메뉴 건너뛰기




Volumn 2014, Issue 1, 2014, Pages

Effect of 2H and 18O water isotopes in kinesin-1 gliding assay

Author keywords

Gliding motility assay; Heavy water; Kinesin 1; Microtubules

Indexed keywords

BUFFER; DEUTERIUM; KINESIN 1; OXYGEN 18; WATER;

EID: 84897932314     PISSN: None     EISSN: 21678359     Source Type: Journal    
DOI: 10.7717/peerj.284     Document Type: Article
Times cited : (2)

References (50)
  • 1
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • DOI10.1126/science.1092985
    • Asbury CL, Fehr AN, Block SM. 2003. Kinesin moves by an asymmetric hand-over-hand mechanism. Science 302:2130-2134 DOI 10.1126/science.1092985.
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 2
    • 2642536608 scopus 로고    scopus 로고
    • Assembly and transport of nanocrystal CdSe quantum dot nanocomposites using microtubules and kinesin motor proteins
    • DOI10.1021/nl049811h
    • Bachand GD, Rivera SB, Boal AK, Gaudioso J, Liu J, Bunker BC. 2004. Assembly and transport of nanocrystal CdSe quantum dot nanocomposites using microtubules and kinesin motor proteins. Nano Letters 4:817-821 DOI 10.1021/nl049811h.
    • (2004) Nano Letters , vol.4 , pp. 817-821
    • Bachand, G.D.1    Rivera, S.B.2    Boal, A.K.3    Gaudioso, J.4    Liu, J.5    Bunker, B.C.6
  • 3
    • 0000410244 scopus 로고
    • Enzyme kinetics and molecular evolution
    • DOI10.1021/cr00094a004
    • Benner SA. 1989. Enzyme kinetics and molecular evolution. Chemical Reviews 89:789-806 DOI 10.1021/cr00094a004.
    • (1989) Chemical Reviews , vol.89 , pp. 789-806
    • Benner, S.A.1
  • 4
    • 0028899953 scopus 로고
    • Failure of a single-headed kinesin to track parallel to microtubule protofilaments
    • DOI10.1038/373718a0
    • Berliner E, Young EC, Anderson K,Mahtani HK, Gelles J. 1995. Failure of a single-headed kinesin to track parallel to microtubule protofilaments. Nature 373:718-721 DOI 10.1038/373718a0.
    • (1995) Nature , vol.373 , pp. 718-721
    • Berliner, E.1    Young, E.C.2    Anderson, K.3    Mahtani, H.K.4    Gelles, J.5
  • 5
    • 0024295023 scopus 로고
    • Triosephosphate isomerase catalysis is diffusion controlled.
    • DOI10.1021/bi00404a013
    • Blacklow SC, Raines RT, LimWA, Zamore PD, Knowles JR. 1988. Triosephosphate isomerase catalysis is diffusion controlled. Biochemistry 27:1158-1165 DOI 10.1021/bi00404a013.
    • (1988) Biochemistry , vol.27 , pp. 1158-1165
    • Blacklow, S.C.1    Raines, R.T.2    Lim, W.A.3    Zamore, P.D.4    Knowles, J.R.5
  • 6
    • 0342445427 scopus 로고    scopus 로고
    • Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity
    • DOI10.1016/S0014-5793(99)01757-3
    • Böohm KJ, Stracke R, Baum M, Zieren M, Unger E. 2000. Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity. FEBS Letters 466:59-62 DOI 10.1016/S0014-5793(99)01757-3.
    • (2000) FEBS Letters , vol.466 , pp. 59-62
    • Böohm, K.J.1    Stracke, R.2    Baum, M.3    Zieren, M.4    Unger, E.5
  • 7
    • 0033747736 scopus 로고    scopus 로고
    • Speeding up kinesin-driven microtubule gliding in vitro by variation of cofactor composition and physicochemical parameters
    • DOI10.1006/CBIR.1999.0515
    • Böohm KJ, Stracke R, Unger E. 2000. Speeding up kinesin-driven microtubule gliding in vitro by variation of cofactor composition and physicochemical parameters. Cell Biology International 24:335-341 DOI 10.1006/cbir.1999.0515.
