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Volumn 13, Issue 15, 2008, Pages 5732-5754

In vitro assays of molecular motors - Impact of motor-surface interactions

Author keywords

Actomyosin; Adsorption; Heavy meromoysin; In vitro motility assay; Review

Indexed keywords

MOLECULAR MOTOR; MYOSIN SUBFRAGMENT; PEPTIDE FRAGMENT;

EID: 52049121034     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3112     Document Type: Review
Times cited : (28)

References (169)
  • 4
    • 0034859387 scopus 로고    scopus 로고
    • Controlling the direction of kinesin-driven microtubule movements along microlithographic tracks
    • Y Hiratsuka, T Tada, K Oiwa, T Kanayama, TQ Uyeda: Controlling the direction of kinesin-driven microtubule movements along microlithographic tracks. Biophys J 81, 1555-61. (2001) (Pubitemid 32783595)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1555-1561
    • Hiratsuka, Y.1    Tada, T.2    Oiwa, K.3    Kanayama, T.4    Uyeda, T.Q.P.5
  • 5
    • 0141744884 scopus 로고    scopus 로고
    • Lithographically patterned channels spatially segregate kinesin motor activity and effectively guide microtubule movements
    • DOI 10.1021/nl034001b
    • SG Moorjani, L Jia, TN Jackson, WO Hancock: Lithographically patterned channels spatially segregate kinesin motor activity and effectively guide microtubule movements. Nano Letters 3, 633-637 (2003) (Pubitemid 37140628)
    • (2003) Nano Letters , vol.3 , Issue.5 , pp. 633-637
    • Moorjani, S.G.1    Jia, L.2    Jackson, T.N.3    Hancock, W.O.4
  • 7
    • 33847397775 scopus 로고    scopus 로고
    • Materials chemistry challenges in the design of hybrid bionanodevices: Supporting protein function within artificial environments
    • DOI 10.1039/b615278c
    • T Fischer, H Hess: Materials chemistry challenges in the design of hybrid bionanodevices: supporting protein function within artificial environments. Journal of Materials Chemistry 17, 943-951 (2007) (Pubitemid 46339449)
    • (2007) Journal of Materials Chemistry , vol.17 , Issue.10 , pp. 943-951
    • Fischer, T.1    Hess, H.2
  • 8
    • 35948956283 scopus 로고    scopus 로고
    • Mode of heavy meromyosin adsorption and motor function correlated with surface hydrophobicity and charge
    • DOI 10.1021/la7008682
    • N Albet-Torres, J O'Mahony, C Charlton, M Balaz, P Lisboa, T Aastrup, A Mansson, IA Nicholls: Mode of Heavy Meromyosin Adsorption and Motor Function Correlated with Surface Hydrophobicity and Charge. Langmuir 23, 11147-11156 (2007) (Pubitemid 350069339)
    • (2007) Langmuir , vol.23 , Issue.22 , pp. 11147-11156
    • Albet-Torres, N.1    O'Mahony, J.2    Charlton, C.3    Balaz, M.4    Lisboa, P.5    Aastrup, T.6    Mansson, A.7    Nicholls, I.A.8
  • 9
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • DOI 10.1021/bm061197b
    • F Rusmini, ZY Zhong, J Feijen: Protein immobilization strategies for protein biochips. Biomacromolecules 8, 1775-1789 (2007) (Pubitemid 47009952)
    • (2007) Biomacromolecules , vol.8 , Issue.6 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 10
    • 0037051037 scopus 로고    scopus 로고
    • Biological surface science
    • DOI 10.1016/S0039-6028(01)01809-X, PII S003960280101809X
    • B Kasemo: Biological surface science. Surface Science 500, 656-677 (2002) (Pubitemid 34222920)
    • (2002) Surface Science , vol.500 , Issue.1-3 , pp. 656-677
    • Kasemo, B.1
  • 11
    • 0029027492 scopus 로고
    • Flexibility of myosin attachment to surfaces influences F-actin motion
    • DA Winkelmann, L Bourdieu, A Ott, F Kinose, A Libchaber: Flexibility of myosin attachment to surfaces influences F-actin motion. Biophys J 68, 2444-53 (1995)
    • (1995) Biophys J , vol.68 , pp. 2444-2453
    • Winkelmann, D.A.1    Bourdieu, L.2    Ott, A.3    Kinose, F.4    Libchaber, A.5
  • 12
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • DOI 10.1016/S0092-8674(00)80911-3
    • A Ishijima, H Kojima, T Funatsu, M Tokunaga, H Higuchi, H Tanaka, T Yanagida: Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92, 161-71 (1998) (Pubitemid 28073040)
    • (1998) Cell , vol.92 , Issue.2 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 14
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • DOI 10.1038/368113a0
    • JT Finer, RM Simmons, JA Spudich: Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113-9 (1994) (Pubitemid 24101520)
    • (1994) Nature , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 17
    • 34249672266 scopus 로고    scopus 로고
    • Protein linear molecular motor-powered nanodevices
    • DOI 10.1071/CH06456
    • DJG Bakewell, DV Nicolau: Protein linear molecular motor-powered nanodevices. Aust J Chem 60, 314-332 (2007) (Pubitemid 46838778)
    • (2007) Australian Journal of Chemistry , vol.60 , Issue.5 , pp. 314-332
    • Bakewell, D.J.G.1    Nicolau, D.V.2
  • 18
    • 34547118553 scopus 로고    scopus 로고
    • Motor proteins at work for nanotechnology
    • DOI 10.1126/science.1139570
    • MGL van den Heuvel, C Dekker: Motor proteins at work for nanotechnology. Science 317, 333-336 (2007) (Pubitemid 47106365)
    • (2007) Science , vol.317 , Issue.5836 , pp. 333-336
    • Van Den Heuvel, M.G.L.1    Dekker, C.2
  • 19
    • 0001711774 scopus 로고    scopus 로고
    • Light-controlled molecular shuttles made from motor proteins carrying cargo on engineered surfaces
    • DOI 10.1021/nl015521e
    • H Hess, J Clemmens, D Qin, J Howard, V Vogel: Light-controlled molecular shuttles made from motor proteins carrying cargo on engineered surfaces. Nano Letters 1, 235-239 (2001) (Pubitemid 33673324)
    • (2001) Nano Letters , vol.1 , Issue.5 , pp. 235-239
    • Hess, H.1    Clemmens, J.2    Qin, D.3    Howard, J.4    Vogel, V.5
  • 20
    • 33749651750 scopus 로고    scopus 로고
    • Reversible switching of microtubule motility using thermoresponsive polymer surfaces
    • DOI 10.1021/nl0611539
    • L Ionov, M Stamm, S Diez: Reversible switching of microtubule motility using thermoresponsive polymer surfaces. Nano Letters 6, 1982-1987 (2006) (Pubitemid 44555241)
    • (2006) Nano Letters , vol.6 , Issue.9 , pp. 1982-1987
    • Ionov, L.1    Stamm, M.2    Diez, S.3
  • 21
    • 0031663377 scopus 로고    scopus 로고
    • Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains
    • DOI 10.1006/jsbi.1998.3980
    • RJC Levine, ZH Yang, ND Epstein, L Fananapazir, JT Stull, HL Sweeney: Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J Struct Biol 122, 149-161 (1998) (Pubitemid 28411195)
    • (1998) Journal of Structural Biology , vol.122 , Issue.1-2 , pp. 149-161
    • Levine, R.J.C.1    Yang, Z.2    Epstein, N.D.3    Fananapazir, L.4    Stull, J.T.5    Sweeney, H.L.6
  • 22
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • DM Warshaw, JM Desrosiers, SS Work, KM Trybus: Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J Cell Biol 111, 453-63 (1990)
    • (1990) J Cell Biol , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4
  • 23
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • DOI 10.1016/j.sbi.2003.12.001
    • JJ Gray: The interaction of proteins with solid surfaces. Curr Opin Struct Biol 14, 110-5 (2004) (Pubitemid 38249599)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 110-115
    • Gray, J.J.1
  • 24
    • 34147200355 scopus 로고    scopus 로고
    • Nanotechnology enhanced functional assays of actomyosin motility -potentials and challenges
    • Eds: Linke H, Mansson A, Springer, Berlin Heidelberg Germany
