메뉴 건너뛰기




Volumn 344, Issue 6184, 2014, Pages

Structural basis for protein antiaggregation activity of the trigger factor chaperone

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; CHAPERONE; ESCHERICHIA COLI PROTEIN; INTRINSICALLY DISORDERED PROTEIN; PEPTIDE; PEPTIDYLPROLYL ISOMERASE; PHOA PROTEIN, E COLI;

EID: 84900336916     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1250494     Document Type: Article
Times cited : (225)

References (93)
  • 1
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • doi: 10.1016/j.cell.2006.04.014; pmid: 16678092
    • B. Bukau, J. Weissman, A. Horwich, Molecular chaperones and protein quality control. Cell 125, 443-451 (2006). doi: 10.1016/j.cell.2006.04.014; pmid: 16678092
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 2
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • doi: 10.1038/nsmb.1614; pmid: 19491936
    • G. Kramer, D. Boehringer, N. Ban, B. Bukau, The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 16, 589-597 (2009). doi: 10.1038/nsmb.1614; pmid: 19491936
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 3
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • doi: 10.1038/nsmb.1591; pmid: 19491934
    • F. U. Hartl, M. Hayer-Hartl, Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574-581 (2009). doi: 10.1038/nsmb.1591; pmid: 19491934
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 80053999780 scopus 로고    scopus 로고
    • Protein folding in the cell: An inside story
    • doi: 10.1038/nm.2468; pmid: 21989012
    • A. L. Horwich, Protein folding in the cell: An inside story. Nat. Med. 17, 1211-1216 (2011). doi: 10.1038/nm.2468; pmid: 21989012
    • (2011) Nat. Med. , vol.17 , pp. 1211-1216
    • Horwich, A.L.1
  • 5
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • doi: 10.1038/nature10317; pmid: 21776078
    • F. U. Hartl, A. Bracher, M. Hayer-Hartl, Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011). doi: 10.1038/nature10317; pmid: 21776078
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 6
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • doi: 10.1038/nrm3658; pmid: 24026055
    • H. Saibil, Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Cancer 13, 630-642 (2013). doi: 10.1038/nrm3658; pmid: 24026055
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 630-642
    • Saibil, H.1
  • 7
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • doi: 10.1126/science.1068408; pmid: 11884745
    • F. Hartl, M. Hayer-Hartl, Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295, 1852-1858 (2002). doi: 10.1126/science.1068408; pmid: 11884745
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.1    Hayer-Hartl, M.2
  • 8
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of chaperone-mediated protein folding in the cytosol
    • doi: 10.1038/nrm1492; pmid: 15459659
    • J. Young, V. Agashe, K. Siegers, F. Hartl, Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5, 781-791 (2004). doi: 10.1038/nrm1492; pmid: 15459659
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 781-791
    • Young, J.1    Agashe, V.2    Siegers, K.3    Hartl, F.4
  • 9
    • 84862848780 scopus 로고    scopus 로고
    • Ribosome-associated chaperones as key players in proteostasis
    • doi: 10.1016/j.tibs.2012.03.002; pmid: 22503700
    • S. Preissler, E. Deuerling, Ribosome-associated chaperones as key players in proteostasis. Trends Biochem. Sci. 37, 274-283 (2012). doi: 10.1016/j.tibs.2012.03.002; pmid: 22503700
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 274-283
    • Preissler, S.1    Deuerling, E.2
  • 10
    • 77953027489 scopus 로고    scopus 로고
    • Structure and function of the molecular chaperone Trigger Factor
    • doi: 10.1016/j.bbamcr.2010.01.017; pmid: 20132842
    • A. Hoffmann, B. Bukau, G. Kramer, Structure and function of the molecular chaperone Trigger Factor. Biochim. Biophys. Acta 1803, 650-661 (2010). doi: 10.1016/j.bbamcr.2010.01.017; pmid: 20132842
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 650-661
    • Hoffmann, A.1    Bukau, B.2    Kramer, G.3
  • 11
    • 0037068441 scopus 로고    scopus 로고
    • L23 protein functions as a chaperone docking site on the ribosome
    • doi: 10.1038/nature01047; pmid: 12226666
    • G. Kramer et al., L23 protein functions as a chaperone docking site on the ribosome. Nature 419, 171-174 (2002). doi: 10.1038/nature01047; pmid: 12226666
    • (2002) Nature , vol.419 , pp. 171-174
    • Kramer, G.1
  • 12
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • doi: 10.1038/nature02899; pmid: 15334087
    • L. Ferbitz et al., Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431, 590-596 (2004). doi: 10.1038/nature02899; pmid: 15334087
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1
