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Volumn 3, Issue , 2004, Pages

Unscrambling an egg: Protein disaggregation by AAA+ proteins

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; PROTEINASE;

EID: 2942596463     PISSN: 14752859     EISSN: None     Source Type: Journal    
DOI: 10.1186/1475-2859-3-1     Document Type: Review
Times cited : (67)

References (93)
  • 1
    • 0025869880 scopus 로고
    • Inside a living cell
    • Goodsell DS: Inside a living cell. TiBS 1991, 16:203-206.
    • (1991) TiBS , vol.16 , pp. 203-206
    • Goodsell, D.S.1
  • 3
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M: Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito RR, Sitia R: Aggresomes and Russell bodies. Symptoms of cellular indigestion? EMBO Rep 2000, 1:225-231.
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 5
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez Y, Lindquist SL: HSP104 required for induced thermotolerance. Science 1990, 248:1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 7
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S: Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994, 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 8
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B: Identification of thermolabile E. coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 1999, 18:6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Röder, D.5    Langen, H.6    Bukau, B.7
  • 9
    • 0029835946 scopus 로고    scopus 로고
    • The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria
    • Schmitt M, Neupert W, Langer T: The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 1996, 134:1375-1386.
    • (1996) J. Cell Biol. , vol.134 , pp. 1375-1386
    • Schmitt, M.1    Neupert, W.2    Langer, T.3
  • 10
    • 0034119621 scopus 로고    scopus 로고
    • Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch C, Hong SW, Vierling E, Lindquist S: Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 2000, 12:479-492.
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1    Hong, S.W.2    Vierling, E.3    Lindquist, S.4
  • 11
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with ClpA, ClpB, and HtpG in vivo
    • Thomas JG, Baneyx F: Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo. J. Bacteriol. 1998, 180:5165-5172.
    • (1998) J. Bacteriol. , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 12
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
    • Laskowska E, Kuczynska-Wisnik D, Skórko-Glonek J, Taylor A: Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Mol. Microbiol. 1996, 22:555-571.
    • (1996) Mol. Microbiol. , vol.22 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skórko-Glonek, J.3    Taylor, A.4
  • 13
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong SW, Vierling E: Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc Natl Acad Sci U S A 2000, 97:4392-4397.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 15
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV: AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 1999, 9:27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 16
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure - Diverse function
    • Ogura T, Wilkinson AJ: AAA+ superfamily ATPases: common structure - diverse function. Genes Cells 2001, 6:575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 17
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale RD: AAA proteins. Lords of the ring. J Cell Biol 2000, 150:F13-9.
    • (2000) J. Cell Biol. , vol.150
    • Vale, R.D.1
  • 18
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo F, Maurizi MR, Esser L, Xia D: Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J Biol Chem 2002, 277:46743-46752.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 20
    • 0037053443 scopus 로고    scopus 로고
    • Crystal structure of E. coli Hsp100 ClpB nucleotidebinding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity
    • Li J, Sha B: Crystal structure of E. coli Hsp100 ClpB nucleotidebinding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity. J Mol Biol 2002, 318:1127-1137.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1127-1137
    • Li, J.1    Sha, B.2
  • 21
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATPdependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu RC, Hanson PI, Jahn R, Brunger AT: Structure of the ATPdependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat Struct Biol 1998, 5:803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 22
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimidesensitive fusion protein
    • Lenzen CU, Steinmann D, Whiteheart SW, Weis WI: Crystal structure of the hexamerization domain of N-ethylmaleimidesensitive fusion protein. Cell 1998, 94:525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 24
    • 0142227208 scopus 로고    scopus 로고
    • The Structure of ClpB. A Molecular Chaperone that Rescues Proteins from an Aggregated State
    • Lee S, Sowa ME, Watanabe Y, Sigler PB, Chiu W, Yoshida M, Tsai FT: The Structure of ClpB. A Molecular Chaperone that Rescues Proteins from an Aggregated State. Cell 2003, 115:229-240.
