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Volumn 2, Issue 1, 2011, Pages 135-152

DEAD-box proteins as RNA helicases and chaperones

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; DEAD BOX PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN DBPA; PROTEIN HERA; RIBONUCLEOPROTEIN; RNA; RNA HELICASE; UNCLASSIFIED DRUG;

EID: 79956071179     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.50     Document Type: Review
Times cited : (130)

References (115)
  • 1
    • 0024967639 scopus 로고
    • Birth of the D-E-A-D box
    • Linder P, Lasko PF, Ashburner M, Leroy P, Nielsen PJ, Nishi K, Schnier J, Slonimski
    • Linder P, Lasko PF, Ashburner M, Leroy P, Nielsen PJ, Nishi K, Schnier J, Slonimski PP. Birth of the D-E-A-D box. Nature 1989, 337:121-122.
    • (1989) Nature , vol.337 , pp. 121-122
  • 2
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: a family affair-active and passive players in RNP-remodeling
    • Linder P. Dead-box proteins: a family affair-active and passive players in RNP-remodeling. Nucleic Acids Res 2006, 34:4168-4180.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4168-4180
    • Linder, P.1
  • 3
    • 34347385000 scopus 로고    scopus 로고
    • RNA helicases-one fold for many functions
    • Jankowsky E, Fairman ME. RNA helicases-one fold for many functions. Curr Opin Struct Biol 2007, 17:316-324.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 5
    • 33749125440 scopus 로고    scopus 로고
    • DEAD-box RNA helicases in Escherichia coli
    • Iost I, Dreyfus M. DEAD-box RNA helicases in Escherichia coli. Nucleic Acids Res 2006, 34:4189-4197.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4189-4197
    • Iost, I.1    Dreyfus, M.2
  • 6
    • 71049181356 scopus 로고    scopus 로고
    • A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit
    • Sharpe Elles LM, Sykes MT, Williamson JR, Uhlenbeck OC. A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit. Nucleic Acids Res 2009, 37:6503-6514.
    • (2009) Nucleic Acids Res , vol.37 , pp. 6503-6514
    • Sharpe Elles, L.M.1    Sykes, M.T.2    Williamson, J.R.3    Uhlenbeck, O.C.4
  • 7
    • 38649135052 scopus 로고    scopus 로고
    • The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly
    • Jain C. The E. coli RhlE RNA helicase regulates the function of related RNA helicases during ribosome assembly. RNA 2008, 14:381-389.
    • (2008) RNA , vol.14 , pp. 381-389
    • Jain, C.1
  • 8
    • 62549144414 scopus 로고    scopus 로고
    • The current understanding of Ded1p/DDX3 homologs from yeast to human
    • Tarn WY, Chang TH. The current understanding of Ded1p/DDX3 homologs from yeast to human. RNA Biol 2009, 6:17-20.
    • (2009) RNA Biol , vol.6 , pp. 17-20
    • Tarn, W.Y.1    Chang, T.H.2
  • 9
    • 33846837482 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase Dbp5 functions in translation termination
    • Gross T, Siepmann A, Sturm D, Windgassen M, Scarcelli JJ, Seedorf M, Cole CN, Krebber H.
    • Gross T, Siepmann A, Sturm D, Windgassen M, Scarcelli JJ, Seedorf M, Cole CN, Krebber H. The DEAD-box RNA helicase Dbp5 functions in translation termination. Science 2007, 315:646-649.
    • (2007) Science , vol.315 , pp. 646-649
  • 10
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang HR, Rowe CE, Mohr S, Jiang Y, Lambowitz AM, Perlman PS.
    • Huang HR, Rowe CE, Mohr S, Jiang Y, Lambowitz AM, Perlman PS. The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc Natl Acad Sci U S A 2005, 102:163-168.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 163-168
  • 11
    • 70350089113 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
    • Hilbert M, Karow AR, Klostermeier D. The mechanism of ATP-dependent RNA unwinding by DEAD box proteins. Biol Chem 2009, 390:1237-1250.
    • (2009) Biol Chem , vol.390 , pp. 1237-1250
    • Hilbert, M.1    Karow, A.R.2    Klostermeier, D.3
  • 12
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 2007, 76:23-50.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 13
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: mechanisms and regulation
    • Lohman TM, Tomko EJ, Wu CG. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat Rev Mol Cell Biol 2008, 9:391-401.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 14
    • 2542510120 scopus 로고    scopus 로고
    • Rearrangement of structured RNA via branch migration structures catalysed by the highly related DEAD-box proteins p68 and p72
    • Rossler OG, Straka A, Stahl H. Rearrangement of structured RNA via branch migration structures catalysed by the highly related DEAD-box proteins p68 and p72. Nucleic Acids Res 2001, 29:2088-2096.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2088-2096
    • Rossler, O.G.1    Straka, A.2    Stahl, H.3
  • 15
    • 0037066739 scopus 로고    scopus 로고
    • The ATPase, RNA unwinding, and RNA binding activities of recombinant p68 RNA helicase
    • Huang Y, Liu ZR. The ATPase, RNA unwinding, and RNA binding activities of recombinant p68 RNA helicase. J Biol Chem 2002, 277:12810-12815.
