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Volumn 3, Issue 3, 2009, Pages 204-212

The tumbleweed: Towards a synthetic protein motor

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EID: 70350665969     PISSN: 19552068     EISSN: 1955205X     Source Type: Journal    
DOI: 10.2976/1.3111282     Document Type: Article
Times cited : (36)

References (83)
  • 1
    • 31944435091 scopus 로고    scopus 로고
    • Computational design of a single amino acid sequence that can switch between two distinct protein folds
    • Ambroggio, XI, and Kuhlman, B (2006). "Computational design of a single amino acid sequence that can switch between two distinct protein folds." J. Am. Chem. Soc. 128(4), 1154-1161.
    • (2006) J. Am. Chem. Soc , vol.128 , Issue.4 , pp. 1154-1161
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 2
    • 12344259551 scopus 로고    scopus 로고
    • Kinesin: World's tiniest biped
    • Asbury, CL (2005). "Kinesin: world's tiniest biped." Curr. Opin. Cell Biol. 17, 89-97.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 89-97
    • Asbury, C.L.1
  • 3
    • 0031003997 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of a Brownian motor
    • Astumian, RD (1997). "Thermodynamics and kinetics of a Brownian motor." Science 276(5314), 917-922.
    • (1997) Science , vol.276 , Issue.5314 , pp. 917-922
    • Astumian, R.D.1
  • 4
    • 34548810775 scopus 로고    scopus 로고
    • Design principles for Brownian molecular machines: How to swim in molasses and walk in a hurricane
    • Astumian, RD (2007). "Design principles for Brownian molecular machines: how to swim in molasses and walk in a hurricane." Phys. Chem. Chem. Phys. 9(37), 5067-5083.
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , Issue.37 , pp. 5067-5083
    • Astumian, R.D.1
  • 5
    • 0036855051 scopus 로고    scopus 로고
    • Brownian motors
    • Astumian, RD, and Hänggi, P (2002). "Brownian motors." Phys. Today 55(11), 33-39.
    • (2002) Phys. Today , vol.55 , Issue.11 , pp. 33-39
    • Astumian, R.D.1    Hänggi, P.2
  • 6
    • 33750227536 scopus 로고    scopus 로고
    • Artificial nanomachines based on interlocked molecular species: Recent advances
    • Balzani, V, Credi, A, Silvi, S, and Venturi, M (2006). "Artificial nanomachines based on interlocked molecular species: recent advances." Chem. Soc. Rev. 35(11), 1135-1149.
    • (2006) Chem. Soc. Rev. , vol.35 , Issue.11 , pp. 1135-1149
    • Balzani, V.1    Credi, A.2    Silvi, S.3    Venturi, M.4
  • 8
    • 22744435502 scopus 로고    scopus 로고
    • A free-running DNA motor powered by a nicking enzyme
    • Bath, J, Green, SJ, and Turberfield, AJ (2005). "A free-running DNA motor powered by a nicking enzyme." Angew. Chem., Int. Ed. 44(28), 4358-4361.
    • (2005) Angew. Chem., Int. Ed. , vol.44 , Issue.28 , pp. 4358-4361
    • Bath, J.1    Green, S.J.2    Turberfield, A.J.3
  • 11
    • 34247571461 scopus 로고    scopus 로고
    • Kinesin motor mechanics: Binding, stepping, tracking, gating, and limping
    • Block, SM (2007). "Kinesin motor mechanics: binding, stepping, tracking, gating, and limping." Biophys. J. 92(9), 2986-2995.
    • (2007) Biophys. J , vol.92 , Issue.9 , pp. 2986-2995
    • Block, S.M.1
  • 12
    • 0026042785 scopus 로고
    • Determination of the orientations of tryptophan analogues bound to the TRP repressor and the relationship to activation
    • Borden, KLB, Beckmann, P, and Lane, AN (1991). "Determination of the orientations of tryptophan analogues bound to the TRP repressor and the relationship to activation." Eur. J. Biochem. 202(2), 459-470.