  • 13
    • 24744435971 scopus 로고    scopus 로고
    • Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action
    • doi: 10.1073/pnas.0505581102; pmid: 16091460
    • D. Baram et al., Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc. Natl. Acad. Sci. U.S.A. 102, 12017-12022 (2005). doi: 10.1073/pnas.0505581102; pmid: 16091460
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12017-12022
    • Baram, D.1
  • 14
    • 27644447766 scopus 로고    scopus 로고
    • The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction
    • doi: 10.1016/j.str.2005.08.007; pmid: 16271892
    • F. Schlünzen et al., The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction. Structure 13, 1685-1694 (2005). doi: 10.1016/j.str.2005.08.007; pmid: 16271892
    • (2005) Structure , vol.13 , pp. 1685-1694
    • Schlünzen, F.1
  • 15
    • 44649188719 scopus 로고    scopus 로고
    • Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
    • doi: 10.1038/emboj.2008.89; pmid: 18497744
    • F. Merz et al., Molecular mechanism and structure of Trigger Factor bound to the translating ribosome. EMBO J. 27, 1622-1632 (2008). doi: 10.1038/emboj.2008.89; pmid: 18497744
    • (2008) EMBO J. , vol.27 , pp. 1622-1632
    • Merz, F.1
  • 16
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • doi: 10.1016/S0092-8674(00)80806-5; pmid: 10786831
    • B. Bukau, E. Deuerling, C. Pfund, E. A. Craig, Getting newly synthesized proteins into shape. Cell 101, 119-122 (2000). doi: 10.1016/S0092-8674(00)80806- 5; pmid: 10786831
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 17
    • 0037436348 scopus 로고    scopus 로고
    • Interaction of trigger factor with the ribosome
    • doi: 10.1016/S0022-2836(02)01427-4; pmid: 12559924
    • R. Maier, B. Eckert, C. Scholz, H. Lilie, F.-X. Schmid, Interaction of trigger factor with the ribosome. J. Mol. Biol. 326, 585-592 (2003). doi: 10.1016/S0022-2836(02)01427-4; pmid: 12559924
    • (2003) J. Mol. Biol. , vol.326 , pp. 585-592
    • Maier, R.1    Eckert, B.2    Scholz, C.3    Lilie, H.4    Schmid, F.-X.5
  • 18
    • 33751321592 scopus 로고    scopus 로고
    • Real-time observation of trigger factor function on translating ribosomes
    • doi: 10.1038/nature05225; pmid: 17051157
    • C. M. Kaiser et al., Real-time observation of trigger factor function on translating ribosomes. Nature 444, 455-460 (2006). doi: 10.1038/nature05225; pmid: 17051157
    • (2006) Nature , vol.444 , pp. 455-460
    • Kaiser, C.M.1
  • 19
    • 42949163134 scopus 로고    scopus 로고
    • Dynamics of trigger factor interaction with translating ribosomes
    • doi: 10.1074/jbc.M708294200; pmid: 18045873
    • A. Rutkowska et al., Dynamics of trigger factor interaction with translating ribosomes. J. Biol. Chem. 283, 4124-4132 (2008). doi: 10.1074/jbc.M708294200; pmid: 18045873
    • (2008) J. Biol. Chem. , vol.283 , pp. 4124-4132
    • Rutkowska, A.1
  • 20
    • 0023766740 scopus 로고
    • The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane
    • doi: 10.1016/0092-8674(88)90116-X; pmid: 3046750
    • R. Lill, E. Crooke, B. Guthrie, W. Wickner, The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane. Cell 54, 1013-1018 (1988). doi: 10.1016/0092-8674(88)90116-X; pmid: 3046750
    • (1988) Cell , vol.54 , pp. 1013-1018
    • Lill, R.1    Crooke, E.2    Guthrie, B.3    Wickner, W.4
  • 21
    • 1942421714 scopus 로고    scopus 로고
    • Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed
    • doi: 10.1016/S0092-8674(04)00299-5; pmid: 15084258
    • V. R. Agashe et al., Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed. Cell 117, 199-209 (2004). doi: 10.1016/S0092-8674(04)00299-5; pmid: 15084258
    • (2004) Cell , vol.117 , pp. 199-209
    • Agashe, V.R.1
  • 22
    • 33646542413 scopus 로고    scopus 로고
    • Trigger factor forms a protective shield for nascent polypeptides at the ribosome
    • doi: 10.1074/jbc.M512345200; pmid: 16407311
    • A. Hoffmann et al., Trigger factor forms a protective shield for nascent polypeptides at the ribosome. J. Biol. Chem. 281, 6539-6545 (2006). doi: 10.1074/jbc.M512345200; pmid: 16407311
    • (2006) J. Biol. Chem. , vol.281 , pp. 6539-6545
    • Hoffmann, A.1
  • 23
    • 29344447067 scopus 로고    scopus 로고
    • Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains
    • doi: 10.1016/j.febslet.2005.11.050; pmid: 16359675
    • S. Tomic, A. E. Johnson, F. U. Hartl, S. A. Etchells, Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. FEBS Lett. 580, 72-76 (2006). doi: 10.1016/j.febslet.2005. 11.050; pmid: 16359675
    • (2006) FEBS Lett. , vol.580 , pp. 72-76
    • Tomic, S.1    Johnson, A.E.2    Hartl, F.U.3    Etchells, S.A.4
  • 24
    • 0037338711 scopus 로고    scopus 로고
    • Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
    • doi: 10.1046/j.1365-2958.2003.03370.x; pmid: 12603737
    • E. Deuerling et al., Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Mol. Microbiol. 47, 1317-1328 (2003). doi: 10.1046/j.1365-2958.2003.03370.x; pmid: 12603737
    • (2003) Mol. Microbiol. , vol.47 , pp. 1317-1328
    • Deuerling, E.1
  • 25
    • 83255164895 scopus 로고    scopus 로고
    • Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo
    • doi: 10.1016/j.cell.2011.10.044; pmid: 22153074
    • E. Oh et al., Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. Cell 147, 1295-1308 (2011). doi: 10.1016/j.cell.2011.10.044; pmid: 22153074
    • (2011) Cell , vol.147 , pp. 1295-1308
    • Oh, E.1
  • 26
    • 77955659939 scopus 로고    scopus 로고
    • Versatility of trigger factor interactions with ribosome-nascent chain complexes
    • doi: 10.1074/jbc.M110.134163; pmid: 20595383
    • S. K. Lakshmipathy, R. Gupta, S. Pinkert, S. A. Etchells, F. U. Hartl, Versatility of trigger factor interactions with ribosome-nascent chain complexes. J. Biol. Chem. 285, 27911-27923 (2010). doi: 10.1074/jbc.M110.134163; pmid: 20595383
    • (2010) J. Biol. Chem. , vol.285 , pp. 27911-27923
    • Lakshmipathy, S.K.1    Gupta, R.2    Pinkert, S.3    Etchells, S.A.4    Hartl, F.U.5
  • 27
    • 69449095153 scopus 로고    scopus 로고
    • Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone
    • doi: 10.1016/j.cell.2009.07.044; pmid: 19737520
    • E. Martinez-Hackert, W. A. Hendrickson, Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell 138, 923-934 (2009). doi: 10.1016/j.cell.2009.07.044; pmid: 19737520
    • (2009) Cell , vol.138 , pp. 923-934
    • Martinez-Hackert, E.1    Hendrickson, W.A.2
  • 28
    • 84863528678 scopus 로고    scopus 로고
    • Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions
    • doi: 10.1021/ja302305u; pmid: 22680285
    • E. P. O'Brien, J. Christodoulou, M. Vendruscolo, C. M. Dobson, Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions. J. Am. Chem. Soc. 134, 10920-10932 (2012). doi: 10.1021/ja302305u; pmid: 22680285
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10920-10932
    • O'Brien, E.P.1    Christodoulou, J.2    Vendruscolo, M.3    Dobson, C.M.4
  • 29
    • 84881480267 scopus 로고    scopus 로고
    • Reshaping of the conformational search of a protein by the chaperone trigger factor
    • doi: 10.1038/nature12293; pmid: 23831649
    • A. Mashaghi et al., Reshaping of the conformational search of a protein by the chaperone trigger factor. Nature 500, 98-101 (2013). doi: 10.1038/nature12293; pmid: 23831649
    • (2013) Nature , vol.500 , pp. 98-101
    • Mashaghi, A.1
  • 30
    • 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; pmid: 22921937
    • A. Hoffmann et al., Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding. Mol. Cell 48, 63-74 (2012). doi: 10.1016/j.molcel.2012.07.018; pmid: 22921937
    • (2012) Mol. Cell , vol.48 , pp. 63-74
    • Hoffmann, A.1
  • 31
    • 1642487106 scopus 로고    scopus 로고
    • In vivo analysis of the overlapping functions of DnaK and trigger factor
    • doi: 10.1038/sj.embor.7400067; pmid: 14726952
    • P. Genevaux et al., In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 5, 195-200 (2004). doi: 10.1038/sj.embor.7400067; pmid: 14726952
    • (2004) EMBO Rep. , vol.5 , pp. 195-200
    • Genevaux, P.1
  • 32
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • doi: 10.1038/23301; pmid: 10458167
    • E. Deuerling, A. Schulze-Specking, T. Tomoyasu, A. Mogk, B. Bukau, Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400, 693-696 (1999). doi: 10.1038/23301; pmid: 10458167
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 33
    • 0033032592 scopus 로고    scopus 로고
    • Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    • doi: 10.1016/S0092-8674(00)80787-4; pmid: 10380927
    • S. A. Teter et al., Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97, 755-765 (1999). doi: 10.1016/S0092-8674(00)80787-4; pmid: 10380927
    • (1999) Cell , vol.97 , pp. 755-765
    • Teter, S.A.1
  • 34
    • 84861139210 scopus 로고    scopus 로고
    • DnaK functions as a central hub in the E. coli chaperone network
    • doi: 10.1016/j.celrep.2011.12.007; pmid: 22832197
    • G. Calloni et al., DnaK functions as a central hub in the E. coli chaperone network. Cell Rep. 1, 251-264 (2012). doi: 10.1016/j.celrep.2011.12. 007; pmid: 22832197
    • (2012) Cell Rep. , vol.1 , pp. 251-264
    • Calloni, G.1
  • 35
    • 36749011854 scopus 로고    scopus 로고
    • Direct observation of chaperone-induced changes in a protein folding pathway
    • doi: 10.1126/science.1144972; pmid: 18048690
