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Volumn 427, Issue 2, 2015, Pages 312-327

Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation

Author keywords

GrpE; Hsp40; Molecular chaperone; Nucleotide exchange factor; Protein disaggregation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; BACTERIAL PROTEIN; BETA GALACTOSIDASE; CHAPERONE; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MALATE DEHYDROGENASE; MONOMER; PROTEIN CLPB; PROTEIN DNAK; PROTEIN GRPE; UNCLASSIFIED DRUG; CLPB PROTEIN, E COLI; DNAK PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; GRPE PROTEIN, E COLI; HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; PROTEIN AGGREGATE; SACCHAROMYCES CEREVISIAE PROTEIN; SSA1 PROTEIN, S CEREVISIAE;

EID: 84920812183     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.10.013     Document Type: Article
Times cited : (53)

References (65)
  • 1
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005;62:670-84.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 4
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010;11:579-92.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 5
    • 0344875614 scopus 로고    scopus 로고
    • GrpE, A nucleotide exchange factor for DnaK
    • Harrison C. GrpE, a nucleotide exchange factor for DnaK. Cell Stress Chaperones 2003;8:218-24.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 218-224
    • Harrison, C.1
  • 6
    • 79957730170 scopus 로고    scopus 로고
    • Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
    • Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci USA 2011;108:8206-11.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 8206-8211
    • Genest, O.1    Hoskins, J.R.2    Camberg, J.L.3    Doyle, S.M.4    Wickner, S.5
  • 7
    • 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. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 1999;96:13732-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 8
    • 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;274:28083-6.
    • (1999) J Biol Chem , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 9
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB. Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein. Nature 1990;346:623-8.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 12
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 1997;276:431-5.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 14
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
    • Kityk R, Kopp J, Sinning I, Mayer MP. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell 2012;48:863-74.
    • (2012) Mol Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 15
    • 84880167772 scopus 로고    scopus 로고
    • Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
    • Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, et al. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat Struct Mol Biol 2013;20:900-7.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 900-907
    • Qi, R.1    Sarbeng, E.B.2    Liu, Q.3    Le, K.Q.4    Xu, X.5    Xu, H.6
  • 16
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 2012;151:1296-307.
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 17
    • 79955565642 scopus 로고    scopus 로고
    • Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
    • Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci USA 2011;108:6987-92.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6987-6992
    • Zhuravleva, A.1    Gierasch, L.M.2
  • 18
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. Coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci USA 2009;106:8471-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.4
  • 19
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • Schlecht R, Erbse AH, Bukau B, Mayer MP. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol 2011;18:345-51.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 20
    • 79959685900 scopus 로고    scopus 로고
    • Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding
    • Schweizer RS, Aponte RA, Zimmermann S, Weber A, Reinstein J. Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding. Chembiochem 2011;12:1559-73.
    • (2011) Chembiochem , vol.12 , pp. 1559-1573
    • Schweizer, R.S.1    Aponte, R.A.2    Zimmermann, S.3    Weber, A.4    Reinstein, J.5
  • 21
    • 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
  • 22
    • 84886446627 scopus 로고    scopus 로고
    • Protein rescue from aggregates by powerful molecular chaperone machines
    • Doyle SM, Genest O, Wickner S. Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol 2013;14:617-29.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 617-629
    • Doyle, S.M.1    Genest, O.2    Wickner, S.3