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.7
  • 25
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • Watanabe YH, Motohashi K, Yoshida M: Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J Biol Chem 2002, 277:5804-5809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5804-5809
    • Watanabe, Y.H.1    Motohashi, K.2    Yoshida, M.3
  • 26
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity
    • Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B: Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity. J Biol Chem 2003, 278:15-24.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15-24
    • Mogk, A.1    Schlieker, C.2    Strub, C.3    Rist, W.4    Weibezahn, J.5    Bukau, B.6
  • 27
    • 0032546911 scopus 로고    scopus 로고
    • The ATPase Activity of Hsp104, Effects of Environmental Conditions and Mutations
    • Schirmer EC, Queitsch C, Kowal AS, Parsell DA, Lindquist S: The ATPase Activity of Hsp104, Effects of Environmental Conditions and Mutations. J. Biol. Chem. 1998, 273:15546-15552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15546-15552
    • Schirmer, E.C.1    Queitsch, C.2    Kowal, A.S.3    Parsell, D.A.4    Lindquist, S.5
  • 29
    • 0037125945 scopus 로고    scopus 로고
    • Site-Directed Mutagenesis of Conserved Charged Amino Acid Residues in ClpB from Escherichia coli(,)
    • Barnett ME, Zolkiewski M: Site-Directed Mutagenesis of Conserved Charged Amino Acid Residues in ClpB from Escherichia coli(,). Biochemistry 2002, 41:11277-11283.
    • (2002) Biochemistry , vol.41 , pp. 11277-11283
    • Barnett, M.E.1    Zolkiewski, M.2
  • 30
    • 0037080611 scopus 로고    scopus 로고
    • Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
    • Hattendorf DA, Lindquist SL: Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. Embo J 2002, 21:12-21.
    • (2002) Embo J. , vol.21 , pp. 12-21
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 31
    • 0035793721 scopus 로고    scopus 로고
    • The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
    • Schlee S, Groemping Y, Herde P, Seidel R, Reinstein J: The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J Mol Biol 2001, 306:889-899.
    • (2001) J. Mol. Biol. , vol.306 , pp. 889-899
    • Schlee, S.1    Groemping, Y.2    Herde, P.3    Seidel, R.4    Reinstein, J.5
  • 32
    • 0037336274 scopus 로고    scopus 로고
    • Crystal Structure of the E. coli Hsp100 ClpB N-Terminal Domain
    • Li J, Sha B: Crystal Structure of the E. coli Hsp100 ClpB N-Terminal Domain. Structure (Camb) 2003, 11:323-328.
    • (2003) Structure (Camb.) , vol.11 , pp. 323-328
    • Li, J.1    Sha, B.2
  • 33
    • 0036349911 scopus 로고    scopus 로고
    • Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity
    • Liu Z, Tek V, Akoev V, Zolkiewski M: Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity. J Mol Biol 2002, 321:111-120.
    • (2002) J. Mol. Biol. , vol.321 , pp. 111-120
    • Liu, Z.1    Tek, V.2    Akoev, V.3    Zolkiewski, M.4
  • 34
    • 0037033053 scopus 로고    scopus 로고
    • The N Terminus of ClpB from Thermus thermophilus Is Not Essential for the Chaperone Activity
    • Beinker P, Schlee S, Groemping Y, Seidel R, Reinstein J: The N Terminus of ClpB from Thermus thermophilus Is Not Essential for the Chaperone Activity. J Biol Chem 2002, 277:47160-47166.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47160-47166
    • Beinker, P.1    Schlee, S.2    Groemping, Y.3    Seidel, R.4    Reinstein, J.5
  • 35
    • 0034462084 scopus 로고    scopus 로고
    • The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Clarke AK, Eriksson MJ: The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. J Bacteriol 2000, 182:7092-7096.