    • (2002) J Biol Chem , vol.277 , pp. 12810-12815
    • Huang, Y.1    Liu, Z.R.2
  • 16
    • 12544250752 scopus 로고    scopus 로고
    • RNA structural rearrangement via unwinding and annealing by the cyanobacterial RNA helicase
    • Chamot D, Colvin KR, Kujat-Choy SL, Owttrim GW. RNA structural rearrangement via unwinding and annealing by the cyanobacterial RNA helicase. CrhR J Biol Chem 2005, 280:2036-2044.
    • (2005) CrhR J Biol Chem , vol.280 , pp. 2036-2044
    • Chamot, D.1    Colvin, K.R.2    Kujat-Choy, S.L.3    Owttrim, G.W.4
  • 17
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
    • Rogers GW Jr, Richter NJ, Merrick WC. Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J Biol Chem 1999, 274:12236-12244.
    • (1999) J Biol Chem , vol.274 , pp. 12236-12244
    • Rogers Jr, G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 18
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • Rogers GW Jr, Lima WF, Merrick WC. Further characterization of the helicase activity of eIF4A. Substrate specificity. J Biol Chem 2001, 276:12598-12608.
    • (2001) J Biol Chem , vol.276 , pp. 12598-12608
    • Rogers Jr, G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 19
    • 58149503706 scopus 로고    scopus 로고
    • DEAD-box proteins can completely separate an RNA duplex using a single ATP
    • Chen Y, Potratz JP, Tijerina P, Del Campo M, Lambowitz AM, Russell R.
    • Chen Y, Potratz JP, Tijerina P, Del Campo M, Lambowitz AM, Russell R. DEAD-box proteins can completely separate an RNA duplex using a single ATP. Proc Natl Acad Sci U S A 2008, 105:20203-20208.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20203-20208
  • 20
    • 2942754127 scopus 로고    scopus 로고
    • Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases
    • Bizebard T, Ferlenghi I, Iost I, Dreyfus M. Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry 2004, 43:7857-7866.
    • (2004) Biochemistry , vol.43 , pp. 7857-7866
    • Bizebard, T.1    Ferlenghi, I.2    Iost, I.3    Dreyfus, M.4
  • 21
    • 33947362880 scopus 로고    scopus 로고
    • Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA
    • Grohman JK, Del Campo M, Bhaskaran H, Tijerina P, Lambowitz AM, Russell R.
    • Grohman JK, Del Campo M, Bhaskaran H, Tijerina P, Lambowitz AM, Russell R. Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA. Biochemistry 2007, 46:3013-3022.
    • (2007) Biochemistry , vol.46 , pp. 3013-3022
  • 22
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F, Putnam A, Jankowsky E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc Natl Acad Sci U S A 2008, 105:20209-20214.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 23
    • 33750593917 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
    • Yang Q, Jankowsky E. The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nat Struct Mol Biol 2006, 13:981-986.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 24
    • 35348941874 scopus 로고    scopus 로고
    • DEAD-box proteins unwind duplexes by local strand separation
    • Yang Q, Del Campo M, Lambowitz AM, Jankowsky E. DEAD-box proteins unwind duplexes by local strand separation. Mol Cell 2007, 28:253-263.
    • (2007) Mol Cell , vol.28 , pp. 253-263
    • Yang, Q.1    Del Campo, M.2    Lambowitz, A.M.3    Jankowsky, E.4
  • 25
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen F, Edery I, Meerovitch K, Dever TE, Merrick WC, Sonenberg N.
    • Rozen F, Edery I, Meerovitch K, Dever TE, Merrick WC, Sonenberg N. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol Cell Biol 1990, 10:1134-1144.
    • (1990) Mol Cell Biol , vol.10 , pp. 1134-1144
  • 26
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls C, Mohr S, Del Campo M, Yang Q, Jankowsky E, Lambowitz AM.
    • Halls C, Mohr S, Del Campo M, Yang Q, Jankowsky E, Lambowitz AM. Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J Mol Biol 2007, 365:835-855.
    • (2007) J Mol Biol , vol.365 , pp. 835-855
  • 27
    • 33750936780 scopus 로고    scopus 로고
    • Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone
    • Tijerina P, Bhaskaran H, Russell R. Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone. Proc Natl Acad Sci U S A 2006, 103:16698-16703.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16698-16703
    • Tijerina, P.1    Bhaskaran, H.2    Russell, R.3
  • 28
    • 0027301893 scopus 로고
    • DbpA: a DEAD box protein specifically activated by 23S rRNA
    • Fuller-Pace FV, Nicol SM, Reid AD, Lane DP. DbpA: a DEAD box protein specifically activated by 23S rRNA. EMBO J 1993, 12:3619-3626.