    • A Mansson, IA Nicholls, P Omling, S Tagerud, L Montelius: Nanotechnology enhanced functional assays of actomyosin motility -potentials and challenges. In: Controlled nanoscale motion, Lecture Notes in Physics 711 Eds: Linke H, Mansson A, Springer, Berlin Heidelberg. Germany, 385-406 (2007)
    • (2007) Controlled Nanoscale Motion, Lecture Notes in Physics , vol.711 , pp. 385-406
    • Mansson, A.1    Nicholls, I.A.2    Omling, P.3    Tagerud, S.4    Montelius, L.5
  • 25
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • DOI 10.1016/S1389-1723(01)80127-4
    • K Nakanishi, T Sakiyama, K Imamura: On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J Biosci Bioeng 91, 233-244 (2001) (Pubitemid 32324614)
    • (2001) Journal of Bioscience and Bioengineering , vol.91 , Issue.3 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 26
    • 0030026989 scopus 로고    scopus 로고
    • Protein adsorption on solid surfaces
    • DOI 10.1016/S0958-1669(96)80098-X
    • V Hlady, J Buijs: Protein adsorption on solid surfaces. Current Opin Biotechnol 7, 72-77 (1996) (Pubitemid 26066591)
    • (1996) Current Opinion in Biotechnology , vol.7 , Issue.1 , pp. 72-77
    • Hlady, V.1    Buijs, J.2
  • 27
    • 0021001513 scopus 로고
    • Movement of myosin-coated structures on actin cables
    • MP Sheetz, JA Spudich: Movement of myosin-coated structures on actin cables. Cell Motil 3, 485-9 (1983)
    • (1983) Cell Motil , vol.3 , pp. 485-489
    • Sheetz, M.P.1    Spudich, J.A.2
  • 28
    • 0022263118 scopus 로고
    • Movement of myosin-coated beads on oriented filaments reconstituted from purified actin
    • DOI 10.1038/315584a0
    • JA Spudich, SJ Kron, MP Sheetz: Movement of myosin-coated beads on oriented filaments reconstituted from purified actin. Nature 315, 584-6 (1985) (Pubitemid 15021197)
    • (1985) Nature , vol.315 , Issue.6020 , pp. 584-586
    • Spudich, J.A.1    Kron, S.J.2    Sheetz, M.P.3
  • 31
    • 0027736090 scopus 로고
    • In vitro methods for measuring force and velocity of the actin-myosin interaction using purified proteins
    • HM Warrick, RM Simmons, JT Finer, TQ Uyeda, S Chu, JA Spudich: In vitro methods for measuring force and velocity of the actin-myosin interaction using purified proteins. Methods Cell Biol 39, 1-21 (1993)
    • (1993) Methods Cell Biol , vol.39 , pp. 1-21
    • Warrick, H.M.1    Simmons, R.M.2    Finer, J.T.3    Uyeda, T.Q.4    Chu, S.5    Spudich, J.A.6
  • 32
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Y Harada, K Sakurada, T Aoki, DD Thomas, T Yanagida: Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol 216, 49-68. (1990) (Pubitemid 20376174)
    • (1990) Journal of Molecular Biology , vol.216 , Issue.1 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 33
    • 0026522849 scopus 로고
    • Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin
    • E Homsher, F Wang, JR Sellers: Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am J Physiol 262, C714-23. (1992)
    • (1992) Am J Physiol , vol.262
    • Homsher, E.1    Wang, F.2    Sellers, J.R.3
  • 35
    • 0023919181 scopus 로고
    • Force Measurements by Micromanipulation of a Single Actin Filament by Glass Needles
    • A Kishino, T Yanagida: Force Measurements by Micromanipulation of a Single Actin Filament by Glass Needles. Nature 334, 74-76 (1988)
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 43
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Y Takagi, EE Homsher, YE Goldman, H Shuman: Force generation in single conventional actomyosin complexes under high dynamic load. Biophys J 90, 1295-307 (2006)
    • (2006) Biophys J , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 44
    • 0035123582 scopus 로고    scopus 로고
    • Single-molecule tracking of myosins with genetically engineered amplifier domains
    • DOI 10.1038/84962
    • C Ruff, M Furch, B Brenner, DJ Manstein, E Meyhofer: Single-molecule tracking of myosins with genetically engineered amplifier domains. Nat Struct Biol 8, 226-229 (2001) (Pubitemid 32180047)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 226-229
    • Ruff, C.1    Furch, M.2    Brenner, B.3    Manstein, D.J.4    Meyhofer, E.5
  • 45
    • 0031668720 scopus 로고    scopus 로고
    • Orientation dependence of displacements by a single one-headed myosin relative to the actin filament
    • H Tanaka, A Ishijima, M Honda, K Saito, T Yanagida: Orientation dependence of displacements by a single oneheaded myosin relative to the actin filament. Biophys J 75, 1886-94 (1998) (Pubitemid 28455183)
    • (1998) Biophysical Journal , vol.75 , Issue.4 , pp. 1886-1894
    • Tanaka, H.1    Ishijima, A.2    Honda, M.3    Saito, K.4    Yanagida, T.5
  • 46
    • 0142187316 scopus 로고    scopus 로고
    • Random walks with thin filaments: Application of in vitro motility assay to the study of actomyosin regulation
    • DOI 10.1023/A:1026097313020
    • S Marston: Random walks with thin filaments: application of in vitro motility assay to the study of actomyosin regulation. J Muscle Res Cell Motil 24, 149-156 (2003) (Pubitemid 37323618)
    • (2003) Journal of Muscle Research and Cell Motility , vol.24 , Issue.2-3 , pp. 149-156
    • Marston, S.1
  • 47
    • 34547118553 scopus 로고    scopus 로고
    • Motor proteins at work for nanotechnology
    • DOI 10.1126/science.1139570
    • MG van den Heuvel, C Dekker: Motor proteins at work for nanotechnology. Science 317, 333-6 (2007) (Pubitemid 47106365)
    • (2007) Science , vol.317 , Issue.5836 , pp. 333-336
    • Van Den Heuvel, M.G.L.1    Dekker, C.2
  • 48
    • 23244468520 scopus 로고    scopus 로고
    • Muscle contraction: Actin filaments enter the fray
    • DOI 10.1529/biophysj.105.059501
    • JE Molloy: Muscle contraction: actin filaments enter the fray. Biophys J 89, 1-2 (2005) (Pubitemid 41098256)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 1-2
    • Molloy, J.E.1
  • 49
    • 0042929817 scopus 로고    scopus 로고
    • Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform
    • DOI 10.1023/A:1024871825135
    • T Scholz, B Brenner: Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform. J Muscle Res Cell Motil 24, 77-86 (2003) (Pubitemid 37011531)
    • (2003) Journal of Muscle Research and Cell Motility , vol.24 , Issue.1 , pp. 77-86
    • Scholz, T.1    Brenner, B.2
  • 50
    • 0033500246 scopus 로고    scopus 로고
    • A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers
    • DOI 10.1023/A:1005658825375
    • E Thedinga, N Karim, T Kraft, B Brenner: A singlefiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers. J Muscle Res Cell Motil 20, 785-96. (1999) (Pubitemid 30128726)
    • (1999) Journal of Muscle Research and Cell Motility , vol.20 , Issue.8 , pp. 785-796
    • Thedinga, E.1    Karim, N.2    Kraft, T.3    Brenner, B.4
  • 51
    • 0032797863 scopus 로고    scopus 로고
    • Speeds of actin translocation in vitro by myosins extracted from single rat muscle fibres of different types
    • DOI 10.1017/S0958067099003504
    • M Canepari, R Rossi, MA Pellegrino, C Reggiani, R Bottinelli: Speeds of actin translocation in vitro by myosins extracted from single rat muscle fibres of different types. Exp Physiol 84, 803-6 (1999) (Pubitemid 29401734)
    • (1999) Experimental Physiology , vol.84 , Issue.4 , pp. 803-806
    • Canepari, M.1    Rossi, R.2    Pellegrino, M.A.3    Reggiani, C.4    Bottinelli, R.5
  • 52
    • 0033808411 scopus 로고    scopus 로고
    • Actomyosin interactions in a novel single muscle fiber in vitro motility assay
    • P Hook, L Larsson: Actomyosin interactions in a novel single muscle fiber in vitro motility assay. J Muscle Res Cell Motil 21, 357-65. (2000)