    • (2000) J. Bacteriol. , vol.182 , pp. 7092-7096
    • Clarke, A.K.1    Eriksson, M.J.2
  • 40
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S: Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 41
    • 85047686128 scopus 로고    scopus 로고
    • Crowbars and ratchets: Hsp100 chaperones as tools in reversing protein aggregation
    • Glover JR, Tkach JM: Crowbars and ratchets: hsp100 chaperones as tools in reversing protein aggregation. Biochem Cell Biol 2001, 79:557-568.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 557-568
    • Glover, J.R.1    Tkach, J.M.2
  • 44
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease, FtsH, are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa T, Okuno T, Karata K, Yamanaka K, Ogura T: Conserved pore residues in the AAA protease, FtsH, are important for proteolysis and its coupling to ATP hydrolysis. J Biol Chem 2003.
    • (2003) J. Biol. Chem.
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5
  • 45
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Peres Ben Zvi A, Tomoyasu T, Bukau B: Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 1999, 96:13732-13737.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Peres Ben Zvi, A.3    Tomoyasu, T.4    Bukau, B.5
  • 46
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • Motohashi K, Watanabe Y, Yohda M, Yoshida M: Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 1999, 96:7184-7189.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 47
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski M: ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 1999, 274:28083-28086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 48
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P: Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem 2000, 275:21107-21113.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21107-21113
    • Diamant, S.1    Ben-Zvi, A.P.2    Bukau, B.3    Goloubinoff, P.4
  • 49
    • 0035951385 scopus 로고    scopus 로고
    • Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
    • Krzewska J, Langer T, Liberek K: Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 2001, 489:92-96.
    • (2001) FEBS Lett. , vol.489 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 51
    • 0036896886 scopus 로고    scopus 로고
    • Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
    • Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA: Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat Struct Biol 2002, 9:906-911.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 906-911
    • Zeth, K.1    Ravelli, R.B.2    Paal, K.3    Cusack, S.4    Bukau, B.5    Dougan, D.A.6
  • 52
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynów A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M: The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 1995, 14:1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynów, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 53
    • 0025337699 scopus 로고
    • Suppression of early competence mutations in Bacillus subtilis by mec mutations
    • Roggiani M, Hahn J, Dubnau D: Suppression of early competence mutations in Bacillus subtilis by mec mutations. J Bacteriol 1990, 172:4056-4063.
    • (1990) J. Bacteriol. , vol.172 , pp. 4056-4063
    • Roggiani, M.1    Hahn, J.2    Dubnau, D.3
  • 54
    • 0031030242 scopus 로고    scopus 로고
    • Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis
    • Turgay K, Hamoen LW, Venema G, Dubnau D: Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis. Genes Dev 1997, 11:119-128.
    • (1997) Genes Dev. , vol.11 , pp. 119-128
    • Turgay, K.1    Hamoen, L.W.2    Venema, G.3    Dubnau, D.4
  • 55
    • 0032538886 scopus 로고    scopus 로고
    • Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
    • Turgay K, Hahn J, Burghoorn J, Dubnau D: Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 1998, 17:6730-6738.
    • (1998) EMBO J. , vol.17 , pp. 6730-6738
    • Turgay, K.1    Hahn, J.2    Burghoorn, J.3    Dubnau, D.4
  • 56
    • 0028290369 scopus 로고
    • Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance
    • Kruger E, Volker U, Hecker M: Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance. J Bacteriol 1994, 176:3360-3367.
    • (1994) J. Bacteriol. , vol.176 , pp. 3360-3367
    • Kruger, E.1    Volker, U.2    Hecker, M.3
  • 57
    • 0028284792 scopus 로고
    • MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a pleiotropic regulator controlling competence gene expression and growth at high temperature
    • Msadek T, Kunst F, Rapoport G: MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a pleiotropic regulator controlling competence gene expression and growth at high temperature. Proc Natl Acad Sci U S A 1994, 91:5788-5792.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 5788-5792
    • Msadek, T.1    Kunst, F.2    Rapoport, G.3
  • 58
    • 0034072580 scopus 로고    scopus 로고
    • The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins
    • Kruger E, Witt E, Ohlmeier S, Hanschke R, Hecker M: The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins. J Bacteriol 2000, 182:3259-3265.