    • (1993) EMBO J , vol.12 , pp. 3619-3626
    • Fuller-Pace, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 29
    • 0035046795 scopus 로고    scopus 로고
    • The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA
    • Tsu CA, Kossen K, Uhlenbeck OC. The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA. RNA 2001, 7:702-709.
    • (2001) RNA , vol.7 , pp. 702-709
    • Tsu, C.A.1    Kossen, K.2    Uhlenbeck, O.C.3
  • 30
    • 0035476705 scopus 로고    scopus 로고
    • Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
    • Diges CM, Uhlenbeck OC. Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA. EMBO J 2001, 20:5503-5512.
    • (2001) EMBO J , vol.20 , pp. 5503-5512
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 31
    • 27444442034 scopus 로고    scopus 로고
    • YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain
    • Karginov FV, Caruthers JM, Hu Y, McKay DB, Uhlenbeck OC. YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. J Biol Chem 2005, 280:35499-35505.
    • (2005) J Biol Chem , vol.280 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 32
    • 33646883060 scopus 로고    scopus 로고
    • The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold
    • Wang S, Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC, McKay DB.
    • Wang S, Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC, McKay DB. The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. RNA 2006, 12:959-967.
    • (2006) RNA , vol.12 , pp. 959-967
  • 33
    • 37749032415 scopus 로고    scopus 로고
    • The Bacillus subtilis RNA helicase YxiN is distended in solution
    • Wang S, Overgaard MT, Hu Y, McKay DB. The Bacillus subtilis RNA helicase YxiN is distended in solution. Biophys J 2008, 94:L01-L03.
    • (2008) Biophys J , vol.94
    • Wang, S.1    Overgaard, M.T.2    Hu, Y.3    McKay, D.B.4
  • 34
    • 54549123661 scopus 로고    scopus 로고
    • The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity
    • Linden MH, Hartmann RK, Klostermeier D. The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity. Nucleic Acids Res 2008, 36:5800-5811.
    • (2008) Nucleic Acids Res , vol.36 , pp. 5800-5811
    • Linden, M.H.1    Hartmann, R.K.2    Klostermeier, D.3
  • 35
    • 70350098206 scopus 로고    scopus 로고
    • The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core
    • Rudolph MG, Klostermeier D. The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core. RNA 2009, 15:1993-2001.
    • (2009) RNA , vol.15 , pp. 1993-2001
    • Rudolph, M.G.1    Klostermeier, D.2
  • 36
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • Mohr G, Del Campo M, Mohr S, Yang Q, Jia H, Jankowsky E, Lambowitz AM.
    • Mohr G, Del Campo M, Mohr S, Yang Q, Jia H, Jankowsky E, Lambowitz AM. Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro. J Mol Biol 2008, 375:1344-1364.
    • (2008) J Mol Biol , vol.375 , pp. 1344-1364
  • 37
    • 59649110939 scopus 로고    scopus 로고
    • A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility
    • Klostermeier D, Rudolph MG. A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. Nucleic Acids Res 2009, 37:421-430.
    • (2009) Nucleic Acids Res , vol.37 , pp. 421-430
    • Klostermeier, D.1    Rudolph, M.G.2
  • 38
    • 36749016233 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events
    • Tran EJ, Zhou Y, Corbett AH, Wente SR. The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events. Mol Cell 2007, 28:850-859.
    • (2007) Mol Cell , vol.28 , pp. 850-859
    • Tran, E.J.1    Zhou, Y.2    Corbett, A.H.3    Wente, S.R.4
  • 39
    • 33846702294 scopus 로고    scopus 로고
    • Ratcheting mRNA out of the nucleus
    • Stewart M. Ratcheting mRNA out of the nucleus. Mol Cell 2007, 25:327-330.
    • (2007) Mol Cell , vol.25 , pp. 327-330
    • Stewart, M.1
  • 40
    • 41449091393 scopus 로고    scopus 로고
    • mRNA export: RNP remodeling by DEAD-box proteins
    • Linder P. mRNA export: RNP remodeling by DEAD-box proteins. Curr Biol 2008, 18:R297-R299.
    • (2008) Curr Biol , vol.18
    • Linder, P.1
  • 41
    • 0033517108 scopus 로고    scopus 로고
    • Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p
    • Schmitt C, von Kobbe C, Bachi A, Pante N, Rodrigues JP, Boscheron C, Rigaut G, Wilm M, Seraphin B, Carmo-Fonseca M, et al.
    • Schmitt C, von Kobbe C, Bachi A, Pante N, Rodrigues JP, Boscheron C, Rigaut G, Wilm M, Seraphin B, Carmo-Fonseca M, et al. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. EMBO J 1999, 18:4332-4347.
    • (1999) EMBO J , vol.18 , pp. 4332-4347
  • 42
    • 0033569962 scopus 로고    scopus 로고
    • Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells
    • Hodge CA, Colot HV, Stafford P, Cole CN. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J 1999, 18:5778-5788.