    • (2000) Cell Biology International , vol.24 , pp. 335-341
    • Böohm, K.J.1    Stracke, R.2    Unger, E.3
  • 8
    • 28444431792 scopus 로고    scopus 로고
    • Inhibition of Kinesin-driven microtubule motility by polyhydroxy compounds
    • In: Hein H-J, Bischoff G, eds. Micro- and nanostructures of biological systems. Aachen: Shaker Verlag GmbH, Germany
    • Böohm KJ, Stracke R, Vater W, Unger E. 2004. Inhibition of Kinesin-driven microtubule motility by polyhydroxy compounds. In: Hein H-J, Bischoff G, eds. Micro- and nanostructures of biological systems. Aachen: Shaker Verlag GmbH, Germany, 153-165. Available at http://lccn.loc.gov/2007440241.
    • (2004) , pp. 153-165
    • Böohm, K.J.1    Stracke, R.2    Vater, W.3    Unger, E.4
  • 9
    • 74249100399 scopus 로고    scopus 로고
    • Heterogeneous and homogeneous nucleation of Taxol crystals in aqueous solutions and gels: effect of tubulin proteins.
    • DOI10.1016/j.colsurfb.2009.10.033
    • Castro JS, Deymier PA, Trzaskowski B, Bucay J. 2010. Heterogeneous and homogeneous nucleation of Taxol crystals in aqueous solutions and gels: effect of tubulin proteins. Colloids and Surfaces B: Biointerfaces 76:199-206 DOI 10.1016/j.colsurfb.2009.10.033.
    • (2010) Colloids and Surfaces B: Biointerfaces , vol.76 , pp. 199-206
    • Castro, J.S.1    Deymier, P.A.2    Trzaskowski, B.3    Bucay, J.4
  • 11
    • 0035519629 scopus 로고    scopus 로고
    • Effect of deuterium oxide on actomyosin motility in vitro
    • DOI10.1016/S0005-2728(01)00216-X
    • Chaen S, Yamamoto N, Shirakawa I, Sugi H. 2001. Effect of deuterium oxide on actomyosin motility in vitro. Biochimica et Biophysica Acta 1506:218-223 DOI 10.1016/S0005-2728(01)00216-X.
    • (2001) Biochimica et Biophysica Acta , vol.1506 , pp. 218-223
    • Chaen, S.1    Yamamoto, N.2    Shirakawa, I.3    Sugi, H.4
  • 14
    • 0030320909 scopus 로고    scopus 로고
    • Liquid water and biological systems: the most important problem in science that hardly anyone wants to see solved
    • DOI10.1039/fd9960300019
    • Cho C, Singh S, Robinson GW. 1996. Liquid water and biological systems: the most important problem in science that hardly anyone wants to see solved. Faraday Discussions 103:19-27 DOI 10.1039/fd9960300019.
    • (1996) Faraday Discussions , vol.103 , pp. 19-27
    • Cho, C.1    Singh, S.2    Robinson, G.W.3
  • 15
    • 0001591464 scopus 로고
    • Use of the glass electrode in deuterium oxide and the relation between the standardized pD (paD) scale and the operational pH in heavy water.
    • DOI10.1021/ac60260a013
    • Covington AK, Paabo M, Robinson RA, Bates RG. 1968. Use of the glass electrode in deuterium oxide and the relation between the standardized pD (paD) scale and the operational pH in heavy water. Analytical Chemistry 40:700-706 DOI 10.1021/ac60260a013.
