269634)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.1 , pp. 120-125
    • Mogk, A.1    Haslberger, T.2    Tessarz, P.3    Bukau, B.4
  • 24
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • DOI 10.1038/sj.emboj.7601974, PII 7601974
    • T. Anelli R. Sitia 2008 EMBO J. 27 315 327 10.1038/sj.emboj.7601974 1:CAS:528:DC%2BD1cXhtVKktL4%3D 18216874 (Pubitemid 351161662)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 25
    • 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
    • P. Goloubinoff P. De Los Rios 2007 Trends Biochem. Sci. 32 372 380 10.1016/j.tibs.2007.06.008 1:CAS:528:DC%2BD2sXosF2jurw%3D 17629485 (Pubitemid 47126861)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.8 , pp. 372-380
    • Goloubinoff, P.1    Rios, P.D.L.2
  • 26
    • 39149143645 scopus 로고    scopus 로고
    • 10.1016/j.sbi.2007.11.006 1:CAS:528:DC%2BD1cXitVGitrc%3D 18242075
    • H.R. Saibil 2008 Curr. Opin. Struct. Biol. 18 35 42 10.1016/j.sbi.2007. 11.006 1:CAS:528:DC%2BD1cXitVGitrc%3D 18242075
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 27
    • 0035861999 scopus 로고    scopus 로고
    • Dynamic association of trigger factor with protein substrates
    • DOI 10.1006/jmbi.2000.5192
    • R. Maier C. Scholz F.X. Schmid 2001 J. Mol. Biol. 314 1181 1190 10.1006/jmbi.2000.5192 1:CAS:528:DC%2BD3MXptVOmu7k%3D 11743733 (Pubitemid 34073080)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.5 , pp. 1181-1190
    • Maier, R.1    Scholz, C.2    Schmid, F.X.3
  • 28
    • 17144403794 scopus 로고    scopus 로고
    • Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding
    • DOI 10.1074/jbc.M414151200
    • C.P. Liu S. Perrett J.M. Zhou 2005 J. Biol. Chem. 280 13315 13320 10.1074/jbc.M414151200 1:CAS:528:DC%2BD2MXivV2ksLo%3D 15632130 (Pubitemid 40517217)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13315-13320
    • Liu, C.-P.1    Perrett, S.2    Zhou, J.-M.3
  • 30
  • 32
    • 0029420098 scopus 로고
    • 1:CAS:528:DyaK2MXmt1Ogsbo%3D 9189717
    • S.G. Burston A.R. Clarke 1995 Essays Biochem. 29 125 136 1:CAS:528:DyaK2MXmt1Ogsbo%3D 9189717
    • (1995) Essays Biochem. , vol.29 , pp. 125-136
    • Burston, S.G.1    Clarke, A.R.2
  • 33
    • 17044387386 scopus 로고    scopus 로고
    • 10.1007/s00018-004-4464-6 1:CAS:528:DC%2BD2MXktlymt78%3D 15770419
    • M.P. Mayer B. Bukau 2005 Cell. Mol. Life Sci. 62 670 684 10.1007/s00018-004-4464-6 1:CAS:528:DC%2BD2MXktlymt78%3D 15770419
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 34
    • 35748962910 scopus 로고    scopus 로고
    • The Hsp70 chaperone machines of Escherichia coli: A paradigm for the repartition of chaperone functions
    • DOI 10.1111/j.1365-2958.2007.05961.x
    • P. Genevaux C. Georgopoulos W.L. Kelley 2007 Mol. Microbiol. 66 840 857 10.1111/j.1365-2958.2007.05961.x 1:CAS:528:DC%2BD2sXhtl2qs7jN 17919282 (Pubitemid 350050417)
    • (2007) Molecular Microbiology , vol.66 , Issue.4 , pp. 840-857
    • Genevaux, P.1    Georgopoulos, C.2    Kelley, W.L.3
  • 35