  • 23
    • 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;489:92-6.
    • (2001) FEBS Lett , vol.489 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 24
    • 84874393637 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
    • Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science 2013. http://dx.doi.org/10.1126/science.1233066.
    • (2013) Science
    • Rosenzweig, R.1    Moradi, S.2    Zarrine-Afsar, A.3    Glover, J.R.4    Kay, L.E.5
  • 25
    • 79955563304 scopus 로고    scopus 로고
    • Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
    • Miot M, Reidy M, Doyle SM, Hoskins JR, Johnston DM, Genest, et al. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci USA 2011;108:6915-20.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6915-6920
    • Miot, M.1    Reidy, M.2    Doyle, S.M.3    Hoskins, J.R.4    Genest, J.D.M.5
  • 26
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA + disaggregase at aggregate surfaces
    • Seyffer F, Kummer E, Oguchi Y, Winkler J, Kumar M, Zahn R, et al. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA + disaggregase at aggregate surfaces. Nat Struct Mol Biol 2012;19:1347-55.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1347-1355
    • Seyffer, F.1    Kummer, E.2    Oguchi, Y.3    Winkler, J.4    Kumar, M.5    Zahn, R.6
  • 28
    • 84866083679 scopus 로고    scopus 로고
    • Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions
    • Reidy M, Miot M, Masison DC. Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 2012;192:185-93.
    • (2012) Genetics , vol.192 , pp. 185-193
    • Reidy, M.1    Miot, M.2    Masison, D.C.3
  • 29
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
    • Kabani M, Beckerich JM, Brodsky JL. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 2002;22:4677-89.
    • (2002) Mol Cell Biol , vol.22 , pp. 4677-4689
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 30
    • 0029126927 scopus 로고
    • Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones andmodulators
    • Levy EJ, McCarty J, Bukau B, Chirico WJ. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones andmodulators. FEBS Lett 1995;368:435-40.
    • (1995) FEBS Lett , vol.368 , pp. 435-440
    • Levy, E.J.1    McCarty, J.2    Bukau, B.3    Chirico, W.J.4
  • 31
    • 34547455220 scopus 로고    scopus 로고
    • Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system
    • Doyle SM, Hoskins JR, Wickner S. Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system. Proc Natl Acad Sci USA 2007;104:11138-44.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11138-11144
    • Doyle, S.M.1    Hoskins, J.R.2    Wickner, S.3
  • 32
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA 1998;95:5752-6.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 33
    • 0042858475 scopus 로고    scopus 로고
    • Characterization of a trap mutant of the AAA+ chaperone ClpB
    • Weibezahn J, Schlieker C, Bukau B, Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem 2003;278:32608-17.
    • (2003) J Biol Chem , vol.278 , pp. 32608-32617
    • Weibezahn, J.1    Schlieker, C.2    Bukau, B.3    Mogk, A.4
  • 35
    • 0027371807 scopus 로고
    • 2+ in RepA monomerization by DnaJ and DnaK
    • 2+ in RepA monomerization by DnaJ and DnaK. J Biol Chem 1993;268:25296-301.
    • (1993) J Biol Chem , vol.268 , pp. 25296-25301
    • Skowyra, D.1    Wickner, S.2
  • 36
    • 51149100951 scopus 로고    scopus 로고
    • The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division
    • Sugimoto S, Saruwatari K, Higashi C, Sonomoto K. The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division. Microbiology 2008;154:1876-85.
    • (2008) Microbiology , vol.154 , pp. 1876-1885
    • Sugimoto, S.1    Saruwatari, K.2    Higashi, C.3    Sonomoto, K.4
  • 38
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 1997;36:3417-22.
    • (1997) Biochemistry , vol.36 , pp. 3417-3422
    • Packschies, L.1    Theyssen, H.2    Buchberger, A.3    Bukau, B.4    Goody, R.S.5    Reinstein, J.6
  • 40
    • 77956178634 scopus 로고    scopus 로고
    • The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner
    • Sielaff B, Tsai FT. The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol 2010;402:30-7.
    • (2010) J Mol Biol , vol.402 , pp. 30-37
    • Sielaff, B.1    Tsai, F.T.2
  • 42
    • 21244497886 scopus 로고    scopus 로고
    • Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104
    • Haslbeck M, Miess A, Stromer T, Walter S, Buchner J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 2005;280:23861-8.
    • (2005) J Biol Chem , vol.280 , pp. 23861-23868
    • Haslbeck, M.1    Miess, A.2    Stromer, T.3    Walter, S.4    Buchner, J.5
  • 43