    • (1991) Eur. J. Biochem. , vol.202 , Issue.2 , pp. 459-470
    • Borden, K.L.B.1    Beckmann, P.2    Lane, A.N.3
  • 13
    • 38749117220 scopus 로고    scopus 로고
    • Peptide and protein building blocks for synthetic biology: From programming biomolecules to self-organized biomolecular systems
    • Bromley, EHC, Channon, K, Moutevelis, E, and Woolfson, DN (2008). "Peptide and protein building blocks for synthetic biology: from programming biomolecules to self-organized biomolecular systems." Chem. Biol. 3(1), 38-50.
    • (2008) Chem. Biol. , vol.3 , Issue.1 , pp. 38-50
    • Bromley, E.1    Channon, K.2    Moutevelis, E.3    Woolfson, D.N.4
  • 15
    • 0034847378 scopus 로고    scopus 로고
    • The physics of molecular motors
    • Bustamante, C, Keller, D, and Oster, G (2001). "The physics of molecular motors." Acc. Chem. Res. 34(6), 412-420.
    • (2001) Acc. Chem. Res. , vol.34 , Issue.6 , pp. 412-420
    • Bustamante, C.1    Keller, D.2    Oster, G.3
  • 16
    • 0023955176 scopus 로고
    • Gel retardation at low PH resolves TRP repressor-DNA complexes for quantitative study
    • Carey, J (1988). "Gel retardation at low PH resolves TRP repressor-DNA complexes for quantitative study." Proc. Natl. Acad. Sci. U.S.A. 85(4), 975-979.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , Issue.4 , pp. 975-979
    • Carey, J.1
  • 17
    • 27544509859 scopus 로고    scopus 로고
    • ZiCo: A peptide designed to switch folded state upon binding zinc
    • Cerasoli, E, Sharpe, BK, and Woolfson, DN (2005). "ZiCo: a peptide designed to switch folded state upon binding zinc." J. Am. Chem. Soc. 127, 15008-15009.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15008-15009
    • Cerasoli, E.1    Sharpe, B.K.2    Woolfson, D.N.3
  • 18
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins
    • Ciani, B, Hutchinson, EG, Sessions, RB, and Woolfson, DN (2002). "A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins." J. Biol. Chem. 277(12), 10150-10155.
    • (2002) J. Biol. Chem. , vol.277 , Issue.12 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 19
    • 0028238102 scopus 로고
    • Calorimetric studies of the energetics of protein-DNA interaction in the Escherichia-coli methionine repressor (METJ) system
    • Cooper, A, McAlpine, A, and Stockley, PG (1994). "Calorimetric studies of the energetics of protein-DNA interaction in the Escherichia-coli methionine repressor (METJ) system." FEBS Lett. 348(1), 41-45.
    • (1994) FEBS Lett , vol.348 , Issue.1 , pp. 41-45
    • Cooper, A.1    McAlpine, A.2    Stockley, P.G.3
  • 20
    • 80051827838 scopus 로고    scopus 로고
    • A mechanokinetic model for the myosin V walking mechanism
    • Craig, E, and Linke, H (2009). "A mechanokinetic model for the myosin V walking mechanism." Biophys. J., 96(3), 128a.
    • (2009) Biophys. J , vol.96 , Issue.3
    • Craig, E.1    Linke, H.2
  • 22
    • 34548760154 scopus 로고    scopus 로고
    • The art of building small: From molecular switches to molecular motors
    • Feringa, BL (2007). "The art of building small: from molecular switches to molecular motors." J. Org. Chem. 72(18), 6635-6652.
    • (2007) J. Org. Chem. , vol.72 , Issue.18 , pp. 6635-6652
    • Feringa, B.L.1
  • 23
    • 84927374884 scopus 로고
    • Feynman's office: The last blackboards
    • Feynman, R (1989). "Feynman's office: the last blackboards." Phys. Today 42, 88.
    • (1989) Phys. Today , vol.42 , Issue.88
    • Feynman, R.1
  • 24
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics-piconewton forces and nanometer steps
    • Finer, JT, Simmons, RM, and Spudich, JA (1994). "Single myosin molecule mechanics-piconewton forces and nanometer steps." Nature (London) 368(6467), 113-119.