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 357-365
    • Hook, P.1    Larsson, L.2
  • 56
    • 0030805052 scopus 로고    scopus 로고
    • Bi-directional movement of actin filaments along long bipolar tracks of oriented rabbit skeletal muscle myosin molecules
    • DOI 10.1016/S0014-5793(97)00558-9, PII S0014579397005589
    • A Yamada, M Yoshio, H Nakayama: Bi-directional movement of actin filaments along long bipolar tracks of oriented rabbit skeletal muscle myosin molecules. FEBS Lett 409, 380-4 (1997) (Pubitemid 27285890)
    • (1997) FEBS Letters , vol.409 , Issue.3 , pp. 380-384
    • Yamada, A.1    Yoshio, M.2    Nakayama, H.3
  • 57
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • AM Gordon, E Homsher, M Regnier: Regulation of contraction in striated muscle. Physiol Rev 80, 853-924. (2000) (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 58
    • 14044259423 scopus 로고    scopus 로고
    • 2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin
    • DOI 10.1074/jbc.M412473200
    • S Fujita-Becker, U Durrwang, M Erent, RJ Clark, MA Geeves, DJ Manstein: Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin. J Biol Chem 280, 6064-71 (2005) (Pubitemid 40280090)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 6064-6071
    • Fujita-Becker, S.1    Durrwang, U.2    Erent, M.3    Clark, R.J.4    Geeves, M.A.5    Manstein, D.J.6
  • 59
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • DOI 10.1074/jbc.R100005200
    • AP Minton: The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 276, 10577-80 (2001) (Pubitemid 38089223)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10577-10580
    • Minton, A.P.1
  • 60
    • 31944433387 scopus 로고    scopus 로고
    • Reconciling the working strokes of a single head of skeletal muscle myosin estimated from laser-trap experiments and crystal structures
    • DOI 10.1073/pnas.0506272103
    • J Sleep, A Lewalle, D Smith: Reconciling the working strokes of a single head of skeletal muscle myosin estimated from laser-trap experiments and crystal structures. Proc Natl Acad Sci U S A 103, 1278-1282 (2006) (Pubitemid 43191156)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.5 , pp. 1278-1282
    • Sleep, J.1    Lewalle, A.2    Smith, D.3
  • 61
    • 0037444025 scopus 로고    scopus 로고
    • Multivariate statistics in analysis of data from the in vitro motility assay
    • DOI 10.1016/S0003-2697(02)00610-3
    • A Mansson, S Tagerud: Multivariate statistics in analysis of data from the in vitro motility assay. Anal Biochem 314, 281-93 (2003) (Pubitemid 36315910)
    • (2003) Analytical Biochemistry , vol.314 , Issue.2 , pp. 281-293
    • Mansson, A.1    Tagerud, S.2
  • 62
    • 0030721473 scopus 로고    scopus 로고
    • Troponin i and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility
    • W Bing, ID Fraser, SB Marston: Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility. Biochem J 327, 335-40 (1997)
    • (1997) Biochem J , vol.327 , pp. 335-340
    • Bing, W.1    Fraser, I.D.2    Marston, S.B.3
  • 63
    • 0028894113 scopus 로고
    • Protein Adsorption-Kinetics Drastically Altered by Repositioning a Single Charge
    • JJ Ramsden, DJ Roush, DS Gill, R Kurrat, RC Willson: Protein Adsorption-Kinetics Drastically Altered by Repositioning a Single Charge. J Am Chem Soc 117, 8511-8516 (1995)
    • (1995) J Am Chem Soc , vol.117 , pp. 8511-8516
    • Ramsden, J.J.1    Roush, D.J.2    Gill, D.S.3    Kurrat, R.4    Willson, R.C.5
  • 64
    • 0000370657 scopus 로고
    • Electrostatic and Vanderwaals Contributions to Protein Adsorption -Computation of Equilibrium-Constants
    • CM Roth, AM Lenhoff: Electrostatic and Vanderwaals Contributions to Protein Adsorption -Computation of Equilibrium-Constants. Langmuir 9, 962-972 (1993)
    • (1993) Langmuir , vol.9 , pp. 962-972
    • Roth, C.M.1    Lenhoff, A.M.2
  • 65
    • 1642311378 scopus 로고    scopus 로고
    • Bacterial adhesion and transport in porous media: Role of the secondary energy minimum
    • DOI 10.1021/es034887l
    • JA Redman, SL Walker, M Elimelech: Bacterial adhesion and transport in porous media: Role of the secondary energy minimum. Environ Sci Technol 38, 1777-1785 (2004) (Pubitemid 38364926)
    • (2004) Environmental Science and Technology , vol.38 , Issue.6 , pp. 1777-1785
    • Redman, J.A.1    Walker, S.L.2    Elimelech, M.3
  • 67
    • 0019360754 scopus 로고
    • Isotonic contraction of skinned muscle fibers on a slow time base. Effects of ionic strength and calcium
    • DOI 10.1085/jgp.78.3.233
    • J Gulati, RJ Podolsky: Isotonic contraction of skinned muscle fibers on a slow time base: effects of ionic strength and calcium. J Gen Physiol 78, 233-57 (1981) (Pubitemid 11005180)
    • (1981) Journal of General Physiology , vol.78 , Issue.3 , pp. 233-257
    • Gulati, J.1    Podolsky, R.J.2
  • 68
    • 0006844340 scopus 로고    scopus 로고
    • Small segmental rearrangements in the myosin head can explain force generation in muscle
    • FGD Banos, J Bordas, J Lowy, A Svensson: Small Segmental Rearrangements in the Myosin Head Can Explain Force Generation in Muscle. Biophys J 71, 576-589 (1996) (Pubitemid 26289142)
    • (1996) Biophysical Journal , vol.71 , Issue.2 , pp. 576-589
    • Diaz Banos, F.G.1    Bordas, J.2    Lowy, J.3    Svensson, A.4
  • 69
    • 0025633388 scopus 로고
    • Electrostatic contributions to the binding of myosin and myosin-MgADP to F-Actin in solution
    • S Highsmith: Electrostatic Contributions to the Binding of Myosin and Myosin-MgADP to F-Actin in Solution. Biochemistry 29, 10690-10694 (1990)
    • (1990) Biochemistry , vol.29 , pp. 10690-10694
    • Highsmith, S.1
  • 70
    • 0033596962 scopus 로고    scopus 로고
    • The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
    • CT Murphy, JA Spudich: The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry 38, 3785-92 (1999)
    • (1999) Biochemistry , vol.38 , pp. 3785-3792
    • Murphy, C.T.1    Spudich, J.A.2
  • 72
    • 0013172998 scopus 로고    scopus 로고
    • Controlling antibody orientation on charged self-assembled monolayers
    • SF Chen, LY Liu, J Zhou, SY Jiang: Controlling antibody orientation on charged self-assembled monolayers. Langmuir 19, 2859-2864 (2003)
    • (2003) Langmuir , vol.19 , pp. 2859-2864
    • Chen, S.F.1    Liu, L.Y.2    Zhou, J.3    Jiang, S.Y.4
  • 73
    • 0037447211 scopus 로고    scopus 로고
    • Orientation of adsorbed antibodies on charged surfaces by computer simulation based on a united-residue model
    • J Zhou, SF Chen, SY Jiang: Orientation of adsorbed antibodies on charged surfaces by computer simulation based on a united-residue model. Langmuir 19, 3472-3478 (2003)
    • (2003) Langmuir , vol.19 , pp. 3472-3478
    • Zhou, J.1    Chen, S.F.2    Jiang, S.Y.3
  • 74
    • 1542345315 scopus 로고    scopus 로고
    • Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry
    • H Wang, DG Castner, BD Ratner, SY Jiang: Probing the orientation of surface-immobilized immunoglobulin G by time-of-flight secondary ion mass spectrometry. Langmuir 20, 1877-1887 (2004)
    • (2004) Langmuir , vol.20 , pp. 1877-1887
    • Wang, H.1    Castner, D.G.2    Ratner, B.D.3    Jiang, S.Y.4
  • 75
    • 0035874552 scopus 로고    scopus 로고
    • Effect of surface hydrophobicity on adsorption and relaxation kinetics of albumin and fibrinogen: Single-species and competitive behavior
    • DOI 10.1021/la0017781