    • (1968) Analytical Chemistry , vol.40 , pp. 700-706
    • Covington, A.K.1    Paabo, M.2    Robinson, R.A.3    Bates, R.G.4
  • 17
    • 44949247428 scopus 로고    scopus 로고
    • Taxol crystals can masquerade as stabilized microtubules
    • DOI10.1371/journal.pone.0001476
    • Foss M,Wilcox BWL, Alsop GB, Zhang D. 2008. Taxol crystals can masquerade as stabilized microtubules. PLoS ONE 3:e1476 DOI 10.1371/journal.pone.0001476.
    • (2008) PLoS ONE , vol.3
    • Foss, M.1    Wilcox, B.W.L.2    Alsop, G.B.3    Zhang, D.4
  • 18
    • 77952093034 scopus 로고    scopus 로고
    • Kinesin velocity increases with the number of motors pulling against viscoelastic drag
    • DOI10.1007/s00249-009-0560-8
    • Gagliano J,Walb M, Blaker B,Macosko JC, Holzwarth G. 2010. Kinesin velocity increases with the number of motors pulling against viscoelastic drag. European Biophysics Journal 39:801-813 DOI 10.1007/s00249-009-0560-8.
    • (2010) European Biophysics Journal , vol.39 , pp. 801-813
    • Gagliano, J.1    Walb, M.2    Blaker, B.3    Macosko, J.C.4    Holzwarth, G.5
  • 19
    • 69949092035 scopus 로고    scopus 로고
    • Direct observation of the binding state of the kinesin head to the microtubule
    • DOI10.1038/nature08259
    • Guydosh NR, Block SM. 2009. Direct observation of the binding state of the kinesin head to the microtubule. Nature 461:125-128 DOI 10.1038/nature08259.
    • (2009) Nature , vol.461 , pp. 125-128
    • Guydosh, N.R.1    Block, S.M.2
  • 20
    • 0018817999 scopus 로고
    • Oxygen-18 probes of enzymic reactions of phosphate compounds.
    • DOI10.1016/S0076.-68798064005-1
    • Hackney DD, Stempel KE, Boyer PD. 1980. Oxygen-18 probes of enzymic reactions of phosphate compounds. Methods in Enzymology 64:60-83 DOI 10.1016/S0076.-68798064005-1.
    • (1980) Methods in Enzymology , vol.64 , pp. 60-83
    • Hackney, D.D.1    Stempel, K.E.2    Boyer, P.D.3
  • 21
    • 0000273430 scopus 로고
    • Viscosity of deuterium oxide and water from 5{ring operator}to 125 {ring operator}C.
    • DOI10.1063/1.1747310
    • Hardy RC, Cottington RL. 1949. Viscosity of deuterium oxide and water from 5{ring operator}to 125 {ring operator}C. The Journal of Chemical Physics 17:509-510 DOI 10.1063/1.1747310.
    • (1949) The Journal of Chemical Physics , vol.17 , pp. 509-510
    • Hardy, R.C.1    Cottington, R.L.2
  • 22
    • 18144390571 scopus 로고    scopus 로고
    • Molecular self-assembly of nanowires and "nanospools" using active transport.
    • DOI10.1021/nl0478427
    • Hess H, Clemmens J, Brunner C, Doot R, Luna S, Ernst K-H, Vogel V. 2005. Molecular self-assembly of nanowires and "nanospools" using active transport. Nano Letters 5:629-633 DOI 10.1021/nl0478427.
    • (2005) Nano Letters , vol.5 , pp. 629-633
    • Hess, H.1    Clemmens, J.2    Brunner, C.3    Doot, R.4    Luna, S.5    Ernst, K.-H.6    Vogel, V.7
  • 23
    • 0017382537 scopus 로고
    • The effects of temperature and salts on myosin subfragment-1 and F-actin association
    • DOI10.1016/0003-9861(77)90054-6
    • Highsmith S. 1977. The effects of temperature and salts on myosin subfragment-1 and F-actin association. Archives of Biochemistry and Biophysics 180:404-408 DOI 10.1016/0003-9861(77)90054-6.