    • (1994) Nature (London) , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 25
    • 0042343679 scopus 로고    scopus 로고
    • Surface plasmon resonance studies of wild-type and AV77 tryptophan repressor resolve ambiguities in super-repressor activity
    • Finucane, MD, and Jardetzky, O (2003). "Surface plasmon resonance studies of wild-type and AV77 tryptophan repressor resolve ambiguities in super-repressor activity." Protein Sci. 12, 1612-1620.
    • (2003) Protein Sci , vol.12 , pp. 1612-1620
    • Finucane, M.D.1    Jardetzky, O.2
  • 26
    • 0034665030 scopus 로고    scopus 로고
    • Direct and indirect readout in mutant Met repressor-operator complexes
    • Garvie, CW, and Phillips, SEV (2000). "Direct and indirect readout in mutant Met repressor-operator complexes." Structure (London) 8(9), 905-914.
    • (2000) Structure (London) , vol.8 , Issue.9 , pp. 905-914
    • Garvie, C.W.1    Phillips, S.E.V.2
  • 27
    • 0032804235 scopus 로고    scopus 로고
    • The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions
    • Glasfeld, A, Koehler, AN, Schumacher, MA, and Brennan, RG (1999). "The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions." J. Mol. Biol. 291(2), 347-361.
    • (1999) J. Mol. Biol. , vol.291 , Issue.2 , pp. 347-361
    • Glasfeld, A.1    Koehler, A.N.2    Schumacher, M.A.3    Brennan, R.G.4
  • 29
    • 0031561795 scopus 로고    scopus 로고
    • A model for the mechanism of polymerase translocation
    • Guajardo, R, and Sousa, R (1997). "A model for the mechanism of polymerase translocation." J. Mol. Biol. 265(1), 8-19.
    • (1997) J. Mol. Biol. , vol.265 , Issue.1 , pp. 8-19
    • Guajardo, R.1    Sousa, R.2
  • 31
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J (1997). "Molecular motors: structural adaptations to cellular functions." Nature (London) 389(6651), 561-567.
    • (1997) Nature (London) , vol.389 , Issue.6651 , pp. 561-567
    • Howard, J.1
  • 32
    • 33745972061 scopus 로고    scopus 로고
    • Protein power strokes
    • Howard, J (2006). "Protein power strokes." Curr. Biol. 16(14), R517-R519.
    • (2006) Curr. Biol. , vol.16 , Issue.14
    • Howard, J.1
  • 33
    • 40449116114 scopus 로고    scopus 로고
    • De novo computational design of retro-aldol enzymes
    • Jiang, L, et al. (2008). "De novo computational design of retro-aldol enzymes." Science 319, 1387-1391.
    • (2008) Science , vol.319 , pp. 1387-1391
    • Jiang, L.1
  • 34
  • 35
    • 41349106934 scopus 로고    scopus 로고
    • Dynamics of molecular motors with finite processivity on heterogeneous tracks
    • Kafri, Y, Lubensky, DK, and Nelson, DR (2005). "Dynamics of molecular motors with finite processivity on heterogeneous tracks." Phys. Rev. E 71(4), 041906.
    • (2005) Phys. Rev. E. , vol.71 , Issue.4 , pp. 041906
    • Kafri, Y.1    Lubensky, D.K.2    Nelson, D.R.3
  • 36
    • 33846152351 scopus 로고    scopus 로고
    • Synthetic molecular motors and mechanical machines
    • Kay, ER, Leigh, DA, and Zerbetto, F (2007). "Synthetic molecular motors and mechanical machines." Angew. Chem., Int. Ed. 46(1-2), 72-191.
    • (2007) Angew. Chem., Int. Ed. , vol.46 , Issue.1-2 , pp. 72-191
    • Kay, E.R.1    Leigh, D.A.2    Zerbetto, F.3
  • 38
    • 0346762537 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • Kitamura, K, Tokunaga, M, Iwane, AH, and Yanagida, T (1999). "A single myosin head moves along an actin filament with regular steps of 5.3 nanometres." Nature (London) 397(6715), 129-134.