    • CF Wertz, MM Santore: Effect of surface hydrophobicity on adsorption and relaxation kinetics of albumin and fibrinogen: Single-species and competitive behavior. Langmuir 17, 3006-3016 (2001) (Pubitemid 35330483)
    • (2001) Langmuir , vol.17 , Issue.10 , pp. 3006-3016
    • Wertz, C.F.1    Santore, M.M.2
  • 76
    • 0031674260 scopus 로고    scopus 로고
    • Human growth hormone adsorption kinetics and conformation on self-assembled monolayers
    • J Buijs, DW Britt, V Hlady: Human growth hormone adsorption kinetics and conformation on self-assembled monolayers. Langmuir 14, 335-341 (1998) (Pubitemid 128559798)
    • (1998) Langmuir , vol.14 , Issue.2 , pp. 335-341
    • Buijs, J.1    Britt, D.W.2    Hlady, V.3
  • 77
    • 33846402453 scopus 로고    scopus 로고
    • Spreading of proteins and its effect on adsorption and desorption kinetics
    • DOI 10.1016/j.colsurfb.2006.08.017, PII S0927776506002712
    • M van der Veen, MC Stuart, W Norde: Spreading of proteins and its effect on adsorption and desorption kinetics. Colloids and Surfaces B-Biointerfaces 54, 136-142 (2007) (Pubitemid 46136922)
    • (2007) Colloids and Surfaces B: Biointerfaces , vol.54 , Issue.2 , pp. 136-142
    • Van Der Veen, M.1    Stuart, M.C.2    Norde, W.3
  • 78
    • 0032905175 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics
    • AP Minton: Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics. Biophys J 76, 176-187 (1999) (Pubitemid 29202447)
    • (1999) Biophysical Journal , vol.76 , Issue.1 , pp. 176-187
    • Minton, A.P.1
  • 79
    • 0027429124 scopus 로고
    • Nonlinear kinetics of ferritin adsorption
    • H Nygren: Nonlinear Kinetics of Ferritin Adsorption. Biophys J 65, 1508-1512 (1993) (Pubitemid 23316970)
    • (1993) Biophysical Journal , vol.65 , Issue.4 , pp. 1508-1512
    • Nygren, H.1
  • 81
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • SS Margossian, S Lowey: Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol 85, 55-71 (1982)
    • (1982) Methods Enzymol , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 82
    • 0019000664 scopus 로고
    • Identification of a Region Susceptible to Proteolysis in Myosin Subfragment-2
    • RC Lu: Identification of a Region Susceptible to Proteolysis in Myosin Subfragment-2. Proc Natl Acad Sci U S A 77, 2010-2013 (1980)
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 2010-2013
    • Lu, R.C.1
  • 83
    • 0021981596 scopus 로고
    • The amino acid sequence and stability predictions of the hinge region in myosin subfragment 2
    • RC Lu, A Wong: The Amino-Acid Sequence and Stability Predictions of the Hinge Region in Myosin Subfragment-2. J Biol Chem 260, 3456-3461 (1985) (Pubitemid 15114342)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3456-3461
    • Lu, R.C.1    Wong, A.2
  • 84
    • 0023010840 scopus 로고
    • Electron microscope study of the effect of temperature on the length of the tail of the myosin molecule
    • DOI 10.1016/0022-2836(86)90283-4
    • M Walker, J Trinick: Electron microscope study of the effect of temperature on the length of the tail of the myosin molecule. J Mol Biol 192, 661-7 (1986) (Pubitemid 17208457)
    • (1986) Journal of Molecular Biology , vol.192 , Issue.3 , pp. 661-667
    • Walker, M.1    Trinick, J.2
  • 85
    • 12844288158 scopus 로고    scopus 로고
    • High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay
    • DOI 10.1016/j.jsb.2004.10.005, PII S1047847704002072
    • D Gundapaneni, J Xu, DD Root: High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay. J Struct Biol 149, 117-126 (2005) (Pubitemid 40170094)
    • (2005) Journal of Structural Biology , vol.149 , Issue.2 , pp. 117-126
    • Gundapaneni, D.1    Xu, J.2    Root, D.D.3
  • 87
    • 0035201291 scopus 로고    scopus 로고
    • Non-contact electrostatic surface force imaging of single protein filaments using intermodular force microscopy
    • T Aoki, Y Sowa, H Yokota, M Hiroshima, M Tokunaga, Y Ishii, T Yanagida: Non-contact electrostatic surface force imaging of single protein filaments using intermolecular force microscopy. Single Molecules 2, 183-190 (2001) (Pubitemid 33723526)
    • (2001) Single Molecules , vol.2 , Issue.3 , pp. 183-190
    • Aoki, T.1    Sowa, Y.2    Yokota, H.3    Hiroshima, M.4    Tokunaga, M.5    Ishii, Y.6    Yanagida, T.7
  • 88
    • 0020485885 scopus 로고
    • Flexibility of myosin rod determined from dilute-solution viscoelastic measurements
    • S Hvidt, FHM Nestler, ML Greaser, JD Ferry: Flexibility of Myosin Rod Determined from Dilute-Solution Viscoelastic Measurements. Biochemistry 21, 4064-4073 (1982)
    • (1982) Biochemistry , vol.21 , pp. 4064-4073
    • Hvidt, S.1    Nestler, F.2    Greaser, M.L.3    Ferry, J.D.4
  • 89
    • 0029913862 scopus 로고    scopus 로고
    • Dynamic behaviour of the head-tail junction of myosin
    • DOI 10.1006/jmbi.1996.0022
    • PJ Knight: Dynamic behaviour of the head-tail junction of myosin. J Mol Biol 255, 269-74. (1996) (Pubitemid 26104200)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.2 , pp. 269-274
    • Knight, P.J.1
  • 90
    • 0029870409 scopus 로고    scopus 로고
    • The structure of the head-tail junction of the myosin molecule
    • DOI 10.1006/jmbi.1996.0096
    • G Offer, P Knight: The structure of the head-tail junction of the myosin molecule. J Mol Biol 256, 407-416 (1996) (Pubitemid 26107193)
    • (1996) Journal of Molecular Biology , vol.256 , Issue.3 , pp. 407-416
    • Offer, G.1    Knight, P.2
  • 92
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition -A novel-approach for predicting invivo stability of a protein from its primary sequence
    • K Guruprasad, BVB Reddy, MW Pandit: Correlation between Stability of a Protein and Its Dipeptide Composition -a Novel-Approach for Predicting Invivo Stability of a Protein from Its Primary Sequence. Protein Eng 4, 155-161 (1990)
    • (1990) Protein Eng , vol.4 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.2    Pandit, M.W.3
  • 93
    • 0025321594 scopus 로고
    • Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin
    • JW Shriver, U Kamath: Differential Scanning Calorimetry of the Unfolding of Myosin Subfragment-1, Subfragment-2, and Heavy-Meromyosin. Biochemistry 29, 2556-2564 (1990) (Pubitemid 20100852)
    • (1990) Biochemistry , vol.29 , Issue.10 , pp. 2556-2564
    • Shriver, J.W.1    Kamath, U.2
  • 95
    • 0023118850 scopus 로고
    • Substructure of skeletal myosin subfragment 1 revealed by thermal denaturation
    • DOI 10.1021/bi00379a042
    • M Burke, S Zaager, J Bliss: Substructure of Skeletal Myosin Subfragment-1 Revealed by Thermal-Denaturation. Biochemistry 26, 1492-1496 (1987) (Pubitemid 17045879)
    • (1987) Biochemistry , vol.26 , Issue.5 , pp. 1492-1496
    • Burke, M.1    Zaager, S.2    Bliss, J.3
  • 96
    • 0023022759 scopus 로고
    • Substructure of Skeletal Myosin Subfragment-1 -Preferential Destabilization of a Domain by Methanol and Its Effect on Catalytic Activity
    • M Burke, M Sivaramakrishnan: Substructure of Skeletal Myosin Subfragment-1 -Preferential Destabilization of a Domain by Methanol and Its Effect on Catalytic Activity. J Biol Chem 261, 2330-2336 (1986)
    • (1986) J Biol Chem , vol.261 , pp. 2330-2336
    • Burke, M.1    Sivaramakrishnan, M.2
  • 97
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • DOI 10.1038/368567a0
    • TQP Uyeda, KM Ruppel, JA Spudich: Enzymatic-Activities Correlate with Chimeric Substitutions at the Actin-Binding Face of Myosin. Nature 368, 567-569 (1994) (Pubitemid 24118777)