    • P. Bechtluft et al., Direct observation of chaperone-induced changes in a protein folding pathway. Science 318, 1458-1461 (2007). doi: 10.1126/science.1144972; pmid: 18048690
    • (2007) Science , vol.318 , pp. 1458-1461
    • Bechtluft, P.1
  • 36
    • 33847629610 scopus 로고    scopus 로고
    • Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli
    • doi: 10.1073/pnas.0608232104; pmid: 17360615
    • R. S. Ullers, D. Ang, F. Schwager, C. Georgopoulos, P. Genevaux, Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 104, 3101-3106 (2007). doi: 10.1073/pnas.0608232104; pmid: 17360615
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 3101-3106
    • Ullers, R.S.1    Ang, D.2    Schwager, F.3    Georgopoulos, C.4    Genevaux, P.5
  • 37
    • 0037143625 scopus 로고    scopus 로고
    • CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
    • doi: 10.1073/pnas.132393699; pmid: 12163643
    • S. Rudiger, S. M. V. Freund, D. B. Veprintsev, A. R. Fersht, CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proc. Natl. Acad. Sci. U.S.A. 99, 11085-11090 (2002). doi: 10.1073/pnas.132393699; pmid: 12163643
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11085-11090
    • Rudiger, S.1    Freund, S.M.V.2    Veprintsev, D.B.3    Fersht, A.R.4
  • 38
    • 24644501099 scopus 로고    scopus 로고
    • Direct NMR observation of a substrate protein bound to the chaperonin GroEL
    • doi: 10.1073/pnas.0505642102; pmid: 16116078
    • R. Horst et al., Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc. Natl. Acad. Sci. U.S.A. 102, 12748-12753 (2005). doi: 10.1073/pnas.0505642102; pmid: 16116078
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12748-12753
    • Horst, R.1
  • 39
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • doi: 10.1073/pnas.0809275106; pmid: 19181847
    • T. A. Walton, C. M. Sandoval, C. A. Fowler, A. Pardi, M. C. Sousa, The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U.S.A. 106, 1772-1777 (2009). doi: 10.1073/pnas.0809275106; pmid: 19181847
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 40
    • 79955642720 scopus 로고    scopus 로고
    • The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    • doi: 10.1038/nsmb.2045; pmid: 21460846
    • S. J. Park, B. N. Borin, M. A. Martinez-Yamout, H. J. Dyson, The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 18, 537-541 (2011). doi: 10.1038/nsmb.2045; pmid: 21460846
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 537-541
    • Park, S.J.1    Borin, B.N.2    Martinez-Yamout, M.A.3    Dyson, H.J.4
  • 41
    • 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; pmid: 23217711
    • A. Zhuravleva, E. M. Clérico, L. M. Gierasch, An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151, 1296-1307 (2012). doi: 10.1016/j.cell.2012.11.002; pmid: 23217711
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clérico, E.M.2    Gierasch, L.M.3
  • 42
    • 84887429368 scopus 로고    scopus 로고
    • Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp
    • doi: 10.1038/nsmb.2677; pmid: 24077225
    • B. M. Burmann, C. Wang, S. Hiller, Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. Nat. Struct. Mol. Biol. 20, 1265-1272 (2013). doi: 10.1038/nsmb.2677; pmid: 24077225
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1265-1272
    • Burmann, B.M.1    Wang, C.2    Hiller, S.3
  • 43
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • doi: 10.1038/nature05512; pmid: 17237764
    • R. Sprangers, L. E. Kay, Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622 (2007). doi: 10.1038/nature05512; pmid: 17237764
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 44
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • doi: 10.1016/j.cell.2007.09.039; pmid: 18022369
    • I. Gelis et al., Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131, 756-769 (2007). doi: 10.1016/j.cell.2007.09.039; pmid: 18022369
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1
  • 45
    • 77950497745 scopus 로고    scopus 로고
    • Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
    • doi: 10.1126/science.1184991; pmid: 20360109
    • T. L. Religa, R. Sprangers, L. E. Kay, Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science 328, 98-102 (2010). doi: 10.1126/science.1184991; pmid: 20360109
    • (2010) Science , vol.328 , pp. 98-102
    • Religa, T.L.1    Sprangers, R.2    Kay, L.E.3
  • 46
    • 84874393637 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
    • doi: 10.1126/science.1233066; pmid: 23393091
    • R. Rosenzweig, S. Moradi, A. Zarrine-Afsar, J. R. Glover, L. E. Kay, Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science 339, 1080-1083 (2013). doi: 10.1126/science.1233066; pmid: 23393091
    • (2013) Science , vol.339 , pp. 1080-1083
    • Rosenzweig, R.1    Moradi, S.2    Zarrine-Afsar, A.3    Glover, J.R.4    Kay, L.E.5