    • (1999) Nature (London) , vol.397 , Issue.6715 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 39
    • 0030824684 scopus 로고    scopus 로고
    • Mechanics of single kinesin molecules measured by optical trapping nanometry
    • Kojima, H, Muto, E, Higuchi, H, and Yanagida, T (1997). "Mechanics of single kinesin molecules measured by optical trapping nanometry." Biophys. J. 73(4), 2012-2022.
    • (1997) Biophys. J , vol.73 , Issue.4 , pp. 2012-2022
    • Kojima, H.1    Muto, E.2    Higuchi, H.3    Yanagida, T.4
  • 40
    • 33847272113 scopus 로고    scopus 로고
    • Molecular motors: A theorist's perspective
    • Kolomeisky, AB, and Fisher, ME (2007). "Molecular motors: a theorist's perspective." Annu. Rev. Phys. Chem. 58, 675-695.
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 675-695
    • Kolomeisky, A.B.1    Fisher, M.E.2
  • 41
    • 18044376803 scopus 로고    scopus 로고
    • Artificial molecular rotors
    • (Washington, D.C.)
    • Kottas, GS, Clarke, LI, Horinek, D, and Michl, J (2005). "Artificial molecular rotors." Chem. Rev. (Washington, D.C.) 105(4), 1281-1376.
    • (2005) Chem. Rev. , vol.105 , Issue.4 , pp. 1281-1376
    • Kottas, G.S.1    Clarke, L.I.2    Horinek, D.3    Michl, J.4
  • 42
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomiclevel accuracy
    • Kuhlman, B, Dantas, G, Ireton, GC, Varani, G, Stoddard, BL, and Baker, D (2003). "Design of a novel globular protein fold with atomiclevel accuracy." Science 302(5649), 1364-1368.
    • (2003) Science , vol.302 , Issue.5649 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 43
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a Trp repressoroperator half-site complex
    • Lawson, CL (1993). "Tandem binding in crystals of a Trp repressoroperator half-site complex." Nature (London) 366(6451), 178-182.
    • (1993) Nature (London) , vol.366 , Issue.6451 , pp. 178-182
    • Lawson, C.L.1
  • 44
    • 34548528158 scopus 로고    scopus 로고
    • Progress in computational protein design
    • Lippow, SM, and Tidor, B (2007). "Progress in computational protein design." Curr. Opin. Biotechnol. 18(4), 305-311.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , Issue.4 , pp. 305-311
    • Lippow, S.M.1    Tidor, B.2
  • 45
    • 33747859373 scopus 로고    scopus 로고
    • RosettaDesign server for protein design
    • Liu, Y, and Kuhlman, B (2006). "RosettaDesign server for protein design." Nucleic Acids Res. 34, W235-W238.
    • (2006) Nucleic Acids Res , vol.34
    • Liu, Y.1    Kuhlman, B.2
  • 46
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas, AN (2005). "The structure of alpha-helical coiled coils." Adv. Protein Chem. 70, 37-78.
    • (2005) Adv. Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1
  • 47
    • 49649121725 scopus 로고    scopus 로고
    • From biological towards artificial molecular motors
    • Mickler, M, Schleiff, E, and Hugel, T (2008). "From biological towards artificial molecular motors." ChemPhysChem 9(11), 1503-1509.
    • (2008) ChemPhysChem , vol.9 , Issue.11 , pp. 1503-1509
    • Mickler, M.1    Schleiff, E.2    Hugel, T.3
  • 48
    • 13244279669 scopus 로고
    • Structural comparison of the free and DNAbound forms of the purine repressor DNA-binding domain
    • Nagadoi, A, et al. (1995). "Structural comparison of the free and DNAbound forms of the purine repressor DNA-binding domain." Structure (London) 3(11), 1217-1224.
    • (1995) Structure (London) , vol.3 , Issue.11 , pp. 1217-1224
    • Nagadoi, A.1
  • 49
    • 0142122076 scopus 로고    scopus 로고
    • Single molecule processes on the stepwise movement of ATP-driven molecular motors
    • Nishiyama, M, Higuchi, H, Ishii, Y, Taniguchi, Y, and Yanagida, T (2003). "Single molecule processes on the stepwise movement of ATP-driven molecular motors." BioSystems 71(1-2), 145-156.