    • (1994) Nature , vol.368 , Issue.6471 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 98
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin v
    • DOI 10.1021/bi035510v
    • CM Yengo, HL Sweeney: Functional role of loop 2 in myosin V. Biochemistry 43, 2605-2612 (2004) (Pubitemid 38327856)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 100
    • 0030983775 scopus 로고    scopus 로고
    • Control of actin moving trajectory by patterned poly(methylmethacrylate) tracks
    • H Suzuki, A Yamada, K Oiwa, H Nakayama, S Mashiko: Control of actin moving trajectory by patterned poly (methylmethacrylate) tracks. Biophys J 72, 1997-2001 (1997) (Pubitemid 27184428)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 1997-2001
    • Suzuki, H.1    Yamada, A.2    Oiwa, K.3    Nakayama, H.4    Mashiko, S.5
  • 101
    • 0032781726 scopus 로고    scopus 로고
    • Actin motion on microlithographically functionalized myosin surfaces and tracks
    • DV Nicolau, H Suzuki, S Mashiko, T Taguchi, S Yoshikawa: Actin motion on microlithographically functionalized myosin surfaces and tracks. Biophys J 77, 1126-1134 (1999) (Pubitemid 29362483)
    • (1999) Biophysical Journal , vol.77 , Issue.2 , pp. 1126-1134
    • Nicolau, D.V.1    Suzuki, H.2    Mashiko, S.3    Taguchi, T.4    Yoshikawa, S.5
  • 105
    • 22144494107 scopus 로고    scopus 로고
    • Continuous modelling and kinetic parameter estimation for cellulose nitration
    • DOI 10.1016/j.ces.2005.05.029, PII S0009250905004677
    • IVM Barbosa, DM Merquior, FC Peixoto: Continuous modelling and kinetic parameter estimation for cellulose nitration. Chem Eng Sci 60, 5406-5413 (2005) (Pubitemid 40980349)
    • (2005) Chemical Engineering Science , vol.60 , Issue.19 , pp. 5406-5413
    • Barbosa, I.V.M.1    Merquior, D.M.2    Peixoto, F.C.3
  • 106
    • 34250848839 scopus 로고    scopus 로고
    • Scanning probe microscopy study of myosin binding, topography and elastic properties of thin nitrocellulose films
    • A Mansson, J Klinth, E Johansson-Karlsson, C Widén, J Johnsson, L Montelius: Scanning probe microscopy study of myosin binding, topography and elastic properties of thin nitrocellulose films. Biophys J 80, 77a (2001)
    • (2001) Biophys J , vol.80
    • Mansson, A.1    Klinth, J.2    Johansson-Karlsson, E.3    Widén, C.4    Johnsson, J.5    Montelius, L.6
  • 107
    • 0032079394 scopus 로고    scopus 로고
    • Quick-freeze deep-etch electron microscopy of the actin-heavy meromyosin complex during the in vitro motility assay
    • DOI 10.1006/jmbi.1998.1715
    • E Katayama: Quick-freeze deep-etch electron microscopy of the actin-heavy meromyosin complex during the in vitro motility assay. J Mol Biol 278, 349-67 (1998) (Pubitemid 28220910)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.2 , pp. 349-367
    • Katayama, E.1
  • 108
    • 0028905551 scopus 로고
    • Atomic force microscopy of the myosin molecule
    • P Hallett, G Offer, MJ Miles: Atomic force microscopy of the myosin molecule. Biophys J 68, 1604-6 (1995)
    • (1995) Biophys J , vol.68 , pp. 1604-1606
    • Hallett, P.1    Offer, G.2    Miles, M.J.3
  • 109
    • 0141925656 scopus 로고    scopus 로고
    • Cryo-atomic force microscopy of unphosphorylated and thiophosphorylated single smooth muscle myosin molecules
    • DOI 10.1074/jbc.M306094200
    • S Sheng, Y Gao, AS Khromov, AV Somlyo, AP Somlyo, Z Shao: Cryo-atomic force microscopy of unphosphorylated and thiophosphorylated single smooth muscle myosin molecules. J Biol Chem 278, 39892-6 (2003) (Pubitemid 37248552)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39892-39896
    • Sheng, S.1    Gao, Y.2    Khromov, A.S.3    Somlyo, A.V.4    Somlyo, A.P.5    Shao, Z.6
  • 111
    • 18744380653 scopus 로고    scopus 로고
    • Guiding motor-propelled molecules with nanoscale precision through silanized bi-channel structures
    • DOI 10.1088/0957-4484/16/6/014, PII S0957448405925580
    • R Bunk, M Sundberg, IA Nicholls, P Omling, S Tågerud, A Månsson, L Montelius: Guiding motorpropelled molecules with nanoscale precision through silanized bi-channel structures. Nanotechnol 16, 710-717 (2005) (Pubitemid 40666571)
    • (2005) Nanotechnology , vol.16 , Issue.6 , pp. 710-717
    • Bunk, R.1    Sundberg, M.2    Mansson, A.3    Nicholls, I.A.4    Omling, P.5    Tgerud, S.6    Montelius, L.7
  • 112
    • 34250818691 scopus 로고    scopus 로고
    • Effects of surface adsorption on catalytic activity of heavy meromyosin studied using a fluorescent ATP analogue
    • DOI 10.1021/bi700211u
    • M Balaz, M Sundberg, M Persson, J Kvassman, A Mansson: Effects of Surface Adsorption on Catalytic Activity of Heavy Meromyosin Studied using Fluorescent ATP Analogue. Biochemistry 46, 7233-7251 (2007) (Pubitemid 46973997)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7233-7251
    • Balaz, M.1    Sundberg, M.2    Persson, M.3    Kvassman, J.4    Mansson, A.5
  • 113
    • 0345119075 scopus 로고    scopus 로고
    • Actomyosin-driven motility on patterned polyelectrolyte mono- and multilayers
    • DOI 10.1021/nl034539h
    • JA Jaber, PB Chase, JB Schlenoff: Actomyosindriven motility on patterned polyelectrolyte mono-and multilayers. Nano Letters 3, 1505-1509 (2003) (Pubitemid 37518161)
    • (2003) Nano Letters , vol.3 , Issue.11 , pp. 1505-1509
    • Jaber, J.A.1    Chase, P.B.2    Schlenoff, J.B.3
  • 114
    • 35448996399 scopus 로고    scopus 로고
    • Surface hydrophobicity modulates the operation of actomyosin-based dynamic nanodevices
    • DOI 10.1021/la700412m
    • DV Nicolau, G Solana, M Kekic, F Fulga, C Mahanivong, J Wright, C dos Remedios: Surface hydrophobicity modulates the operation of actomyosinbased dynamic nanodevices. Langmuir 23, 10846-10854 (2007) (Pubitemid 47623263)
    • (2007) Langmuir , vol.23 , Issue.21 , pp. 10846-10854
    • Nicolau, D.V.1    Solana, G.2    Kekic, M.3    Fulga, F.4    Mahanivong, C.5    Wright, J.6    Dos Remedios, C.G.7
  • 115
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • TQ Uyeda, SJ Kron, JA Spudich: Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J Mol Biol 214, 699-710 (1990)
    • (1990) J Mol Biol , vol.214 , pp. 699-710
    • Uyeda, T.Q.1    Kron, S.J.2    Spudich, J.A.3
  • 116
    • 0025076927 scopus 로고
    • The myosin step size: Measurement of the unit displacement per ATP hydrolyzed in an in vitro assay
    • YY Toyoshima, SJ Kron, JA Spudich: The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc Natl Acad Sci U S A 87, 7130-4 (1990)
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7130-7134
    • Toyoshima, Y.Y.1    Kron, S.J.2    Spudich, J.A.3
  • 118
    • 0344882519 scopus 로고
    • The hydrolysis of purine and pyrimidine nucleoside triphosphates by myosin
    • WW Kielley, HM Kalckar, LB Bradley: The hydrolysis of purine and pyrimidine nucleoside triphosphates by myosin. J Biol Chem 219, 95-101 (1956)
    • (1956) J Biol Chem , vol.219 , pp. 95-101
    • Kielley, W.W.1    Kalckar, H.M.2    Bradley, L.B.3
  • 120
    • 10944231111 scopus 로고    scopus 로고
    • The tail of myosin reduces actin filament velocity in the in vitro motility assay
    • DOI 10.1002/cm.20040
    • B Guo, WH Guilford: The tail of myosin reduces actin filament velocity in the in vitro motility assay. Cell Motil Cytoskeleton 59, 264-72 (2004) (Pubitemid 40012994)
    • (2004) Cell Motility and the Cytoskeleton , vol.59 , Issue.4 , pp. 264-272
    • Guo, B.1    Guilford, W.H.2
  • 121
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • DE Harris, DM Warshaw: Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J Biol Chem 268, 14764-8. (1993) (Pubitemid 23206617)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 122