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • DOI 10.1038/sj.emboj.7601970, PII 7601970
    • K. Liberek A. Lewandowska S. Zietkiewicz 2008 EMBO J. 27 328 335 10.1038/sj.emboj.7601970 1:CAS:528:DC%2BD1cXhtVKktLo%3D 18216875 (Pubitemid 351161659)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 36
    • 44549085390 scopus 로고    scopus 로고
    • 10.1016/j.abb.2008.03.015 1:CAS:528:DC%2BD1cXmvFeksL0%3D 18395510
    • M.G. Bigotti A.R. Clarke 2008 Arch. Biochem. Biophys. 474 331 339 10.1016/j.abb.2008.03.015 1:CAS:528:DC%2BD1cXmvFeksL0%3D 18395510
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 331-339
    • Bigotti, M.G.1    Clarke, A.R.2
  • 37
    • 33746265142 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: Making the impossible, possible
    • DOI 10.1080/10409230600760382, PII M315627H22375T33
    • Z. Lin H.S. Rye 2006 Crit. Rev. Biochem. Mol. Biol. 41 211 239 10.1080/10409230600760382 1:CAS:528:DC%2BD28XptlCisbc%3D 16849107 (Pubitemid 44100582)
    • (2006) Critical Reviews in Biochemistry and Molecular Biology , vol.41 , Issue.4 , pp. 211-239
    • Lin, Z.1    Rye, H.2
  • 38
    • 61749094567 scopus 로고    scopus 로고
    • 10.1016/j.pbiomolbio.2008.10.007 1:CAS:528:DC%2BD1MXjtFOjtbc%3D 19027782
    • T.K. Chaudhuri V.K. Verma A. Maheshwari 2009 Prog. Biophys. Mol. Biol. 99 42 50 10.1016/j.pbiomolbio.2008.10.007 1:CAS:528:DC%2BD1MXjtFOjtbc%3D 19027782
    • (2009) Prog. Biophys. Mol. Biol. , vol.99 , pp. 42-50
    • Chaudhuri, T.K.1    Verma, V.K.2    Maheshwari, A.3
  • 39
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • DOI 10.1038/41944
    • Z. Xu A.L. Horwich P.B. Sigler 1997 Nature 388 741 750 10.1038/41944 1:CAS:528:DyaK2sXls1GltLo%3D 9285585 (Pubitemid 27375147)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 43
    • 0037418665 scopus 로고    scopus 로고
    • 14 at 2.0 a resolution
    • DOI 10.1016/S0022-2836(03)00184-0
    • J. Wang D.C. Boisvert 2003 J. Mol. Biol. 327 843 855 10.1016/S0022- 2836(03)00184-0 1:CAS:528:DC%2BD3sXitlWgsL4%3D 12654267 (Pubitemid 36315923)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.4 , pp. 843-855
    • Wang, J.1    Boisvert, D.C.2
  • 44
    • 0037926429 scopus 로고    scopus 로고
    • Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes
    • DOI 10.1093/emboj/cdg313
    • G.W. Farr W.A. Fenton T.K. Chaudhuri D.K. Clare H.R. Saibil A.L. Horwich 2003 EMBO J. 22 3220 3230 10.1093/emboj/cdg313 1:CAS:528:DC%2BD3sXltFyhsbs%3D 12839985 (Pubitemid 36834853)
    • (2003) EMBO Journal , vol.22 , Issue.13 , pp. 3220-3230
    • Farr, G.W.1    Fenton, W.A.2    Chaudhuri, T.K.3    Clare, D.K.4    Saibil, H.R.5    Horwich, A.L.6
  • 45
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • L.H. Pearl Ch. Prodromou 2006 Annu. Rev. Biochem. 75 271 294 10.1146/annurev.biochem.75.103004.142738 1:CAS:528:DC%2BD28XosVKhs78%3D 16756493 (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 46
    • 84934439633 scopus 로고    scopus 로고
    • 10.1007/978-0-387-39975-1-3 17205672
    • R. Zhao W.A. Houry 2007 Adv. Exp. Med. Biol. 594 27 36 10.1007/978-0-387-39975-1-3 17205672