    • (1999) EMBO J , vol.18 , pp. 5778-5788
    • Hodge, C.A.1    Colot, H.V.2    Stafford, P.3    Cole, C.N.4
  • 43
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich CS, Erzberger JP, Flick JS, Berger JM, Thorner J, Weis K.
    • Weirich CS, Erzberger JP, Flick JS, Berger JM, Thorner J, Weis K. Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat Cell Biol 2006, 8:668-676.
    • (2006) Nat Cell Biol , vol.8 , pp. 668-676
  • 44
    • 70349513606 scopus 로고    scopus 로고
    • Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1
    • Dossani ZY, Weirich CS, Erzberger JP, Berger JM, Weis K. Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1. Proc Natl Acad Sci U S A 2009, 106:16251-16256.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16251-16256
    • Dossani, Z.Y.1    Weirich, C.S.2    Erzberger, J.P.3    Berger, J.M.4    Weis, K.5
  • 45
    • 62549108142 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19
    • Napetschnig J, Kassube SA, Debler EW, Wong RW, Blobel G, Hoelz A.
    • Napetschnig J, Kassube SA, Debler EW, Wong RW, Blobel G, Hoelz A. Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19. Proc Natl Acad Sci U S A 2009, 106:3089-3094.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3089-3094
  • 46
    • 62049084648 scopus 로고    scopus 로고
    • The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner
    • von Moeller H, Basquin C, Conti E. The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner. Nat Struct Mol Biol 2009, 16:247-254.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 247-254
    • von Moeller, H.1    Basquin, C.2    Conti, E.3
  • 47
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • Oberer M, Marintchev A, Wagner G. Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev 2005, 19:2212-2223.
    • (2005) Genes Dev , vol.19 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 48
    • 72149105341 scopus 로고    scopus 로고
    • The ELAV protein HuD stimulates cap-dependent translation in a Poly(A)- and eIF4A-dependent manner
    • Fukao A, Sasano Y, Imataka H, Inoue K, Sakamoto H, Sonenberg N, Thoma C, Fujiwara T.
    • Fukao A, Sasano Y, Imataka H, Inoue K, Sakamoto H, Sonenberg N, Thoma C, Fujiwara T. The ELAV protein HuD stimulates cap-dependent translation in a Poly(A)- and eIF4A-dependent manner. Mol Cell 2009, 36:1007-1017.
    • (2009) Mol Cell , vol.36 , pp. 1007-1017
  • 49
    • 77953370114 scopus 로고    scopus 로고
    • Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex
    • Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E.
    • Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. Proc Natl Acad Sci U S A 2010, 107:10050-10055.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10050-10055
  • 50
    • 47749123500 scopus 로고    scopus 로고
    • Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions
    • Schutz P, Bumann M, Oberholzer AE, Bieniossek C, Trachsel H, Altmann M, Baumann U.
    • Schutz P, Bumann M, Oberholzer AE, Bieniossek C, Trachsel H, Altmann M, Baumann U. Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions. Proc Natl Acad Sci U S A 2008, 105:9564-9569.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9564-9569
  • 51
    • 61649102918 scopus 로고    scopus 로고
    • Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B
    • Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O.
    • Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O. Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B. Mol Cell 2009, 33:661-668.
    • (2009) Mol Cell , vol.33 , pp. 661-668
  • 52
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley JP, Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 1998, 92:315-326.
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 53
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • Lorsch JR, Herschlag D. The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry 1998, 37:2180-2193.
    • (1998) Biochemistry , vol.37 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 54
    • 84872575238 scopus 로고    scopus 로고
    • Mechanisms of DEAD-box proteins in ATP-dependent processes.
    • Jankowsky E, ed. Cambridge, UK: Royal Society of Chemistry. RSC Biomolecular Sciences No. 19;
    • Potratz JP, Tijerina P, Russell R. Mechanisms of DEAD-box proteins in ATP-dependent processes. In: Jankowsky E, ed. RNA Helicases. Cambridge, UK: Royal Society of Chemistry. RSC Biomolecular Sciences No. 19; 2010, 61-98.
    • (2010) RNA Helicases , pp. 61-98
    • Potratz, J.P.1    Tijerina, P.2    Russell, R.3
  • 55
    • 77950349699 scopus 로고    scopus 로고
    • Motif III in superfamily 2 "helicases" helps convert the binding energy of ATP into a high-affinity RNA binding site in the yeast DEAD-box protein Ded1
    • Banroques J, Doere M, Dreyfus M, Linder P, Tanner NK. Motif III in superfamily 2 "helicases" helps convert the binding energy of ATP into a high-affinity RNA binding site in the yeast DEAD-box protein Ded1. J Mol Biol 2010, 396:949-966.
    • (2010) J Mol Biol , vol.396 , pp. 949-966
    • Banroques, J.1    Doere, M.2    Dreyfus, M.3    Linder, P.4    Tanner, N.K.5
  • 56
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA
    • Del Campo M, Lambowitz AM. Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell 2009, 35:598-609.