    • 0029938646 scopus 로고    scopus 로고
    • Competitive protein adsorption studied with TIRF and ellipsometry
    • DOI 10.1006/jcis.1996.0239
    • B Lassen, M Malmsten: Competitive protein adsorption studied with TIRF and ellipsometry. J Colloid Interface Sci 179, 470-477 (1996) (Pubitemid 26188474)
    • (1996) Journal of Colloid and Interface Science , vol.179 , Issue.2 , pp. 470-477
    • Lassen, B.1    Malmsten, M.2
  • 123
    • 0037284103 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • DOI 10.1016/S0076-6879(03)61003-7
    • D Axelrod: Total internal reflection fluorescence microscopy in cell biology. Methods Enzymol 361, 1-33 (2003) (Pubitemid 36240992)
    • (2003) Methods in Enzymology , vol.361 , pp. 1-33
    • Axelrod, D.1
  • 124
    • 0022410284 scopus 로고
    • Electric birefringence study of rabbit skeletal myosin subfragments HMM, LMM, and rod in solution
    • R Cardinaud, JC Bernengo: Electric birefringence study of rabbit skeletal myosin subfragments HMM, LMM, and rod in solution. Biophys J 48, 751-63 (1985) (Pubitemid 16234572)
    • (1985) Biophysical Journal , vol.48 , Issue.5 , pp. 751-763
    • Cardinaud, R.1    Bernengo, J.C.2
  • 125
    • 0024399719 scopus 로고
    • Measurement of ATPase activity of immobilized myosin heads
    • H Hayashi, K Takiguchi, S Higashi-Fujime: Measurement of ATPase activity of immobilized myosin heads. J Biochem (Tokyo) 105, 875-7 (1989) (Pubitemid 19147412)
    • (1989) Journal of Biochemistry , vol.105 , Issue.6 , pp. 875-877
    • Hayashi, H.1    Takiguchi, K.2    Higashi-Fujime, S.3
  • 126
    • 0031931878 scopus 로고    scopus 로고
    • Reversible inactivation of myosin subfragment 1 activity by mechanical immobilization
    • S Highsmith, K Duignan, K Franks-Skiba, K Polosukhina, R Cooke: Reversible inactivation of myosin subfragment 1 activity by mechanical immobilization. Biophys J 74, 1465-72 (1998) (Pubitemid 28108554)
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1465-1472
    • Highsmith, S.1    Duignan, K.2    Franks-Skiba, K.3    Polosukhina, K.4    Cooke, R.5
  • 127
    • 0032704734 scopus 로고    scopus 로고
    • Commercial quartz crystal microbalances -theory and applications
    • CK O'Sullivan, GG Guilbault: Commercial quartz crystal microbalances -theory and applications. Biosensors & Bioelectronics 14, 663-670 (1999)
    • (1999) Biosensors & Bioelectronics , vol.14 , pp. 663-670
    • O'Sullivan, C.K.1    Guilbault, G.G.2
  • 128
    • 0034680544 scopus 로고    scopus 로고
    • Piezoelectric masssensing devices as biosensors -An alternative to optical biosensors?
    • A Janshoff, HJ Galla, C Steinem: Piezoelectric masssensing devices as biosensors -An alternative to optical biosensors? Angew Chemie-Int Ed 39, 4004-4032 (2000)
    • (2000) Angew Chemie-Int Ed , vol.39 , pp. 4004-4032
    • Janshoff, A.1    Galla, H.J.2    Steinem, C.3
  • 129
    • 34447498398 scopus 로고    scopus 로고
    • A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: Applications of acoustic physics to the analysis of biomolecular interactions
    • DOI 10.1002/jmr.826
    • MA Cooper, VT Singleton: A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions. J Mol Rec 20, 154-184 (2007) (Pubitemid 47075114)
    • (2007) Journal of Molecular Recognition , vol.20 , Issue.3 , pp. 154-184
    • Cooper, M.A.1    Singleton, V.T.2
  • 130
    • 84951279351 scopus 로고
    • Verwendung Von Schwingquarzen Zur Wagung Dunner Schichten Und Zur Mikrowagung
    • G Sauerbrey: Verwendung Von Schwingquarzen Zur Wagung Dunner Schichten Und Zur Mikrowagung. Zeitschrift Fur Physik 155, 206-222 (1959)
    • (1959) Zeitschrift fur Physik , vol.155 , pp. 206-222
    • Sauerbrey, G.1
  • 131
    • 0035894177 scopus 로고    scopus 로고
    • Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: A quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study
    • DOI 10.1021/ac0106501
    • F Hook, B Kasemo, T Nylander, C Fant, K Sott, H Elwing: Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: A quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study. Anal Chem 73, 5796-5804 (2001) (Pubitemid 34042194)
    • (2001) Analytical Chemistry , vol.73 , Issue.24 , pp. 5796-5804
    • Hook, F.1    Kasemo, B.2
  • 132
    • 0029933072 scopus 로고    scopus 로고
    • Effects of hydrophilization and immobilization on the interfacial behavior of immunoglobulins
    • DOI 10.1006/jcis.1996.0007
    • M Malmsten, B Lassen, K Holmberg, V Thomas, G Quash: Effects of hydrophilization and immobilization on the interfacial behavior of immunoglobulins. J Colloid Interface Sci 177, 70-78 (1996) (Pubitemid 26165135)
    • (1996) Journal of Colloid and Interface Science , vol.177 , Issue.1 , pp. 70-78
    • Malmsten, M.1    Lassen, B.2    Holmberg, K.3    Thomas, V.4    Quash, G.5
  • 133
    • 22444442001 scopus 로고    scopus 로고
    • Relationship between interfacial forces measured by colloid-probe atomic force microscopy and protein resistance of poly(ethylene glycol)-grafted poly(L-lysine) adlayers on niobia surfaces
    • DOI 10.1021/la050386x
    • S Pasche, M Textor, L Meagher, ND Spencer, HJ Griesser: Relationship between interfacial forces measured by colloid-probe atomic force microscopy and protein resistance of poly (ethylene glycol)-grafted poly (L-lysine) adlayers on niobia surfaces. Langmuir 21, 6508-6520 (2005) (Pubitemid 41006467)
    • (2005) Langmuir , vol.21 , Issue.14 , pp. 6508-6520
    • Pasche, S.1    Textor, M.2    Meagher, L.3    Spencer, N.D.4    Griesser, H.J.5
  • 134
    • 7544221688 scopus 로고    scopus 로고
    • A novel approach to produce protein nanopatterns by combining nanoimprint lithography and molecular self-assembly
    • D Falconnet, D Pasqui, S Park, R Eckert, H Schift, J Gobrecht, R Barbucci, M Textor: A novel approach to produce protein nanopatterns by combining nanoimprint lithography and molecular self-assembly. Nano Letters 4, 1909-1914 (2004)
    • (2004) Nano Letters , vol.4 , pp. 1909-1914
    • Falconnet, D.1    Pasqui, D.2    Park, S.3    Eckert, R.4    Schift, H.5    Gobrecht, J.6    Barbucci, R.7    Textor, M.8
  • 135
    • 0037109730 scopus 로고    scopus 로고
    • Photon-modulated wettability changes on spiropyran-coated surfaces
    • DOI 10.1021/la025963l
    • R Rosario, D Gust, M Hayes, F Jahnke, J Springer, AA Garcia: Photon-modulated wettability changes on spiropyrancoated surfaces. Langmuir 18, 8062-8069 (2002) (Pubitemid 35390097)
    • (2002) Langmuir , vol.18 , Issue.21 , pp. 8062-8069
    • Rosario, R.1    Gust, D.2    Hayes, M.3    Jahnke, F.4    Springer, J.5    Garcia, A.A.6
  • 136
    • 0032522286 scopus 로고    scopus 로고
    • Effect of surface wettability on the adsorption of proteins and detergents
    • DOI 10.1021/ja970819l
    • GB Sigal, M Mrksich, GM Whitesides: Effect of surface wettability on the adsorption of proteins and detergents. J Am Chem Soc 120, 3464-3473 (1998) (Pubitemid 28289085)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.14 , pp. 3464-3473
    • Sigal, G.B.1    Mrksich, M.2    Whitesides, G.M.3
  • 137
    • 0031818992 scopus 로고    scopus 로고
    • Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin
    • PB Conibear, MA Geeves: Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin. Biophys J 75, 926-37 (1998) (Pubitemid 28357533)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 926-937
    • Conibear, P.B.1    Geeves, M.A.2
  • 138