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 27-36
    • Zhao, R.1    Houry, W.A.2
  • 47
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • DOI 10.1016/j.cell.2007.07.036, PII S0092867407009749
    • A.J. McClellan Y. Xia A.M. Deutschbauer R.W. Davis M. Gerstein J. Frydman 2007 Cell 131 121 135 10.1016/j.cell.2007.07.036 1:CAS:528:DC%2BD2sXht1CntLnK 17923092 (Pubitemid 47498528)
    • (2007) Cell , vol.131 , Issue.1 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 48
    • 41149111451 scopus 로고    scopus 로고
    • 10.1042/BJ20071640 1:CAS:528:DC%2BD1cXisVWgtrs%3D 18290764
    • L.H. Pearl Ch. Prodromou P. Workman 2008 Biochem. J. 410 439 453 10.1042/BJ20071640 1:CAS:528:DC%2BD1cXisVWgtrs%3D 18290764
    • (2008) Biochem. J. , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, Ch.2    Workman, P.3
  • 51
    • 0035718899 scopus 로고    scopus 로고
    • Structure, function, and mechanism of the Hsp90 molecular chaperone
    • DOI 10.1016/S0065-3233(01)59005-1
    • L.H. Pearl Ch. Prodromou 2001 Adv. Protein Chem. 59 157 186 10.1016/S0065-3233(01)59005-1 1:STN:280:DC%2BD387jtleiug%3D%3D 11868271 (Pubitemid 34169304)
    • (2001) Advances in Protein Chemistry , vol.59 , pp. 157-186
    • Pearl, L.H.1    Prodromou, C.2
  • 52
    • 20444371377 scopus 로고    scopus 로고
    • Constantly updated knowledge of Hsp90
    • DOI 10.1093/jb/mvi056
    • K. Terasawa M. Minami Y. Minami 2005 J. Biochem. 137 443 447 10.1093/jb/mvi056 1:CAS:528:DC%2BD2MXlt1Ors7Y%3D 15858167 (Pubitemid 40806042)
    • (2005) Journal of Biochemistry , vol.137 , Issue.4 , pp. 443-447
    • Terasawa, K.1    Minami, M.2    Minami, Y.3
  • 53
    • 34447649757 scopus 로고    scopus 로고
    • Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process
    • DOI 10.1016/j.jmb.2007.05.057, PII S0022283607007103
    • A. Lewandowska M. Matuszewska K. Liberek 2007 J. Mol. Biol. 371 800 811 10.1016/j.jmb.2007.05.057 1:CAS:528:DC%2BD2sXotlSjt7g%3D 17588600 (Pubitemid 47087823)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.3 , pp. 800-811
    • Lewandowska, A.1    Matuszewska, M.2    Liberek, K.3
  • 55
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • DOI 10.1016/j.jsb.2003.10.010, PII S1047847703002235
    • L.M. Iyer D.D. Leipe E.V. Koonin L. Aravind 2004 J. Struct. Biol. 146 11 31 10.1016/j.jsb.2003.10.010 1:CAS:528:DC%2BD2cXisVSmtro%3D 15037234 (Pubitemid 38369015)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 57
    • 0036914160 scopus 로고    scopus 로고
    • AAA proteins
    • DOI 10.1016/S0959-440X(02)00388-3
    • A.N. Lupas J. Martin 2002 Curr. Opin. Struct. Biol. 12 746 753 10.1016/S0959-440X(02)00388-3 1:CAS:528:DC%2BD38XpslSks7c%3D 12504679 (Pubitemid 36009491)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 746-753
    • Lupas, A.N.1    Martin, J.2
  • 58
  • 59
    • 36549048006 scopus 로고    scopus 로고
    • The AAA+ superfamily - a myriad of motions
    • DOI 10.1016/j.sbi.2007.09.012, PII S0959440X07001546, Catalysis and Regulation /Protein