    • (2009) Mol Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 57
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER, McKay DB. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci U S A 2000, 97:13080-13085.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 58
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story RM, Li H, Abelson JN. Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc Natl Acad Sci U S A 2001, 98:1465-1470.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 59
    • 11144222543 scopus 로고    scopus 로고
    • Crystal structure of the human ATP-dependent splicing and export factor UAP56
    • Shi H, Cordin O, Minder CM, Linder P, Xu RM. Crystal structure of the human ATP-dependent splicing and export factor UAP56. Proc Natl Acad Sci U S A 2004, 101:17628-17633.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17628-17633
    • Shi, H.1    Cordin, O.2    Minder, C.M.3    Linder, P.4    Xu, R.M.5
  • 60
    • 23644449094 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of DEAD-box protein Dhh1p
    • Cheng Z, Coller J, Parker R, Song H. Crystal structure and functional analysis of DEAD-box protein Dhh1p. RNA 2005, 11:1258-1270.
    • (2005) RNA , vol.11 , pp. 1258-1270
    • Cheng, Z.1    Coller, J.2    Parker, R.3    Song, H.4
  • 61
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 2006, 125:287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 62
    • 33749332762 scopus 로고    scopus 로고
    • Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA
    • Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Seraphin B, Le Hir H, Andersen GR.
    • Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Seraphin B, Le Hir H, Andersen GR. Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. Science 2006, 313:1968-1972.
    • (2006) Science , vol.313 , pp. 1968-1972
  • 63
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono F, Ebert J, Lorentzen E, Conti E. The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 2006, 126:713-725.
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 64
    • 34547751991 scopus 로고    scopus 로고
    • Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP
    • Hogbom M, Collins R, van den Berg S, Jenvert RM, Karlberg T, Kotenyova T, Flores A, Karlsson Hedestam GB, Schiavone LH.
    • Hogbom M, Collins R, van den Berg S, Jenvert RM, Karlberg T, Kotenyova T, Flores A, Karlsson Hedestam GB, Schiavone LH. Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP. J Mol Biol 2007, 372:150-159.
    • (2007) J Mol Biol , vol.372 , pp. 150-159
  • 65
    • 63649159790 scopus 로고    scopus 로고
    • Solution and crystal structures of mRNA exporter Dbp5p and its interaction with nucleotides
    • Fan JS, Cheng Z, Zhang J, Noble C, Zhou Z, Song H, Yang D.
    • Fan JS, Cheng Z, Zhang J, Noble C, Zhou Z, Song H, Yang D. Solution and crystal structures of mRNA exporter Dbp5p and its interaction with nucleotides. J Mol Biol 2009, 388:1-10.
    • (2009) J Mol Biol , vol.388 , pp. 1-10
  • 66
    • 67449105353 scopus 로고    scopus 로고
    • The DEXD/H-box RNA helicase DDX19 is regulated by an α-helical switch
    • Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H.
    • Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H. The DEXD/H-box RNA helicase DDX19 is regulated by an α-helical switch. J Biol Chem 2009, 284:10296-10300.
    • (2009) J Biol Chem , vol.284 , pp. 10296-10300
  • 67
    • 58149092125 scopus 로고    scopus 로고
    • Mechanism of ATP turnover inhibition in the EJC
    • Nielsen KH, Chamieh H, Andersen CB, Fredslund F, Hamborg K, Le Hir H, Andersen GR.
    • Nielsen KH, Chamieh H, Andersen CB, Fredslund F, Hamborg K, Le Hir H, Andersen GR. Mechanism of ATP turnover inhibition in the EJC. RNA 2009, 15:67-75.
    • (2009) RNA , vol.15 , pp. 67-75
  • 68
    • 0035032444 scopus 로고    scopus 로고
    • ′ secondary structure
    • Svitkin YV, Pause A, Haghighat A, Pyronnet S, Witherell G, Belsham GJ, Sonenberg N.
    • ′ secondary structure. RNA 2001, 7:382-394.
    • (2001) RNA , vol.7 , pp. 382-394
  • 69
    • 43249100378 scopus 로고    scopus 로고
    • A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins
    • Banroques J, Cordin O, Doere M, Linder P, Tanner NK. A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins. Mol Cell Biol 2008, 28:3359-3371.
    • (2008) Mol Cell Biol , vol.28 , pp. 3359-3371
    • Banroques, J.1    Cordin, O.2    Doere, M.3    Linder, P.4    Tanner, N.K.5
  • 70
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys 2008, 37:317-336.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 71
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Buttner K, Nehring S, Hopfner KP. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat Struct Mol Biol 2007, 14:647-652.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.P.3
  • 72
    • 0024415732 scopus 로고
    • A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity
    • Rozen F, Pelletier J, Trachsel H, Sonenberg N. A lysine substitution in the ATP-binding site of eucaryotic initiation factor 4A abrogates nucleotide-binding activity. Mol Cell Biol 1989, 9:4061-4063.