    • 1842339908 scopus 로고    scopus 로고
    • The biphasic force-velocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function
    • DOI 10.1111/j.1469-7793.1997.141bi.x
    • KA.P. Edman, A Mansson, C Caputo: The biphasic forcevelocity relationship in frog muscle fibres and its evaluation in terms of cross-bridge function (published erratum appears in J Physiol (Lond) 1997 Nov 1;504 (Pt 3):763). J Physiol (Lond) 503, 141-56 (1997) (Pubitemid 27390027)
    • (1997) Journal of Physiology , vol.503 , Issue.1 , pp. 141-156
    • Edman, K.A.P.1    Mansson, A.2    Caputo, C.3
  • 139
    • 0031018999 scopus 로고    scopus 로고
    • Rapid regeneration of power stroke in contracting muscle by attachment of second myosin head
    • DOI 10.1023/A:1018641218961
    • AF Huxley, S Tideswell: Rapid regeneration of power stroke in contracting muscle by attachment of second myosin head. J Muscle Res Cell Motil 18, 111-4 (1997) (Pubitemid 27073609)
    • (1997) Journal of Muscle Research and Cell Motility , vol.18 , Issue.1 , pp. 111-114
    • Huxley, A.F.1    Tideswell, S.2
  • 140
    • 0018566740 scopus 로고
    • Cross-linking of actin filaments by heavy meromyosin
    • DOI 10.1016/0022-2836(79)90407-8
    • JA Trinick, G Offer: Cross-linking of actin filaments by heavy meromyosin. J. Mol. Biol. 133, 549-556 (1979) (Pubitemid 10157906)
    • (1979) Journal of Molecular Biology , vol.133 , Issue.4 , pp. 549-556
    • Trinick, J.1    Offer, G.2
  • 141
    • 3142766062 scopus 로고    scopus 로고
    • A review of atomic force microscopy imaging systems: Application to molecular metrology and biological sciences
    • N Jalili, K Laxminarayana: A review of atomic force microscopy imaging systems: application to molecular metrology and biological sciences. Mechatronics 14, 907-945 (2004)
    • (2004) Mechatronics , vol.14 , pp. 907-945
    • Jalili, N.1    Laxminarayana, K.2
  • 142
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • P Hinterdorfer, YF Dufrene: Detection and localization of single molecular recognition events using atomic force microscopy. Nat Methods 3, 347-355 (2006)
    • (2006) Nat Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 144
    • 0342624757 scopus 로고    scopus 로고
    • Contact angle measurement and contact angle interpretation
    • DOI 10.1016/S0001-8686(98)00087-6
    • DY Kwok, AW Neumann: Contact angle measurement and contact angle interpretation. Adv Colloid Interface Sci 81, 167-249 (1999) (Pubitemid 32080114)
    • (1999) Advances in Colloid and Interface Science , vol.81 , Issue.3 , pp. 167-249
    • Kwok, D.Y.1    Neumann, A.W.2
  • 145
    • 34547165970 scopus 로고    scopus 로고
    • Contact angle measurements by confocal microscopy for non-destructive microscale surface characterization
    • DOI 10.1016/j.jcis.2007.04.067, PII S0021979707005450
    • M Sundberg, A Mansson, S Tagerud: Contact angle measurements by confocal microscopy for non-destructive microscale surface characterization. J Colloid Interface Sci 313, 454-60 (2007) (Pubitemid 47126475)
    • (2007) Journal of Colloid and Interface Science , vol.313 , Issue.2 , pp. 454-460
    • Sundberg, M.1    Mansson, A.2    Tagerud, S.3
  • 146
    • 0033964689 scopus 로고    scopus 로고
    • Surface modification using silanated poly(ethylene glycol)s
    • DOI 10.1016/S0142-9612(99)00224-0, PII S0142961299002240
    • S Jo, K Park: Surface modification using silanated poly (ethylene glycol)s. Biomaterials 21, 605-16. (2000) (Pubitemid 30083924)
    • (2000) Biomaterials , vol.21 , Issue.6 , pp. 605-616
    • Jo, S.1    Park, K.2
  • 147
    • 0242552594 scopus 로고    scopus 로고
    • Quantitative analysis of protein adsorption on a planar surface by Fourier transform infrared spectroscopy: Lysozyme adsorbed on hydrophobic silicon-containing polymer
    • DOI 10.1016/j.jcis.2003.07.011
    • Y Yokoyama, R Ishiguro, H Maeda, M Mukaiyama, K Kameyama, K Hiramatsu: Quantitative analysis of protein adsorption on a planar surface by Fourier transform infrared spectroscopy: lysozyme adsorbed on hydrophobic silicon-containing polymer. J Colloid Interface Sci 268, 23-32 (2003) (Pubitemid 37377978)
    • (2003) Journal of Colloid and Interface Science , vol.268 , Issue.1 , pp. 23-32
    • Yokoyama, Y.1    Ishiguro, R.2    Maeda, H.3    Mukaiyama, M.4    Kameyama, K.5    Hiramatsu, K.6
  • 148
    • 34248569227 scopus 로고    scopus 로고
    • Protein adsorption studied by neutron reflection
    • DOI 10.1016/j.cocis.2007.02.001, PII S1359029407000155
    • JR Lu, XB Zhao, M Yaseen: Protein adsorption studied by neutron reflection. Curr Opin Colloid Interface Sci 12, 9-16 (2007) (Pubitemid 46756383)
    • (2007) Current Opinion in Colloid and Interface Science , vol.12 , Issue.1 , pp. 9-16
    • Lu, J.R.1    Zhao, X.2    Yaseen, M.3
  • 149
    • 0032029432 scopus 로고    scopus 로고
    • Protein absorption and ellipsometry in biomaterial research
    • DOI 10.1016/S0142-9612(97)00112-9, PII S0142961297001129
    • H Elwing: Protein absorption and ellipsometry in biomaterial research. Biomaterials 19, 397-406 (1998) (Pubitemid 28246061)
    • (1998) Biomaterials , vol.19 , Issue.4-5 , pp. 397-406
    • Elwing, H.1
  • 150
    • 0031171122 scopus 로고    scopus 로고
    • Adsorption kinetics, conformation, and mobility of the growth hormone and lysozyme on solid surfaces, studied with TIRF
    • DOI 10.1006/jcis.1997.4876
    • J Buijs, V Hlady: Adsorption kinetics, conformation, and mobility of the growth hormone and lysozyme on solid surfaces, studied with TIRF. J Colloid Interface Sci 190, 171-181 (1997) (Pubitemid 27472896)
    • (1997) Journal of Colloid and Interface Science , vol.190 , Issue.1 , pp. 171-181
    • Buijs, J.1    Hlady, V.2
  • 151
    • 2542465914 scopus 로고    scopus 로고
    • SPR for molecular interaction analysis: A review of emerging application areas
    • DOI 10.1002/jmr.660
    • R Karlsson: SPR for molecular interaction analysis: a review of emerging application areas. J Mol Rec 17, 151-61 (2004) (Pubitemid 38688875)
    • (2004) Journal of Molecular Recognition , vol.17 , Issue.3 , pp. 151-161
    • Karlsson, R.1
  • 152
    • 33746742909 scopus 로고    scopus 로고
    • Looking towards label-free biomolecular interaction analysis in a high-throughput format: A review of new surface plasmon resonance technologies
    • DOI 10.1016/j.copbio.2006.06.012, PII S0958166906000966
    • C Boozer, G Kim, SX Cong, HW Guan, T Londergan: Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies. Curr Opin Biotechnol 17, 400-405 (2006) (Pubitemid 44163461)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 400-405
    • Boozer, C.1    Kim, G.2    Cong, S.3    Guan, H.4    Londergan, T.5
  • 153
    • 0036161285 scopus 로고    scopus 로고
    • A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation
    • DOI 10.1016/S0927-7765(01)00236-3, PII S0927776501002363
    • F Hook, J Voros, M Rodahl, R Kurrat, P Boni, JJ Ramsden, M Textor, ND Spencer, P Tengvall, J Gold, B Kasemo: A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation. Colloids and Surfaces BBiointerfaces 24, 155-170 (2002) (Pubitemid 34119110)
    • (2002) Colloids and Surfaces B: Biointerfaces , vol.24 , Issue.2 , pp. 155-170
    • Hook, F.F.1    Voros, J.2    Rodahl, M.3    Kurrat, R.4    Boni, P.5    Ramsden, J.J.6    Textor, M.7    Spencer, N.D.8    Tengvall, P.9    Gold, J.10    Kasemo, B.11
  • 154
    • 0034680544 scopus 로고    scopus 로고
    • Piezoelectric Mass-Sensing Devices as Biosensors-An Alternative to Optical Biosensors?