    • P.A. Tucker L. Sallai 2007 Curr. Opin. Struct. Biol. 17 641 652 10.1016/j.sbi.2007.09.012 1:CAS:528:DC%2BD2sXhtlyktLvJ 18023171 (Pubitemid 350180410)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.6 , pp. 641-652
    • Tucker, P.A.1    Sallai, L.2
  • 61
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • DOI 10.1016/S0092-8674(03)00807-9
    • S. Lee M.E. Sowa Y.H. Watanabe P.B. Sigler W. Chiu M. Yoshida F.T. Tsai 2003 Cell 115 229 240 10.1016/S0092-8674(03)00807-9 1:CAS:528: DC%2BD3sXosFCqsLk%3D 14567920 (Pubitemid 37329586)
    • (2003) Cell , vol.115 , Issue.2 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.-H.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.F.7
  • 63
    • 67650331111 scopus 로고    scopus 로고
    • 10.1042/BJ20082238 1:CAS:528:DC%2BD1MXntFeqtb0%3D 19351326
    • Y.H. Watanabe Y. Nakazaki R. Suno M. Yoshida 2009 Biochem. J. 421 71 77 10.1042/BJ20082238 1:CAS:528:DC%2BD1MXntFeqtb0%3D 19351326
    • (2009) Biochem. J. , vol.421 , pp. 71-77
    • Watanabe, Y.H.1    Nakazaki, Y.2    Suno, R.3    Yoshida, M.4
  • 64
    • 39449097830 scopus 로고    scopus 로고
    • Common and specific mechanisms of AAA+ proteins involved in protein quality control
    • DOI 10.1042/BST0360120
    • A. Mogk T. Haslberger P. Tessarz B. Bukau 2008 Biochem. Soc. Trans. 36 120 125 10.1042/BST0360120 1:CAS:528:DC%2BD1cXht1aju7w%3D 18208398 (Pubitemid 351269634)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.1 , pp. 120-125
    • Mogk, A.1    Haslberger, T.2    Tessarz, P.3    Bukau, B.4
  • 66
    • 0036809333 scopus 로고    scopus 로고
    • 10.1007/PL00012492 1:CAS:528:DC%2BD38XovVOntbY%3D 12475175
    • M. Haslbeck 2002 Cell. Mol. Life Sci. 59 1649 1657 10.1007/PL00012492 1:CAS:528:DC%2BD38XovVOntbY%3D 12475175
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1649-1657
    • Haslbeck, M.1
  • 68
    • 33846945050 scopus 로고    scopus 로고
    • 10.1007/s00018-006-6321-2 1:CAS:528:DC%2BD2sXjtlSrsrY%3D 17187175
    • H. Nakamoto L. Vigh 2007 Cell. Mol. Life Sci. 64 294 306 10.1007/s00018-006-6321-2 1:CAS:528:DC%2BD2sXjtlSrsrY%3D 17187175
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 69
    • 0033953974 scopus 로고    scopus 로고
    • Protein folding in vivo: The importance of molecular chaperones
    • DOI 10.1016/S0959-440X(99)00044-5
    • D.E. Feldman J. Frydman 2000 Curr. Opin. Struct. Biol. 10 26 33 10.1016/S0959-440X(99)00044-5 1:CAS:528:DC%2BD3cXhs1Sltro%3D 10679467 (Pubitemid 30099323)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 26-33
    • Feldman, D.E.1    Frydman, J.2
  • 70
    • 0034856940 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding in the cell cytoplasm
    • DOI 10.2174/1389203013381134
    • W.A. Houry 2001 Curr. Prot. Pept. Sci. 2 227 244 10.2174/1389203013381134 1:CAS:528:DC%2BD3MXmt1Shs7k%3D (Pubitemid 32798793)
    • (2001) Current Protein and Peptide Science , vol.2 , Issue.3 , pp. 227-244
    • Houry, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.