    • (2000) J. Bacteriol. , vol.182 , pp. 3259-3265
    • Kruger, E.1    Witt, E.2    Ohlmeier, S.3    Hanschke, R.4    Hecker, M.5
  • 59
    • 0035073906 scopus 로고    scopus 로고
    • Proteome and transcriptome based analysis of Bacillus subtilis cells overproducing an insoluble heterologous protein
    • Jurgen B, Hanschke R, Sarvas M, Hecker M, Schweder T: Proteome and transcriptome based analysis of Bacillus subtilis cells overproducing an insoluble heterologous protein. Appl Microbiol Biotechnol 2001, 55:326-332.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 326-332
    • Jurgen, B.1    Hanschke, R.2    Sarvas, M.3    Hecker, M.4    Schweder, T.5
  • 61
    • 0032796135 scopus 로고    scopus 로고
    • The N and the C-terminal domains of MecA recognize different partners in the competence molecular switch
    • Persuh M, Turgay K, Mandic-Mulec I, Dubnau D: The N and the C-terminal domains of MecA recognize different partners in the competence molecular switch. Mol. Microbiol. 1999, 33:886-894.
    • (1999) Mol. Microbiol. , vol.33 , pp. 886-894
    • Persuh, M.1    Turgay, K.2    Mandic-Mulec, I.3    Dubnau, D.4
  • 62
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor JP, Hardy J, Fischbeck KH: Toxic proteins in neurodegenerative disease. Science 2002, 296:1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 63
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz Max F., Johnson Tony, Suzuki Masashi, Finch John T.: Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA 1994, 91:5355-5358.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 64
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S, Lindquist S: Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci U S A 2000, 97:1589-1594.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 65
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • Lunkes A, Mandel JL: A cellular model that recapitulates major pathogenic steps of Huntington's disease. Hum Mol Genet 1998, 7:1355-1361.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1355-1361
    • Lunkes, A.1    Mandel, J.L.2
  • 69
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto A, Lucas JJ, Hen R: Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 2000, 101:57-66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 70
    • 0034160086 scopus 로고    scopus 로고
    • Protein-only inheritance in yeast: Something to get [PSI+]-ched about
    • Serio TR, Lindquist SL: Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol 2000, 10:98-105.
    • (2000) Trends Cell Biol. , vol.10 , pp. 98-105
    • Serio, T.R.1    Lindquist, S.L.2
  • 71
    • 0029052468 scopus 로고
    • Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-like Factor [psi+]
    • Chernoff Yury O., Lindquist Susan L., Ono Bun-ichiro, Inge-Vechtomov Sergei G., Liebman Susan W.: Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-like Factor [psi+]. Science 1995, 268:880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.-I.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 72
    • 0032503963 scopus 로고    scopus 로고
    • Structure and Replication of Yeast Prions
    • Kushnirov VV, Ter-Avanesyan MD: Structure and Replication of Yeast Prions. Cell 1998, 94:13-16.
    • (1998) Cell , vol.94 , pp. 13-16
    • Kushnirov, V.V.1    Ter-Avanesyan, M.D.2
  • 73
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H, Breuer P, Hayer-Hartl MK, Hartl FU: Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci U S A 2002, 99 Suppl 4:16412-16418.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 74
    • 0242635839 scopus 로고    scopus 로고
    • p97, a protein coping with multiple identities
    • Woodman PG: p97, a protein coping with multiple identities. J Cell Sci 2003, 116:4283-4290.
    • (2003) J. Cell Sci. , vol.116 , pp. 4283-4290
    • Woodman, P.G.1
  • 78
    • 0042326841 scopus 로고    scopus 로고
    • Characterization of human torsinA and its dystonia-associated mutant form
    • Liu Z, Zolkiewska A, Zolkiewski M: Characterization of human torsinA and its dystonia-associated mutant form. Biochem J 2003, 374:117-122.