  • 47
    • 66349083528 scopus 로고    scopus 로고
    • Structural basis for cAMP-mediated allosteric control of the catabolite activator protein
    • doi: 10.1073/pnas.0900595106; pmid: 19359484
    • N. Popovych, S.-R. Tzeng, M. Tonelli, R. H. Ebright, C. G. Kalodimos, Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc. Natl. Acad. Sci. U.S.A. 106, 6927-6932 (2009). doi: 10.1073/pnas.0900595106; pmid: 19359484
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6927-6932
    • Popovych, N.1    Tzeng, S.-R.2    Tonelli, M.3    Ebright, R.H.4    Kalodimos, C.G.5
  • 48
    • 83455225628 scopus 로고    scopus 로고
    • Structural instability tuning as a regulatory mechanism in protein-protein interactions
    • doi: 10.1016/j.molcel.2011.09.022; pmid: 22152477
    • L. Chen et al., Structural instability tuning as a regulatory mechanism in protein-protein interactions. Mol. Cell 44, 734-744 (2011). doi: 10.1016/j.molcel.2011.09.022; pmid: 22152477
    • (2011) Mol. Cell , vol.44 , pp. 734-744
    • Chen, L.1
  • 49
    • 34249691985 scopus 로고    scopus 로고
    • Identification of nascent chain interaction sites on trigger factor
    • doi: 10.1074/jbc.M609871200; pmid: 17296610
    • S. K. Lakshmipathy et al., Identification of nascent chain interaction sites on trigger factor. J. Biol. Chem. 282, 12186-12193 (2007). doi: 10.1074/jbc.M609871200; pmid: 17296610
    • (2007) J. Biol. Chem. , vol.282 , pp. 12186-12193
    • Lakshmipathy, S.K.1
  • 50
    • 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; pmid: 16926148
    • F. Merz et al., The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J. Biol. Chem. 281, 31963-31971 (2006). doi: 10.1074/jbc.M605164200; pmid: 16926148
    • (2006) J. Biol. Chem. , vol.281 , pp. 31963-31971
    • Merz, F.1
  • 51
    • 0036806274 scopus 로고    scopus 로고
    • Three-state equilibrium of Escherichia coli trigger factor
    • doi: 10.1515/BC.2002.182; pmid: 12452438
    • H. Patzelt et al., Three-state equilibrium of Escherichia coli trigger factor. Biol. Chem. 383, 1611-1619 (2002). doi: 10.1515/BC.2002.182; pmid: 12452438
    • (2002) Biol. Chem. , vol.383 , pp. 1611-1619
    • Patzelt, H.1
  • 52
    • 65649125973 scopus 로고    scopus 로고
    • 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli
    • doi: 10.1007/s12104-008-9130-8; pmid: 19636937
    • 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli. Biomol. NMR Assign. 3, 17-20 (2009). doi: 10.1007/s12104-008-9130-8; pmid: 19636937
    • (2009) Biomol. NMR Assign. , vol.3 , pp. 17-20
    • Hsu, S.-T.D.1    Dobson, C.M.2
  • 53
    • 37849023833 scopus 로고    scopus 로고
    • Structure discrimination for the C-terminal domain of Escherichia coli trigger factor in solution
    • doi: 10.1007/s10858-007-9207-1; pmid: 18043871
    • Y. Yao, G. Bhabha, G. Kroon, M. Landes, H. J. Dyson, Structure discrimination for the C-terminal domain of Escherichia coli trigger factor in solution. J. Biomol. NMR 40, 23-30 (2008). doi: 10.1007/s10858-007-9207-1; pmid: 18043871
    • (2008) J. Biomol. NMR , vol.40 , pp. 23-30
    • Yao, Y.1    Bhabha, G.2    Kroon, G.3    Landes, M.4    Dyson, H.J.5
  • 54
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • doi: 10.1016/0092-8674(91)90532-4; pmid: 1934062
    • J. C. Bardwell, K. McGovern, J. Beckwith, Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589 (1991). doi: 10.1016/0092-8674(91)90532-4; pmid: 1934062
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 55
    • 0024558885 scopus 로고
    • Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein
    • pmid: 2535843
    • Y. Akiyama, K. Ito, Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein, SecY. J. Biol. Chem. 264, 437-442 (1989). pmid: 2535843
    • (1989) SecY. J. Biol. Chem. , vol.264 , pp. 437-442
    • Akiyama, Y.1    Ito, K.2
  • 56
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • pmid: 1740115
    • S. Kamitani, Y. Akiyama, K. Ito, Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11, 57-62 (1992). pmid: 1740115
    • (1992) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 57
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
    • pmid: 8521806
    • Q. A. Valent et al., Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14, 5494-5505 (1995). pmid: 8521806
    • (1995) EMBO J. , vol.14 , pp. 5494-5505
    • Valent, Q.A.1
  • 58
    • 0037044752 scopus 로고    scopus 로고
    • Trigger factor retards protein export in Escherichia coli
    • doi: 10.1074/jbc.M205950200; pmid: 12205085
    • H. C. Lee, H. D. Bernstein, Trigger factor retards protein export in Escherichia coli. J. Biol. Chem. 277, 43527-43535 (2002). doi: 10.1074/jbc.M205950200; pmid: 12205085
    • (2002) J. Biol. Chem. , vol.277 , pp. 43527-43535