    • (1977) Archives of Biochemistry and Biophysics , vol.180 , pp. 404-408
    • Highsmith, S.1
  • 24
    • 0030013038 scopus 로고    scopus 로고
    • Osmotic pressure probe of actin-myosin hydration changes during ATP hydrolysis
    • DOI10.1016/S0006-3495(96)79852-1
    • Highsmith S, Duignan K, Cooke R, Cohen J. 1996. Osmotic pressure probe of actin-myosin hydration changes during ATP hydrolysis. Biophysical Journal 70:2830-2837 DOI 10.1016/S0006-3495(96)79852-1.
    • (1996) Biophysical Journal , vol.70 , pp. 2830-2837
    • Highsmith, S.1    Duignan, K.2    Cooke, R.3    Cohen, J.4
  • 26
    • 0016169139 scopus 로고
    • Solvent isotope effects on microtubule and depolymerization polymerization
    • DOI10.1016/0022-2836(74)90566-X
    • Houston LL, Odell J, Lee YC, Himes RH. 1974. Solvent isotope effects on microtubule and depolymerization polymerization. Journal of Molecular Biology 87:141-146 DOI 10.1016/0022-2836(74)90566-X.
    • (1974) Journal of Molecular Biology , vol.87 , pp. 141-146
    • Houston, L.L.1    Odell, J.2    Lee, Y.C.3    Himes, R.H.4
  • 27
    • 0016678747 scopus 로고
    • Effects of deuterium oxide on elementary steps in the ATPase reactions evidence for the similarity of key intermediates in contractile and transport ATPase
    • Inoue A, Fukushima Y, Tonomura Y. 1975. Effects of deuterium oxide on elementary steps in the ATPase reactions evidence for the similarity of key intermediates in contractile and transport ATPase. The Journal of Biochemistry 78:1113-1121.
    • (1975) The Journal of Biochemistry , vol.78 , pp. 1113-1121
    • Inoue, A.1    Fukushima, Y.2    Tonomura, Y.3
  • 28
    • 0030052290 scopus 로고    scopus 로고
    • Role of hydration and water structure in biological and colloidal interactions
    • DOI10.1038/379219a0
    • Israelachvili J,Wennerström H. 1996. Role of hydration and water structure in biological and colloidal interactions. Nature 379:219-225 DOI 10.1038/379219a0.
    • (1996) Nature , vol.379 , pp. 219-225
    • Israelachvili, J.1    Wennerström, H.2
  • 29
    • 84876459245 scopus 로고    scopus 로고
    • Electrical control of kinesin-microtubule motility using a transparent functionalizedgraphene substrate
    • DOI10.1088/0957-4484/24/19/195102
    • Kim E, Byun K-E, Choi DS, Lee DJ, Cho DH, Lee BY, Yang H, Heo J, Chung H-J, Seo S, Hong S. 2013. Electrical control of kinesin-microtubule motility using a transparent functionalizedgraphene substrate. Nanotechnology 24:195102 DOI 10.1088/0957-4484/24/19/195102.
    • (2013) Nanotechnology , vol.24 , pp. 195102
    • Kim, E.1    Byun, K.-E.2    Choi, D.S.3    Lee, D.J.4    Cho, D.H.5    Lee, B.Y.6    Yang, H.7    Heo, J.8    Chung, H.-J.9    Seo, S.10    Hong, S.11
  • 31
    • 0032772532 scopus 로고    scopus 로고
    • Pharmacological uses and perspectives of heavy water and deuterated compounds.
    • DOI10.1139/y99-005
    • Kushner DJ, Baker A, Dunstall TG. 1999. Pharmacological uses and perspectives of heavy water and deuterated compounds. Canadian Journal of Physiology and Pharmacology 77:79-88 DOI 10.1139/y99-005.