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, et al. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 2003;115:229-40.
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.H.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6
  • 44
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ. ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 2004;20:45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 45
    • 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
    • Desantis ME, Sweeny EA, Snead D, Leung EH, Go MS, Gupta K, et al. 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 2014;289:848-67.
    • (2014) J Biol Chem , vol.289 , 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
  • 47
    • 84899854286 scopus 로고    scopus 로고
    • Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
    • Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, et al. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. eLife 2014;3:e02481.
    • (2014) eLife , vol.3 , pp. e02481
    • Carroni, M.1    Kummer, E.2    Oguchi, Y.3    Wendler, P.4    Clare, D.K.5    Sinning, I.6
  • 48
    • 33750479525 scopus 로고    scopus 로고
    • Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism
    • Battesti A, Bouveret E. Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism. Mol Microbiol 2006;62:1048-63.
    • (2006) Mol Microbiol , vol.62 , pp. 1048-1063
    • Battesti, A.1    Bouveret, E.2
  • 49
    • 0025788990 scopus 로고
    • Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin
    • Wickner S, Hoskins J, McKenney K. Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. Proc Natl Acad Sci USA 1991;88:7903-7.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7903-7907
    • Wickner, S.1    Hoskins, J.2    McKenney, K.3
  • 50
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • Hoskins JR, Singh SK, Maurizi MR, Wickner S. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc Natl Acad Sci USA 2000;97:8892-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1    Singh, S.K.2    Maurizi, M.R.3    Wickner, S.4
  • 51
    • 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;41:11277-83.
    • (2002) Biochemistry , vol.41 , pp. 11277-11283
    • Barnett, M.E.1    Zolkiewski, M.2
  • 52
    • 0026739395 scopus 로고
    • Regulation of Hsp70 function by a eukaryotic DnaJ homolog
    • Cyr DM, Lu X, Douglas MG. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J Biol Chem 1992;267:20927-31.
    • (1992) J Biol Chem , vol.267 , pp. 20927-20931
    • Cyr, D.M.1    Lu, X.2    Douglas, M.G.3
  • 53
    • 0021169352 scopus 로고
    • Energy consumption in a cyclic phosphorylation/dephosphorylation cascade
    • Shacter E, Chock PB, Stadtman ER. Energy consumption in a cyclic phosphorylation/dephosphorylation cascade. J Biol Chem 1984;259:12260-4.
    • (1984) J Biol Chem , vol.259 , pp. 12260-12264
    • Shacter, E.1    Chock, P.B.2    Stadtman, E.R.3
  • 54
    • 0015340985 scopus 로고
    • Detection and isolation of the repressor protein for the tryptophan operon of Escherichia coli
    • Zubay G, Morse DE, Schrenk WJ, Miller JH. Detection and isolation of the repressor protein for the tryptophan operon of Escherichia coli. Proc Natl Acad Sci USA 1972;69:1100-3.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 1100-1103
    • Zubay, G.1    Morse, D.E.2    Schrenk, W.J.3    Miller, J.H.4
  • 55
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008;9:40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 58
    • 70350772363 scopus 로고    scopus 로고
    • Structures of asymmetric ClpX hexamers reveal nucleotidedependent motions in a AAA+ protein-unfolding machine
    • Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT. Structures of asymmetric ClpX hexamers reveal nucleotidedependent motions in a AAA+ protein-unfolding machine. Cell 2009;139:744-56.
    • (2009) Cell , vol.139 , pp. 744-756
    • Glynn, S.E.1    Martin, A.2    Nager, A.R.3    Baker, T.A.4    Sauer, R.T.5
  • 62
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFT-based protein docking program with pairwise potentials
    • Kozakov D, Brenke R, Comeau SR, Vajda S. PIPER: an FFT-based protein docking program with pairwise potentials. Proteins 2006;65:392-406.
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 63
    • 33846200437 scopus 로고    scopus 로고
    • Prediction-based fingerprints of protein-protein interactions
    • Porollo A, Meller J. Prediction-based fingerprints of protein-protein interactions. Proteins 2007;66:630-45.
    • (2007) Proteins , vol.66 , pp. 630-645
    • Porollo, A.1    Meller, J.2
  • 64
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2


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