    • Lee, H.C.1    Bernstein, H.D.2
  • 59
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation
    • doi: 10.1110/ps.062465306; pmid: 17088319
    • J. A. Marsh, V. K. Singh, Z. Jia, J. D. Forman-Kay, Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation. Protein Sci. 15, 2795-2804 (2006). doi: 10.1110/ps.062465306; pmid: 17088319
    • (2006) Protein Sci. , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 60
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • doi: 10.1016/S0076-6879(05)94011-1; pmid: 15808225
    • H. J. Dyson, P. E. Wright, Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394, 299-321 (2005). doi: 10.1016/S0076-6879(05)94011- 1; pmid: 15808225
    • (2005) Methods Enzymol. , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 61
    • 32344445231 scopus 로고    scopus 로고
    • NMR studies of protein interactions
    • doi: 10.1016/j.sbi.2006.01.006; pmid: 16427776
    • K. Takeuchi, G. Wagner, NMR studies of protein interactions. Curr. Opin. Struct. Biol. 16, 109-117 (2006). doi: 10.1016/j.sbi.2006.01.006; pmid: 16427776
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 109-117
    • Takeuchi, K.1    Wagner, G.2
  • 62
    • 0035807963 scopus 로고    scopus 로고
    • Binding specificity of Escherichia coli trigger factor
    • doi: 10.1073/pnas.261432298; pmid: 11724963
    • H. Patzelt et al., Binding specificity of Escherichia coli trigger factor. Proc. Natl. Acad. Sci. U.S.A. 98, 14244-14249 (2001). doi: 10.1073/pnas.261432298; pmid: 11724963
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14244-14249
    • Patzelt, H.1
  • 63
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • doi: 10.1038/371614a0; pmid: 7935796
    • W. A. Fenton, Y. Kashi, K. Furtak, A. L. Horwich, Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619 (1994). doi: 10.1038/371614a0; pmid: 7935796
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 64
    • 33749538453 scopus 로고    scopus 로고
    • Convergent evolution of clamp-like binding sites in diverse chaperones
    • doi: 10.1038/nsmb1153; pmid: 17021621
    • P. C. Stirling, S. F. Bakhoum, A. B. Feigl, M. R. Leroux, Convergent evolution of clamp-like binding sites in diverse chaperones. Nat. Struct. Mol. Biol. 13, 865-870 (2006). doi: 10.1038/nsmb1153; pmid: 17021621
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 865-870
    • Stirling, P.C.1    Bakhoum, S.F.2    Feigl, A.B.3    Leroux, M.R.4
  • 65
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • doi: 10.1126/science.1124964; pmid: 16614210
    • A. Mittermaier, L. E. Kay, New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228 (2006). doi: 10.1126/science.1124964; pmid: 16614210
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 66
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • doi: 10.1021/cr030413t; pmid: 15303831
    • A. Palmer, NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 104, 3623-3640 (2004). doi: 10.1021/cr030413t; pmid: 15303831
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer, A.1
  • 67
    • 0032719427 scopus 로고    scopus 로고
    • A TROSY CPMG sequence for characterizing chemical exchange in large proteins
    • doi: 10.1023/A:1008355631073; pmid: 10605088
    • J. P. Loria, M. Rance, A. G. Palmer, A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15, 151-155 (1999). doi: 10.1023/A:1008355631073; pmid: 10605088
    • (1999) J. Biomol. NMR , vol.15 , pp. 151-155
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 68
    • 0034759979 scopus 로고    scopus 로고
    • Studying excited states of proteins by NMR spectroscopy
    • doi: 10.1038/nsb1101-932; pmid: 11685237
    • F. A. Mulder, A. Mittermaier, B. Hon, F. W. Dahlquist, L. E. Kay, Studying excited states of proteins by NMR spectroscopy. Nat. Struct. Biol. 8, 932-935 (2001). doi: 10.1038/nsb1101-932; pmid: 11685237
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 932-935
    • Mulder, F.A.1    Mittermaier, A.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 69
    • 36749058463 scopus 로고    scopus 로고
    • Measurement of bond vector orientations in invisible excited states of proteins
    • doi: 10.1073/pnas.0708296104; pmid: 18006656
    • P. Vallurupalli, D. F. Hansen, E. Stollar, E. Meirovitch, L. E. Kay, Measurement of bond vector orientations in invisible excited states of proteins. Proc. Natl. Acad. Sci. U.S.A. 104, 18473-18477 (2007). doi: 10.1073/pnas.0708296104; pmid: 18006656
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 18473-18477
    • Vallurupalli, P.1    Hansen, D.F.2    Stollar, E.3    Meirovitch, E.4    Kay, L.E.5
  • 70
    • 35948933151 scopus 로고    scopus 로고
    • Tailoring relaxation dispersion experiments for fast-associating protein complexes