    • (1989) Mol Cell Biol , vol.9 , pp. 4061-4063
    • Rozen, F.1    Pelletier, J.2    Trachsel, H.3    Sonenberg, N.4
  • 73
    • 0026668609 scopus 로고
    • ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae
    • Blum S, Schmid SR, Pause A, Buser P, Linder P, Sonenberg N, Trachsel H.
    • Blum S, Schmid SR, Pause A, Buser P, Linder P, Sonenberg N, Trachsel H. ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 1992, 89:7664-7668.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7664-7668
  • 74
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A
    • Pause A, Sonenberg N. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J 1992, 11:2643-2654.
    • (1992) EMBO J , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 75
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause A, Methot N, Sonenberg N. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol Cell Biol 1993, 13:6789-6798.
    • (1993) Mol Cell Biol , vol.13 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 76
    • 0033580840 scopus 로고    scopus 로고
    • Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase
    • Iost I, Dreyfus M, Linder P. Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J Biol Chem 1999, 274:17677-17683.
    • (1999) J Biol Chem , vol.274 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 77
    • 14244260321 scopus 로고    scopus 로고
    • Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs
    • Rocak S, Emery B, Tanner NK, Linder P. Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs. Nucleic Acids Res 2005, 33:999-1009.
    • (2005) Nucleic Acids Res , vol.33 , pp. 999-1009
    • Rocak, S.1    Emery, B.2    Tanner, N.K.3    Linder, P.4
  • 78
    • 33847652952 scopus 로고    scopus 로고
    • A DEAD protein that activates intron self-splicing without unwinding RNA
    • Solem A, Zingler N, Pyle AM. A DEAD protein that activates intron self-splicing without unwinding RNA. Mol Cell 2006, 24:611-617.
    • (2006) Mol Cell , vol.24 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.3
  • 79
    • 67949115632 scopus 로고    scopus 로고
    • A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN
    • Karow AR, Klostermeier D. A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN. Nucleic Acids Res 2009, 37:4464-4471.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4464-4471
    • Karow, A.R.1    Klostermeier, D.2
  • 80
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner NK, Cordin O, Banroques J, Doere M, Linder P. The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol Cell 2003, 11:127-138.
    • (2003) Mol Cell , vol.11 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 81
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • Cordin O, Tanner NK, Doere M, Linder P, Banroques J. The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J 2004, 23:2478-2487.
    • (2004) EMBO J , vol.23 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 82
    • 0032562221 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes
    • Lorsch JR, Herschlag D. The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes. Biochemistry 1998, 37:2194-2206.
    • (1998) Biochemistry , vol.37 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 83
    • 38649106732 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
    • Theissen B, Karow AR, Kohler J, Gubaev A, Klostermeier D. Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. Proc Natl Acad Sci U S A 2008, 105:548-553.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 548-553
    • Theissen, B.1    Karow, A.R.2    Kohler, J.3    Gubaev, A.4    Klostermeier, D.5
  • 84
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • Polach KJ, Uhlenbeck OC. Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry 2002, 41:3693-3702.
    • (2002) Biochemistry , vol.41 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2
  • 85
    • 39649096274 scopus 로고    scopus 로고
    • The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
    • Henn A, Cao W, Hackney DD, De La Cruz EM. The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. J Mol Biol 2008, 377:193-205.
    • (2008) J Mol Biol , vol.377 , pp. 193-205
    • Henn, A.1    Cao, W.2    Hackney, D.D.3    De La Cruz, E.M.4
  • 86
    • 77749239820 scopus 로고    scopus 로고
    • Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA
    • Henn A, Cao W, Licciardello N, Heitkamp SE, Hackney DD, De La Cruz EM.
    • Henn A, Cao W, Licciardello N, Heitkamp SE, Hackney DD, De La Cruz EM. Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proc Natl Acad Sci U S A 2010, 107:4046-4050.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4046-4050
  • 87
    • 77950361633 scopus 로고    scopus 로고
    • Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase
    • Wang Q, Arnold JJ, Uchida A, Raney KD, Cameron CE. Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase. Nucleic Acids Res 2010, 38:1312-1324.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1312-1324
    • Wang, Q.1    Arnold, J.J.2    Uchida, A.3    Raney, K.D.4    Cameron, C.E.5
  • 88
    • 19644362046 scopus 로고    scopus 로고
    • Escherichia coli DbpA is a 3′→ 5′ RNA helicase
    • Diges CM, Uhlenbeck OC. Escherichia coli DbpA is a 3′→ 5′ RNA helicase Biochemistry 2005, 44:7903-7911.
    • (2005) Biochemistry , vol.44 , pp. 7903-7911
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 89
    • 0016526609 scopus 로고
    • Acceleration of RNA renaturation by nucleic acid unwinding proteins
    • Karpel RL, Swistel DG, Miller NS, Geroch ME, Lu C, Fresco JR.
    • Karpel RL, Swistel DG, Miller NS, Geroch ME, Lu C, Fresco JR. Acceleration of RNA renaturation by nucleic acid unwinding proteins. Brookhaven Symp Biol 1975, 26:165-174.