    • (2003) BioSystems , vol.71 , Issue.1-2 , pp. 145-156
    • Nishiyama, M.1    Higuchi, H.2    Ishii, Y.3    Taniguchi, Y.4    Yanagida, T.5
  • 50
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F-1-ATPase
    • Noji, H, Yasuda, R, Yoshida, M, and Kinosita, K (1997). "Direct observation of the rotation of F-1-ATPase." Nature (London) 386(6622), 299-302.
    • (1997) Nature (London) , vol.386 , Issue.6622 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 52
    • 11244335621 scopus 로고    scopus 로고
    • Sequence and structural duality: Designing peptides to adopt two stable conformations
    • Pandya, MJ, Cerasoli, E, Joseph, A, Stoneman, RG, Waite, E, and Woolfson, DN (2004). "Sequence and structural duality: designing peptides to adopt two stable conformations." J. Am. Chem. Soc. 126(51), 17016-17024.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.51 , pp. 17016-17024
    • Pandya, M.J.1    Cerasoli, E.2    Joseph, A.3    Stoneman, R.G.4    Waite, E.5    Woolfson, D.N.6
  • 53
    • 0028963302 scopus 로고
    • Probing the molecular mechanism of action of co-repressor in the E. coli methionine repressor-operator complex using surface-plasmon resonance (SPR)
    • Parsons, ID, Persson, B, Mekhalfia, A, Blackburn, GM, and Stockley, PG (1995). "Probing the molecular mechanism of action of co-repressor in the E. coli methionine repressor-operator complex using surface-plasmon resonance (SPR)." Nucleic Acids Res. 23(2), 211-216.
    • (1995) Nucleic Acids Res , vol.23 , Issue.2 , pp. 211-216
    • Parsons, I.D.1    Persson, B.2    Mekhalfia, A.3    Blackburn, G.M.4    Stockley, P.G.5
  • 55
    • 0028773287 scopus 로고
    • Electrostatic activation of Escherichia-coli methionine repressor
    • Phillips, K, and Phillips, SE V (1994). "Electrostatic activation of Escherichia-coli methionine repressor." Structure (London) 2(4), 309-316.
    • (1994) Structure (London) , vol.2 , Issue.4 , pp. 309-316
    • Phillips, K.1    Phillips, S.2
  • 56
    • 33746592898 scopus 로고    scopus 로고
    • Knowledge-based potentials in protein design
    • Poole, AM, and Ranganathan, R (2006). "Knowledge-based potentials in protein design." Curr. Opin. Struct. Biol. 16(4), 508-513.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , Issue.4 , pp. 508-513
    • Poole, A.M.1    Ranganathan, R.2
  • 57
    • 0031592940 scopus 로고    scopus 로고
    • Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides
    • Reedstrom, RJ, Brown, MP, Grillo, A, Roen, D, and Royer, CA (1997). "Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides." J. Mol. Biol. 273(3), 572-585.
    • (1997) J. Mol. Biol. , vol.273 , Issue.3 , pp. 572-585
    • Reedstrom, R.J.1    Brown, M.P.2    Grillo, A.3    Roen, D.4    Royer, C.A.5
  • 58
    • 0036681042 scopus 로고    scopus 로고
    • Introduction to the physics of Brownian motors
    • Reimann, P, and Hänggi, P (2002). "Introduction to the physics of Brownian motors." Appl. Phys. A: Mater. Sci. Process. 75(2), 169-178.
    • (2002) Appl. Phys. A: Mater. Sci. Process. , vol.75 , Issue.2 , pp. 169-178
    • Reimann, P.1    Hänggi, P.2
  • 59
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • Rice, S, et al. (1999). "A structural change in the kinesin motor protein that drives motility." Nature (London) 402(6763), 778-784.
    • (1999) Nature (London) , vol.402 , Issue.6763 , pp. 778-784
    • Rice, S.1
  • 61
    • 0025182048 scopus 로고
    • Purification of the Escherichia-coli purine regulon repressor and identification of co-repressors
    • Rolfes, RJ, and Zalkin, H (1990). "Purification of the Escherichia-coli purine regulon repressor and identification of co-repressors." J. Bacteriol. 172(10), 5637-5642.