    • doi: 10.1021/ja0762238; pmid: 17935336
    • K. Sugase, J. C. Lansing, H. J. Dyson, P. E. Wright, Tailoring relaxation dispersion experiments for fast-associating protein complexes. J. Am. Chem. Soc. 129, 13406-13407 (2007). doi: 10.1021/ja0762238; pmid: 17935336
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 13406-13407
    • Sugase, K.1    Lansing, J.C.2    Dyson, H.J.3    Wright, P.E.4
  • 71
    • 0035861999 scopus 로고    scopus 로고
    • Dynamic association of trigger factor with protein substrates
    • doi: 10.1006/jmbi.2000.5192; pmid: 11743733
    • R. Maier, C. Scholz, F. Schmid, Dynamic association of trigger factor with protein substrates. J. Mol. Biol. 314, 1181-1190 (2001). doi: 10.1006/jmbi.2000.5192; pmid: 11743733
    • (2001) J. Mol. Biol. , vol.314 , pp. 1181-1190
    • Maier, R.1    Scholz, C.2    Schmid, F.3
  • 72
    • 39649107959 scopus 로고    scopus 로고
    • Kinetics and energetics of the translocation of maltose binding protein folding mutants
    • doi: 10.1016/j.jmb.2008.01.014; pmid: 18241889
    • D. Tomkiewicz, N. Nouwen, A. J. M. Driessen, Kinetics and energetics of the translocation of maltose binding protein folding mutants. J. Mol. Biol. 377, 83-90 (2008). doi: 10.1016/j.jmb.2008.01.014; pmid: 18241889
    • (2008) J. Mol. Biol. , vol.377 , pp. 83-90
    • Tomkiewicz, D.1    Nouwen, N.2    Driessen, A.J.M.3
  • 73
    • 73949133922 scopus 로고    scopus 로고
    • GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state
    • doi: 10.1073/pnas.0911556106; pmid: 19915138
    • N. K. Tyagi, W. A. Fenton, A. L. Horwich, GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proc. Natl. Acad. Sci. U.S.A. 106, 20264-20269 (2009). doi: 10.1073/pnas.0911556106; pmid: 19915138
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20264-20269
    • Tyagi, N.K.1    Fenton, W.A.2    Horwich, A.L.3
  • 74
    • 77954277524 scopus 로고    scopus 로고
    • Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
    • doi: 10.1016/j.cell.2010.05.027; pmid: 20603018
    • K. Chakraborty et al., Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Cell 142, 112-122 (2010). doi: 10.1016/j.cell.2010. 05.027; pmid: 20603018
    • (2010) Cell , vol.142 , pp. 112-122
    • Chakraborty, K.1
  • 75
    • 0029923189 scopus 로고    scopus 로고
    • Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies
    • doi: 10.1074/jbc.271.14.8046; pmid: 8626487
    • J. M. Betton, M. Hofnung, Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies. J. Biol. Chem. 271, 8046-8052 (1996). doi: 10.1074/jbc.271.14.8046; pmid: 8626487
    • (1996) J. Biol. Chem. , vol.271 , pp. 8046-8052
    • Betton, J.M.1    Hofnung, M.2
  • 76
    • 0031764460 scopus 로고    scopus 로고
    • Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein
    • doi: 10.1002/pro.5560071010; pmid: 9792100
    • S. Raffy, N. Sassoon, M. Hofnung, J. M. Betton, Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7, 2136-2142 (1998). doi: 10.1002/pro.5560071010; pmid: 9792100
    • (1998) Protein Sci. , vol.7 , pp. 2136-2142
    • Raffy, S.1    Sassoon, N.2    Hofnung, M.3    Betton, J.M.4
  • 77
    • 0037369139 scopus 로고    scopus 로고
    • Crystal structure of a defective folding protein
    • doi: 10.1110/ps.0235103; pmid: 12592028
    • F. A. Saul et al., Crystal structure of a defective folding protein. Protein Sci. 12, 577-585 (2003). doi: 10.1110/ps.0235103; pmid: 12592028
    • (2003) Protein Sci. , vol.12 , pp. 577-585
    • Saul, F.A.1
  • 78
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • doi: 10.1038/nature06524; pmid: 18075577
    • J. Kuriyan, D. Eisenberg, The origin of protein interactions and allostery in colocalization. Nature 450, 983-990 (2007). doi: 10.1038/nature06524; pmid: 18075577
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 79
    • 0031030202 scopus 로고    scopus 로고
    • Thermodynamics of maltose binding protein unfolding
    • doi: 10.1002/pro.5560060116; pmid: 9007986
    • V. Novokhatny, K. Ingham, Thermodynamics of maltose binding protein unfolding. Protein Sci. 6, 141-146 (1997). doi: 10.1002/pro.5560060116; pmid: 9007986
    • (1997) Protein Sci. , vol.6 , pp. 141-146
    • Novokhatny, V.1    Ingham, K.2
  • 80
    • 41149089882 scopus 로고    scopus 로고
    • Monitoring protein conformation along the pathway of chaperonin-assisted folding
    • doi: 10.1016/j.cell.2008.01.048; pmid: 18394994
    • S. Sharma et al., Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 133, 142-153 (2008). doi: 10.1016/j.cell.2008. 01.048; pmid: 18394994
    • (2008) Cell , vol.133 , pp. 142-153
    • Sharma, S.1
  • 81
    • 0034598920 scopus 로고    scopus 로고
    • Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