    • (1999) Canadian Journal of Physiology and Pharmacology , vol.77 , pp. 79-88
    • Kushner, D.J.1    Baker, A.2    Dunstall, T.G.3
  • 32
    • 0346137004 scopus 로고
    • The biochemistry of water containing hydrogen isotope
    • DOI10.1021/ja01335a509
    • Lewis GN. 1933. The biochemistry of water containing hydrogen isotope. Journal of the American Chemical Society 55:3503-3504 DOI 10.1021/ja01335a509.
    • (1933) Journal of the American Chemical Society , vol.55 , pp. 3503-3504
    • Lewis, G.N.1
  • 33
    • 0000945479 scopus 로고
    • The biology of heavy water
    • DOI10.1126/science.79.2042.151
    • Lewis GN. 1934. The biology of heavy water. Science 79:151-153 DOI 10.1126/science.79.2042.151.
    • (1934) Science , vol.79 , pp. 151-153
    • Lewis, G.N.1
  • 34
    • 79958070430 scopus 로고    scopus 로고
    • Effects of surface passivation on gliding motility assays.
    • DOI10.1371/journal.pone.0019522
    • Maloney A, Herskowitz LJ, Koch SJ. 2011. Effects of surface passivation on gliding motility assays. PLoS ONE 6:e19522 DOI 10.1371/journal.pone.0019522.
    • (2011) PLoS ONE , vol.6
    • Maloney, A.1    Herskowitz, L.J.2    Koch, S.J.3
  • 35
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • DOI10.1074/jbc.272.2.724
    • Ma Y-Z, Taylor EW. 1997. Interacting head mechanism of microtubule-kinesin ATPase. The Journal of Biological Chemistry 272:724-730 DOI 10.1074/jbc.272.2.724.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 724-730
    • Ma, Y.-Z.1    Taylor, E.W.2
  • 37
    • 0032548491 scopus 로고    scopus 로고
    • Pathway of ATP hydrolysis by monomeric and dimeric kinesin.
    • DOI10.1021/bi9711184
    • Moyer ML, Gilbert SP, Johnson KA. 1998. Pathway of ATP hydrolysis by monomeric and dimeric kinesin. Biochemistry 37:800-813 DOI 10.1021/bi9711184.
    • (1998) Biochemistry , vol.37 , pp. 800-813
    • Moyer, M.L.1    Gilbert, S.P.2    Johnson, K.A.3
  • 38
    • 61449240125 scopus 로고    scopus 로고
    • The processivity of kinesin-2 motors suggests diminished front-head gating
    • DOI10.1016/j.cub.2009.01.058
    • Muthukrishnan G, Zhang Y, Shastry S, HancockWO. 2009. The processivity of kinesin-2 motors suggests diminished front-head gating. Current Biology 19:442-447 DOI 10.1016/j.cub.2009.01.058.
    • (2009) Current Biology , vol.19 , pp. 442-447
    • Muthukrishnan, G.1    Zhang, Y.2    Shastry, S.3    Hancock, W.O.4
  • 39
    • 0037085126 scopus 로고    scopus 로고
    • Imaging microscopic viscosity with confocal scanning optical tweezers.
    • DOI10.1364/OL.27.000264
    • Nemet BA, Shabtai Y, Cronin-Golomb M. 2002. Imaging microscopic viscosity with confocal scanning optical tweezers. Optics Letters 27:264-266 DOI 10.1364/OL.27.000264.
    • (2002) Optics Letters , vol.27 , pp. 264-266
    • Nemet, B.A.1    Shabtai, Y.2    Cronin-Golomb, M.3
  • 40
    • 0016813649 scopus 로고
    • Ionic and nucleotide requirements for microtubule polymerization in vitro?
    • DOI10.1021/bi00684a032
    • Olmstedt JB, Borisy GG. 1975. Ionic and nucleotide requirements for microtubule polymerization in vitro? Biochemistry 14:2996-3005 DOI 10.1021/bi00684a032.
    • (1975) Biochemistry , vol.14 , pp. 2996-3005
    • Olmstedt, J.B.1    Borisy, G.G.2
  • 41
    • 0034595187 scopus 로고    scopus 로고
    • Suppression of microtubule dynamic instability and treadmilling by deuterium oxide.