    • (1975) Brookhaven Symp Biol , vol.26 , pp. 165-174
  • 90
    • 0020492233 scopus 로고
    • Mechanistic studies of ribonucleic acid renaturation by a helix-destabilizing protein
    • Karpel RL, Miller NS, Fresco JR. Mechanistic studies of ribonucleic acid renaturation by a helix-destabilizing protein. Biochemistry 1982, 21:2102-2108.
    • (1982) Biochemistry , vol.21 , pp. 2102-2108
    • Karpel, R.L.1    Miller, N.S.2    Fresco, J.R.3
  • 91
    • 39049131090 scopus 로고    scopus 로고
    • RNA chaperones, RNA annealers and RNA helicases
    • Rajkowitsch L, Chen D, Stampfl S, Semrad K, Waldsich C, Mayer O, Jantsch MF, Konrat R, Blasi U, Schroeder R.
    • Rajkowitsch L, Chen D, Stampfl S, Semrad K, Waldsich C, Mayer O, Jantsch MF, Konrat R, Blasi U, Schroeder R. RNA chaperones, RNA annealers and RNA helicases. RNA Biol 2007, 4:118-130.
    • (2007) RNA Biol , vol.4 , pp. 118-130
  • 92
    • 0037077127 scopus 로고    scopus 로고
    • DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr S, Stryker JM, Lambowitz AMA. DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell 2002, 109:769-779.
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.A.3
  • 94
    • 38449108345 scopus 로고    scopus 로고
    • RNA misfolding and the action of chaperones
    • Russell R. RNA misfolding and the action of chaperones. Front Biosci 2008, 13:1-20.
    • (2008) Front Biosci , vol.13 , pp. 1-20
    • Russell, R.1
  • 95
    • 0030452773 scopus 로고    scopus 로고
    • New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme
    • Lehnert V, Jaeger L, Michel F, Westhof E. New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme. Chem Biol 1996, 3:993-1009.
    • (1996) Chem Biol , vol.3 , pp. 993-1009
    • Lehnert, V.1    Jaeger, L.2    Michel, F.3    Westhof, E.4
  • 96
    • 41749109563 scopus 로고    scopus 로고
    • Crystal structure of a self-spliced group II intron
    • Toor N, Keating KS, Taylor SD, Pyle AM. Crystal structure of a self-spliced group II intron. Science 2008, 320:77-82.
    • (2008) Science , vol.320 , pp. 77-82
    • Toor, N.1    Keating, K.S.2    Taylor, S.D.3    Pyle, A.M.4
  • 97
    • 75649084603 scopus 로고    scopus 로고
    • Tertiary architecture of the Oceanobacillus iheyensis group II intron
    • Toor N, Keating KS, Fedorova O, Rajashankar K, Wang J, Pyle AM.
    • Toor N, Keating KS, Fedorova O, Rajashankar K, Wang J, Pyle AM. Tertiary architecture of the Oceanobacillus iheyensis group II intron. RNA 2010, 16:57-69.
    • (2010) RNA , vol.16 , pp. 57-69
  • 98
    • 33748936120 scopus 로고    scopus 로고
    • The paradoxical behavior of a highly structured misfolded intermediate in RNA folding
    • Russell R, Das R, Suh H, Travers KJ, Laederach A, Engelhardt MA, Herschlag D.
    • Russell R, Das R, Suh H, Travers KJ, Laederach A, Engelhardt MA, Herschlag D. The paradoxical behavior of a highly structured misfolded intermediate in RNA folding. J Mol Biol 2006, 363:531-544.
    • (2006) J Mol Biol , vol.363 , pp. 531-544
  • 99
    • 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, 62:670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 100
    • 34547146401 scopus 로고    scopus 로고
    • The mechanism of Hsp70 chaperones: (entropic) pulling the models together
    • Goloubinoff P, De Los Rios P. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem Sci 2007, 32:372-380.
    • (2007) Trends Biochem Sci , vol.32 , pp. 372-380
    • Goloubinoff, P.1    De Los Rios, P.2
  • 101
    • 35548989806 scopus 로고    scopus 로고
    • Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone
    • Bhaskaran H, Russell R. Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone. Nature 2007, 449:1014-1018.
    • (2007) Nature , vol.449 , pp. 1014-1018
    • Bhaskaran, H.1    Russell, R.2
  • 102
    • 67349117103 scopus 로고    scopus 로고
    • Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones
    • Del Campo M, Mohr S, Jiang Y, Jia H, Jankowsky E, Lambowitz AM.
    • Del Campo M, Mohr S, Jiang Y, Jia H, Jankowsky E, Lambowitz AM. Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones. J Mol Biol 2009, 389: 674-693.