    • (1990) J. Bacteriol , vol.172 , Issue.10 , pp. 5637-5642
    • Rolfes, R.J.1    Zalkin, H.2
  • 63
    • 0035146785 scopus 로고    scopus 로고
    • Conformational changes during kinesin motility
    • Schief, WR, and Howard, J (2001). "Conformational changes during kinesin motility." Curr. Opin. Cell Biol. 13, 19-28.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 19-28
    • Schief, W.R.1    Howard, J.2
  • 64
    • 0034306462 scopus 로고    scopus 로고
    • Force production by single kinesin motors
    • Schnitzer, MJ, Visscher, K, and Block, SM (2000). "Force production by single kinesin motors." Nat. Cell Biol. 2(10), 718-723.
    • (2000) Nat. Cell Biol. , vol.2 , Issue.10 , pp. 718-723
    • Schnitzer, M.J.1    Visscher, K.2    Block, S.M.3
  • 65
    • 0028810684 scopus 로고
    • Mechanism of corepressor-mediated specific DNA-binding by the purine repressor
    • Schumacher, MA, Choi, KY, Lu, F, Zalkin, H and Brennan, RG (1995). "Mechanism of corepressor-mediated specific DNA-binding by the purine repressor." Cell 83(1), 147-155.
    • (1995) Cell , vol.83 , Issue.1 , pp. 147-155
    • Schumacher, M.A.1    Choi, K.Y.2    Lu, F.3    Zalkin, H.4    Brennan, R.G.5
  • 66
    • 0028173030 scopus 로고
    • Crystalstructure of LacI member, PurR, bound to DNA-minor-groove binding by alpha-helices
    • Schumacher, MA, Choi, KY, Zalkin, H, and Brennan, RG (1994). "Crystalstructure of LacI member, PurR, bound to DNA-minor-groove binding by alpha-helices." Science 266(5186), 763-770.
    • (1994) Science , vol.266 , Issue.5186 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 68
    • 4444298687 scopus 로고    scopus 로고
    • A synthetic DNA walker for molecular transport
    • Shin, JS, and Pierce, NA (2004). "A synthetic DNA walker for molecular transport." J. Am. Chem. Soc. 126(35), 10834-10835.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.35 , pp. 10834-10835
    • Shin, J.S.1    Pierce, N.A.2
  • 69
    • 0032531265 scopus 로고    scopus 로고
    • Dissecting the molecular details of prokaryotic transcriptional control by surface plasmon resonance: The methionine and arginine repressor proteins
    • Stockley, PG, Baron, AJ, Wild, CM, Parsons, ID, Miller, CM, Holtham, CAM, and Baumberg, S (1998). "Dissecting the molecular details of prokaryotic transcriptional control by surface plasmon resonance: the methionine and arginine repressor proteins." Biosens. Bioelectron. 13, 637-650.
    • (1998) Biosens. Bioelectron. , vol.13 , pp. 637-650
    • Stockley, P.G.1    Baron, A.J.2    Wild, C.M.3    Parsons, I.D.4    Miller, C.M.5    Holtham, C.A.M.6    Baumberg, S.7
  • 70
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K, Schmidt, CF, Schnapp, BJ, and Block, SM (1993). "Direct observation of kinesin stepping by optical trapping interferometry." Nature (London) 365(6448), 721-727.
    • (1993) Nature (London) , vol.365 , Issue.6448 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 71
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, RD, and Milligan, RA (2000). "The way things move: looking under the hood of molecular motor proteins." Science 288(5463), 88-95.
    • (2000) Science , vol.288 , Issue.5463 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 72
    • 0025222740 scopus 로고
    • Protein motors and Maxwell's demons: Does mechanochemical transduction involve a thermal ratchet?
    • Vale, RD, and Oosawa, F (1990). "Protein motors and Maxwell's demons: does mechanochemical transduction involve a thermal ratchet?" Adv. Biophys. 26, 97-134.