    • doi: 10.1016/S0092-8674(00)80692-3; pmid: 10721993
    • G. W. Farr et al., Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. Cell 100, 561-573 (2000). doi: 10.1016/S0092-8674(00) 80692-3; pmid: 10721993
    • (2000) Cell , vol.100 , pp. 561-573
    • Farr, G.W.1
  • 82
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • doi: 10.1126/science.284.5415.822; pmid: 10221918
    • M. Shtilerman, G. H. Lorimer, S. W. Englander, Chaperonin function: Folding by forced unfolding. Science 284, 822-825 (1999). doi: 10.1126/science.284.5415.822; pmid: 10221918
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 83
    • 70349832775 scopus 로고    scopus 로고
    • Trigger factor finds new jobs and contacts
    • doi: 10.1038/nsmb1009-1006; pmid: 19809489
    • A. Hoffmann, B. Bukau, Trigger factor finds new jobs and contacts. Nat. Struct. Mol. Biol. 16, 1006-1008 (2009). doi: 10.1038/nsmb1009-1006; pmid: 19809489
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1006-1008
    • Hoffmann, A.1    Bukau, B.2
  • 84
    • 2942519292 scopus 로고    scopus 로고
    • Functional dissection of Escherichia coli trigger factor: Unraveling the function of individual domains
    • doi: 10.1128/JB.186.12.3777-3784.2004; pmid: 15175291
    • G. Kramer et al., Functional dissection of Escherichia coli trigger factor: Unraveling the function of individual domains. J. Bacteriol. 186, 3777-3784 (2004). doi: 10.1128/JB.186.12.3777-3784.2004; pmid: 15175291
    • (2004) J. Bacteriol. , vol.186 , pp. 3777-3784
    • Kramer, G.1
  • 85
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • doi: 10.1007/BF00197809; pmid: 8520220
    • F. Delaglio et al., NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995). doi: 10.1007/BF00197809; pmid: 8520220
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 86
    • 34548304719 scopus 로고    scopus 로고
    • Solution NMR of supramolecular complexes: Providing new insights into function
    • doi: 10.1038/nmeth1080; pmid: 17762877
    • R. Sprangers, A. Velyvis, L. Kay, Solution NMR of supramolecular complexes: Providing new insights into function. Nat. Methods 4, 697-703 (2007). doi: 10.1038/nmeth1080; pmid: 17762877
    • (2007) Nat. Methods , vol.4 , pp. 697-703
    • Sprangers, R.1    Velyvis, A.2    Kay, L.3
  • 87
    • 84866272306 scopus 로고    scopus 로고
    • 3-threonine for solution NMR studies of large protein complexes: Application to the 670 kDa proteasome
    • doi: 10.1371/journal.pone.0043725; pmid: 22984438
    • 3-threonine for solution NMR studies of large protein complexes: Application to the 670 kDa proteasome. PLOS One 7, e43725 (2012). doi: 10.1371/journal.pone.0043725; pmid: 22984438
    • (2012) PLOS One , vol.7
    • Velyvis, A.1    Ruschak, A.M.2    Kay, L.E.3
  • 88
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • pmid: 15318003
    • P. Güntert, Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378 (2004). pmid: 15318003
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 89
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • doi: 10.1007/s10858-009-9333-z; pmid: 19548092
    • Y. Shen, F. Delaglio, G. Cornilescu, A. Bax, TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223 (2009). doi: 10.1007/s10858-009-9333-z; pmid: 19548092
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 90
    • 33645868288 scopus 로고    scopus 로고
    • Using Xplor-NIH for NMR molecular structure determination
    • doi: 10.1016/j.pnmrs.2005.10.001
    • C. Schwieters, J. Kuszewski, G.M. Clore, Using Xplor-NIH for NMR molecular structure determination. Prog. Nucl. Magn. Res. Spect. 48, 47-62 (2006). doi: 10.1016/j.pnmrs.2005.10.001
    • (2006) Prog. Nucl. Magn. Res. Spect. , vol.48 , pp. 47-62
    • Schwieters, C.1    Kuszewski, J.2    Clore, G.M.3
  • 91
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • doi: 10.1038/nprot.2007.406; pmid: 18007608
    • A. T. Brunger, Version 1.2 of the Crystallography and NMR system. Nat. Protoc. 2, 2728-2733 (2007). doi: 10.1038/nprot.2007.406; pmid: 18007608
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 92
    • 0002889918 scopus 로고
    • 2 on the Carr-Purcell pulse separation
    • doi: 10.1016/0022-2364(72)90090-X
    • 2 on the Carr-Purcell pulse separation. J. Magn. Reson. 6, 89-105 (1972). doi: 10.1016/0022-2364(72)90090-X
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 93
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • doi: 10.1038/nature11271; pmid: 22801505
    • S.-R. Tzeng, C. G. Kalodimos, Protein activity regulation by conformational entropy. Nature 488, 236-240 (2012). doi: 10.1038/nature11271; pmid: 22801505
    • (2012) Nature , vol.488 , pp. 236-240
    • Tzeng, S.-R.1    Kalodimos, C.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.