    • (2009) J Mol Biol , vol.389 , pp. 674-693
  • 103
    • 33644852160 scopus 로고    scopus 로고
    • DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone
    • Mohr S, Matsuura M, Perlman PS, Lambowitz AMA. DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone. Proc Natl Acad Sci U S A 2006, 103:3569-3574.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3569-3574
    • Mohr, S.1    Matsuura, M.2    Perlman, P.S.3    Lambowitz, A.M.A.4
  • 104
    • 34948833173 scopus 로고    scopus 로고
    • Do DEAD-box proteins promote group II intron splicing without unwinding RNA?
    • Del Campo M, Tijerina P, Bhaskaran H, Mohr S, Yang Q, Jankowsky E, Russell R, Lambowitz AM.
    • Del Campo M, Tijerina P, Bhaskaran H, Mohr S, Yang Q, Jankowsky E, Russell R, Lambowitz AM. Do DEAD-box proteins promote group II intron splicing without unwinding RNA? Mol Cell 2007, 28:159-166.
    • (2007) Mol Cell , vol.28 , pp. 159-166
  • 105
    • 77649337588 scopus 로고    scopus 로고
    • Protein-facilitated folding of group II intron ribozymes
    • Fedorova O, Solem A, Pyle AM. Protein-facilitated folding of group II intron ribozymes. J Mol Biol 2010, 397:799-813.
    • (2010) J Mol Biol , vol.397 , pp. 799-813
    • Fedorova, O.1    Solem, A.2    Pyle, A.M.3
  • 106
    • 0033010430 scopus 로고    scopus 로고
    • ′ splice site requires ATP and the DEAD box protein Prp28p
    • ′ splice site requires ATP and the DEAD box protein Prp28p. Mol Cell 1999, 3:55-64.
    • (1999) Mol Cell , vol.3 , pp. 55-64
    • Staley, J.P.1    Guthrie, C.2
  • 107
    • 0037781588 scopus 로고    scopus 로고
    • Yeast RNA helicases of the DEAD-box family involved in translation initiation
    • Linder P. Yeast RNA helicases of the DEAD-box family involved in translation initiation. Biol Cell 2003, 95:157-167.
    • (2003) Biol Cell , vol.95 , pp. 157-167
    • Linder, P.1
  • 108
    • 33746253985 scopus 로고    scopus 로고
    • Unwinding single RNA molecules using helicases involved in eukaryotic translation initiation
    • Marsden S, Nardelli M, Linder P, McCarthy JE. Unwinding single RNA molecules using helicases involved in eukaryotic translation initiation. J Mol Biol 2006, 361:327-335.
    • (2006) J Mol Biol , vol.361 , pp. 327-335
    • Marsden, S.1    Nardelli, M.2    Linder, P.3    McCarthy, J.E.4
  • 109
    • 78049293801 scopus 로고    scopus 로고
    • Dual roles for the Mss116 cofactor during splicing of the ai5γ group II intron
    • Zingler N, Solem A, Pyle AM. Dual roles for the Mss116 cofactor during splicing of the ai5γ group II intron. Nucleic Acids Res 2010.
    • (2010) Nucleic Acids Res
    • Zingler, N.1    Solem, A.2    Pyle, A.M.3
  • 110
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir H, Izaurralde E, Maquat LE, Moore MJ. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J 2000, 19:6860-6869.
    • (2000) EMBO J , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 111
    • 1842577707 scopus 로고    scopus 로고
    • eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay
    • Shibuya T, Tange TO, Sonenberg N, Moore MJ. eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay. Nat Struct Mol Biol 2004, 11:346-351.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 346-351
    • Shibuya, T.1    Tange, T.O.2    Sonenberg, N.3    Moore, M.J.4
  • 112
    • 2342443461 scopus 로고    scopus 로고
    • Protein displacement by DExH/D "RNA helicases" without duplex unwinding
    • Fairman ME, et al. Protein displacement by DExH/D "RNA helicases" without duplex unwinding. Science 2004, 304:730-734.
    • (2004) Science , vol.304 , pp. 730-734
    • Fairman, M.E.1
  • 113
    • 33646181578 scopus 로고    scopus 로고
    • Discriminatory RNP remodeling by the DEAD-box protein DED1
    • Bowers HA, Maroney PA, Fairman ME, Kastner B, Luhrmann R, Nilsen TW, Jankowsky E.
    • Bowers HA, Maroney PA, Fairman ME, Kastner B, Luhrmann R, Nilsen TW, Jankowsky E. Discriminatory RNP remodeling by the DEAD-box protein DED1. RNA 2006, 12:903-912.
    • (2006) RNA , vol.12 , pp. 903-912
  • 114
    • 44949117567 scopus 로고    scopus 로고
    • A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release
    • Schwer B. A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release. Mol Cell 2008, 30:743-754.
    • (2008) Mol Cell , vol.30 , pp. 743-754
    • Schwer, B.1
  • 115
    • 26644450709 scopus 로고    scopus 로고
    • ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
    • Yang Q, Jankowsky E. ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry 2005, 44:13591-13601.
    • (2005) Biochemistry , vol.44 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.