    • (1990) Adv. Biophys. , vol.26 , pp. 97-134
    • Vale, R.D.1    Oosawa, F.2
  • 73
    • 0031934004 scopus 로고    scopus 로고
    • Force generation in RNA polymerase
    • Wang, HY, Elston, T, Mogilner, A, and Oster, G (1998). "Force generation in RNA polymerase." Biophys. J. 74(3), 1186-1202.
    • (1998) Biophys. J , vol.74 , Issue.3 , pp. 1186-1202
    • Wang, H.Y.1    Elston, T.2    Mogilner, A.3    Oster, G.4
  • 74
    • 0032547899 scopus 로고    scopus 로고
    • Energy transduction in the F-1 motor of ATP synthase
    • Wang, HY, and Oster, G (1998). "Energy transduction in the F-1 motor of ATP synthase." Nature (London) 396(6708), 279-282.
    • (1998) Nature (London) , vol.396 , Issue.6708 , pp. 279-282
    • Wang, H.Y.1    Oster, G.2
  • 75
    • 58849148610 scopus 로고    scopus 로고
    • Quantitative transcription factor binding kinetics at the single-molecule level
    • Wang, Y, Guo, L, Cox, EC, and Ong, NP (2009). "Quantitative transcription factor binding kinetics at the single-molecule level." Biophys. J. 96, 609-620.
    • (2009) Biophys. J , vol.96 , pp. 609-620
    • Wang, Y.1    Guo, L.2    Cox, E.C.3    Ong, N.P.4
  • 76
    • 34147196369 scopus 로고    scopus 로고
    • When is a distribution not a distribution, and why would you care: Singlemolecule measurements of repressor protein 1-D diffusion on DNA
    • Springer, Berlin
    • Wang, YM, Flyvbjerg, H, Cox, EC, and Austin, RH (2007). "When is a distribution not a distribution, and why would you care: singlemolecule measurements of repressor protein 1-D diffusion on DNA." Controlled Nanoscale Motion, Vol. 711, pp. 217-240 Springer, Berlin.
    • (2007) Controlled Nanoscale Motion , vol.711 , pp. 217-240
    • Wang, Y.M.1    Flyvbjerg, H.2    Cox, E.C.3    Austin, R.H.4
  • 78
    • 0028930479 scopus 로고
    • Invitro motility of immunoadsorbed brain myosin-V using a limulus acrosomal process and optical tweezer-based assay
    • Wolenski, JS, Cheney, RE, Mooseker, MS, and Forscher, P (1995). "Invitro motility of immunoadsorbed brain myosin-V using a limulus acrosomal process and optical tweezer-based assay." J. Cell. Sci. 108, 1489-1496.
    • (1995) J. Cell. Sci. , vol.108 , pp. 1489-1496
    • Wolenski, J.S.1    Cheney, R.E.2    Mooseker, M.S.3    Forscher, P.4
  • 79
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson, DN (2005). "The design of coiled-coil structures and assemblies." Adv. Protein Chem. 70, 79-112.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 80
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz, A, Forkey, JN, McKinney, SA, Ha, T, Goldman, YE, and Selvin, PR (2003). "Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization." Science 300(5628), 2061-2065.
    • (2003) Science , vol.300 , Issue.5628 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 82
    • 34147200710 scopus 로고    scopus 로고
    • Using DNA to power the nanoworld
    • Yurke, B (2007). "Using DNA to power the nanoworld." Lect. Notes Phys. 711, 331-347.
    • (2007) Lect. Notes Phys. , vol.711 , pp. 331-347
    • Yurke, B.1
  • 83
    • 0023256884 scopus 로고
    • The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity
    • Zhang, RG, Joachimiak, A, Lawson, CL, Schevitz, RW, Otwinowski, Z, and Sigler, PB (1987). "The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity." Nature (London) 327(6123), 591-597.
    • (1987) Nature (London) , vol.327 , Issue.6123 , pp. 591-597
    • Zhang, R.G.1    Joachimiak, A.2    Lawson, C.L.3    Schevitz, R.W.4    Otwinowski, Z.5    Sigler, P.B.6


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