    • (2003) Biochem. J. , vol.374 , pp. 117-122
    • Liu, Z.1    Zolkiewska, A.2    Zolkiewski, M.3
  • 79
    • 0034623158 scopus 로고    scopus 로고
    • Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations
    • Kustedjo K, Bracey MH, Cravatt BF: Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. J Biol Chem 2000, 275:27933-27939.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27933-27939
    • Kustedjo, K.1    Bracey, M.H.2    Cravatt, B.F.3
  • 82
    • 0035404388 scopus 로고    scopus 로고
    • A close association of torsinA and alpha-synuclein in Lewy bodies: A fluorescence resonance energy transfer study
    • Sharma N, Hewett J, Ozelius LJ, Ramesh V, McLean PJ, Breakefield XO, Hyman BT: A close association of torsinA and alpha-synuclein in Lewy bodies: a fluorescence resonance energy transfer study. Am J Pathol 2001, 159:339-344.
    • (2001) Am. J. Pathol. , vol.159 , pp. 339-344
    • Sharma, N.1    Hewett, J.2    Ozelius, L.J.3    Ramesh, V.4    McLean, P.J.5    Breakefield, X.O.6    Hyman, B.T.7
  • 83
    • 0037319121 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced protein aggregation in Caenorhabditis elegans by torsin proteins
    • Caldwell GA, Cao S, Sexton EG, Gelwix CC, Bevel JP, Caldwell KA: Suppression of polyglutamine-induced protein aggregation in Caenorhabditis elegans by torsin proteins. Hum Mol Genet 2003, 12:307-319.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 307-319
    • Caldwell, G.A.1    Cao, S.2    Sexton, E.G.3    Gelwix, C.C.4    Bevel, J.P.5    Caldwell, K.A.6
  • 84
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY: Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nature Genetics 1998, 19:148-154.
    • (1998) Nature Genetics , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 85
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S, Boeddrich A, Lurz R, Scherzinger E, Lueder G, Lehrach H, Wanker EE: Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell 2001, 12:1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 86
  • 87
    • 0031157025 scopus 로고    scopus 로고
    • Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold
    • Thomas JG, Ayling A, Baneyx F: Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold. Appl Biochem Biotechnol 1997, 66:197-238.
    • (1997) Appl. Biochem. Biotechnol. , vol.66 , pp. 197-238
    • Thomas, J.G.1    Ayling, A.2    Baneyx, F.3
  • 88
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B: Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 2001, 40:397-413.
    • (2001) Mol. Microbiol. , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 89
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carrio MM, Villaverde A: Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett 2001, 489:29-33.
    • (2001) FEBS Lett. , vol.489 , pp. 29-33
    • Carrio, M.M.1    Villaverde, A.2
  • 90
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I, Seidel M, Sauer RT, Baker TA: A specificity-enhancing factor for the ClpXP degradation machine. Science 2000, 289:2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 91
    • 0035281566 scopus 로고    scopus 로고
    • The RssB response regulator directly targets sigma(S) for degradation by ClpXP
    • Zhou Y, Gottesman S, Hoskins JR, Maurizi MR, Wickner S: The RssB response regulator directly targets sigma(S) for degradation by ClpXP. Genes Dev 2001, 15:627-637.
    • (2001) Genes Dev. , vol.15 , pp. 627-637
    • Zhou, Y.1    Gottesman, S.2    Hoskins, J.R.3    Maurizi, M.R.4    Wickner, S.5
  • 92
    • 0034596991 scopus 로고    scopus 로고
    • Subunit-specific degradation of the UmuD/D′ heterodimer by the ClpXP protease: The role of trans recognition in UmuD' stability
    • Gonzalez M, Rasulova F, Maurizi MR, Woodgate R: Subunit-specific degradation of the UmuD/D′ heterodimer by the ClpXP protease: the role of trans recognition in UmuD′ stability. Embo J 2000, 19:5251-5258.
    • (2000) Embo J. , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 93
    • 0345687188 scopus 로고    scopus 로고
    • Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate processing by the ClpXP protease
    • Neher SB, Sauer RT, Baker TA: Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate processing by the ClpXP protease. Proc Natl Acad Sci U S A 2003, 100:13219-13224.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 13219-13224
    • Neher, S.B.1    Sauer, R.T.2    Baker, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.