    • A Janshoff, HJ Galla, C Steinem: Piezoelectric Mass-Sensing Devices as Biosensors-An Alternative to Optical Biosensors? Angew Chem Int Ed Engl 39, 4004-4032 (2000)
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 4004-4032
    • Janshoff, A.1    Galla, H.J.2    Steinem, C.3
  • 155
    • 33645211745 scopus 로고    scopus 로고
    • Actomyosin motility detection using quartz crystal microbalance
    • KL Hanson, V Viidyanathan, DV Nicolau: Actomyosin motility detection using quartz crystal microbalance. Proc SPIE Vol. 6036, 1-8 (2006)
    • (2006) Proc SPIE , vol.6036 , pp. 1-8
    • Hanson, K.L.1    Viidyanathan, V.2    Nicolau, D.V.3
  • 156
    • 1242319429 scopus 로고    scopus 로고
    • Zeta potential of microfluidic substrates: 1. Theory, experimental techniques, and effects on separations
    • DOI 10.1002/elps.200305754
    • BJ Kirby, EF Hasselbrink: Zeta potential of microfluidic substrates: 1. Theory, experimental techniques, and effects on separations. Electrophoresis 25, 187-202 (2004) (Pubitemid 38219784)
    • (2004) Electrophoresis , vol.25 , Issue.2 , pp. 187-202
    • Kirby, B.J.1    Hasselbrink Jr., E.F.2
  • 157
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • T Yanagida, M Nakase, K Nishiyama, F Oosawa: Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307, 58-60 (1984) (Pubitemid 14132930)
    • (1984) Nature , vol.307 , Issue.5946 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 158
    • 0023260975 scopus 로고
    • Myosin subfragment-1 is sufficient to move actin filaments in vitro
    • DOI 10.1038/328536a0
    • YY Toyoshima, SJ Kron, EM McNally, KR Niebling, C Toyoshima, JA Spudich: Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature 328, 536-9 (1987) (Pubitemid 17098356)
    • (1987) Nature , vol.328 , Issue.6130 , pp. 536-539
    • Toyoshima, Y.Y.1    Kron, S.J.2    McNally, E.M.3
  • 159
    • 0023145911 scopus 로고
    • Sliding movement of single actin filaments on one-headed myosin filaments
    • DOI 10.1038/326805a0
    • Y Harada, A Noguchi, A Kishino, T Yanagida: Sliding Movement of Single Actin-Filaments on One-Headed Myosin-Filaments. Nature 326, 805-808 (1987) (Pubitemid 17057801)
    • (1987) Nature , vol.326 , Issue.6115 , pp. 805-808
    • Harada, Y.1    Noguchi, A.2    Kishino, A.3    Yanagida, T.4
  • 160
    • 0024423195 scopus 로고
    • Bidirectional movement of actin filaments along tracks of myosin heads
    • DOI 10.1038/341154a0
    • YY Toyoshima, C Toyoshima, JA Spudich: Bidirectional movement of actin filaments along tracks of myosin heads. Nature 341, 154-6 (1989) (Pubitemid 19222778)
    • (1989) Nature , vol.341 , Issue.6238 , pp. 154-156
    • Toyoshima, Y.Y.1    Toyoshima, C.2    Spudich, J.A.3
  • 161
    • 0025900542 scopus 로고
    • Quantized velocities at low myosin densities in an in vitro motility assay
    • TQ Uyeda, HM Warrick, SJ Kron, JA Spudich: Quantized velocities at low myosin densities in an in vitro motility assay. Nature 352, 307-11. (1991) (Pubitemid 21912342)
    • (1991) Nature , vol.352 , Issue.6333 , pp. 307-311
    • Uyeda, T.Q.P.1    Warrick, H.M.2    Kron, S.J.3    Spudich, J.A.4
  • 162
    • 0027390794 scopus 로고
    • Right-handed rotation of an actin filament in an in vitro motile system
    • DOI 10.1038/361269a0
    • T Nishizaka, T Yagi, Y Tanaka, S Ishiwata: Righthanded rotation of an actin filament in an in vitro motile system. Nature 361, 269-71 (1993) (Pubitemid 23034479)
    • (1993) Nature , vol.361 , Issue.6409 , pp. 269-271
    • Nishizaka, T.1    Yagi, T.2    Tanaka, Y.3    Ishiwata, S.4
  • 163
    • 0030068430 scopus 로고    scopus 로고
    • Preparation of bead-tailed actin filaments: Estimation of the torque produced by the sliding force in an in vitro motility assay
    • N Suzuki, H Miyata, S Ishiwata, K Kinosita, Jr.: Preparation of bead-tailed actin filaments: estimation of the torque produced by the sliding force in an in vitro motility assay. Biophys J 70, 401-8 (1996) (Pubitemid 26021478)
    • (1996) Biophysical Journal , vol.70 , Issue.1 , pp. 401-408
    • Suzuki, N.1    Miyata, H.2    Ishiwata, S.3    Kinosita Jr., K.4
  • 164
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • E Homsher, B Kim, A Bobkova, LS Tobacman: Calcium regulation of thin filament movement in an in vitro motility assay. Biophys J 70, 1881-92 (1996) (Pubitemid 26103961)
    • (1996) Biophysical Journal , vol.70 , Issue.4 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bobkova, A.3    Tobacman, L.S.4
  • 165
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • DOI 10.1038/ncb1060
    • C Veigel, JE Molloy, S Schmitz, J Kendrick-Jones: Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nature Cell Biology 5, 980-986 (2003) (Pubitemid 37406911)
    • (2003) Nature Cell Biology , vol.5 , Issue.11 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 166
    • 1142286682 scopus 로고    scopus 로고
    • Molecular engineering of a backwards-moving myosin motor
    • DOI 10.1038/nature02303
    • G Tsiavaliaris, S Fujita-Becker, DJ Manstein: Molecular engineering of a backwards-moving myosin motor. Nature 427, 558-561 (2004) (Pubitemid 38209115)
    • (2004) Nature , vol.427 , Issue.6974 , pp. 558-561
    • Tsiavaliaris, G.1    Fujita-Becker, S.2    Manstein, D.J.3
  • 167
    • 0030814752 scopus 로고    scopus 로고
    • Light chain-dependent myosin structural dynamics in solution investigated by transient electrical birefringence
    • D Eden, S Highsmith: Light chain-dependent myosin structural dynamics in solution investigated by transient electrical birefringence. Biophys J 73, 952-958 (1997) (Pubitemid 27337629)
    • (1997) Biophysical Journal , vol.73 , Issue.2 , pp. 952-958
    • Eden, D.1    Highsmith, S.2
  • 168
    • 0000720307 scopus 로고    scopus 로고
    • Luminescence of dye molecules on oxidized silicon and fluorescence interference contrast microscopy of biomembranes
    • A Lambacher, P Fromherz: Luminescence of dye molecules on oxidized silicon and fluorescence interference contrast microscopy of biomembranes. J Opt Soc Am BOpt Phys 19, 1435 (2002)
    • (2002) J Opt Soc Am BOpt Phys , vol.19 , pp. 1435
    • Lambacher, A.1    Fromherz, P.2
  • 169
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • R Koradi, M Billeter, K Wuthrich: MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14, 51-5, 29-32 (1996) (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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