    • DOI10.1021/bi992217f
    • Panda D, Chakrabarti G, Hudson J, Pigg K,Miller HP,Wilson L, Himes RH. 2000. Suppression of microtubule dynamic instability and treadmilling by deuterium oxide. Biochemistry 39:5075-5081 DOI 10.1021/bi992217f.
    • (2000) Biochemistry , vol.39 , pp. 5075-5081
    • Panda, D.1    Chakrabarti, G.2    Hudson, J.3    Pigg, K.4    Miller, H.P.5    Wilson, L.6    Himes, R.H.7
  • 43
    • 0029130871 scopus 로고
    • Macromolecules and water: probing with osmotic stress
    • DOI10.1016/0076.-68799559039-0
    • Parsegian VA, Rand RP, Rau DC. 1995. Macromolecules and water: probing with osmotic stress. Methods in Enzymology 259:43-94 DOI 10.1016/0076.-68799559039-0.
    • (1995) Methods in Enzymology , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 45
    • 70449413761 scopus 로고    scopus 로고
    • Role of heavy water in biological sciences with an emphasis on thermostabilization of vaccines
    • DOI10.1586/erv.09.105
    • Sen A, Balamurugan V, Rajak KK, Chakravarti S, Bhanuprakash V, Singh RK. 2009. Role of heavy water in biological sciences with an emphasis on thermostabilization of vaccines. Expert Review of Vaccines 8:1587-1602 DOI 10.1586/erv.09.105.
    • (2009) Expert Review of Vaccines , vol.8 , pp. 1587-1602
    • Sen, A.1    Balamurugan, V.2    Rajak, K.K.3    Chakravarti, S.4    Bhanuprakash, V.5    Singh, R.K.6
  • 47
    • 0035919819 scopus 로고    scopus 로고
    • Linkage of EcoRI dissociation from its specific DNA recognition site to water activity, salt concentration, and pH: separating their roles in specific and non-specific binding
    • DOI10.1006/jmbi.2001.4781
    • Sidorova NY, Rau DC. 2001. Linkage of EcoRI dissociation from its specific DNA recognition site to water activity, salt concentration, and pH: separating their roles in specific and non-specific binding. Journal of Molecular Biology 310:801-816 DOI 10.1006/jmbi.2001.4781.
    • (2001) Journal of Molecular Biology , vol.310 , pp. 801-816
    • Sidorova, N.Y.1    Rau, D.C.2
  • 49
    • 0036655405 scopus 로고    scopus 로고
    • Heavy-water-based solutions of rhodamine dyes: photophysical properties and laser operation
    • DOI10.1007/s00340-002-0932-6
    • Sinha S, Ray AK, Kundu S, Sasikumar S, Dasgupta K. 2002. Heavy-water-based solutions of rhodamine dyes: photophysical properties and laser operation. Applied Physics B 75:85-90 DOI 10.1007/s00340-002-0932-6.
    • (2002) Applied Physics B , vol.75 , pp. 85-90
    • Sinha, S.1    Ray, A.K.2    Kundu, S.3    Sasikumar, S.4    Dasgupta, K.5
  • 50
    • 0027497918 scopus 로고
    • Naturally occurring deuterium is essential for the normal growth rate of cells
    • DOI10.1016/0014-5793(93)81479-J
    • Somlyai G, Jancsó G, Jákli G, Vass K, Barna B, Lakics V, Gaál T. 1993. Naturally occurring deuterium is essential for the normal growth rate of cells. FEBS Letters 317:1-4 DOI 10.1016/0014-5793(93)81479-J.
    • (1993) FEBS Letters , vol.317 , pp. 1-4
    • Somlyai, G.1    Jancsó, G.2    Jákli, G.3    Vass, K.4    Barna, B.5    Lakics, V.6    Gaál, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.