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Volumn 105, Issue 41, 2008, Pages 15743-15748

Probing the origin of tubulin rigidity with molecular simulations

Author keywords

Coarse grained simulations; Dynamic instability; Forced unfolding; Single molecule; Unfolding pathways

Indexed keywords

BETA TUBULIN; HETERODIMER; MONOMER; TUBULIN;

EID: 57349100824     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0806113105     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • Howard J, Hyman A (2003) Dynamics and mechanics of the microtubule plus end. Nature 422:753-758.
    • (2003) Nature , vol.422 , pp. 753-758
    • Howard, J.1    Hyman, A.2
  • 2
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan MA, Wilson L (2004) Microtubules as a target for anticancer drugs. Nat Rev Cancer 4:253-265.
    • (2004) Nat Rev Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 3
    • 33745918018 scopus 로고    scopus 로고
    • Insights into the mechanism of microtubule stabilization by taxol
    • Xiao H, et al. (2006) Insights into the mechanism of microtubule stabilization by taxol. Proc Natl Acad Sci USA 103:10166-10173.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10166-10173
    • Xiao, H.1
  • 4
    • 33644853818 scopus 로고    scopus 로고
    • Structural intermediates in microtubule assembly and disassembly: How and why?
    • Nogales E, Wang H (2006) Structural intermediates in microtubule assembly and disassembly: How and why? Curr Opin Cell Biol 18:179-184.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 179-184
    • Nogales, E.1    Wang, H.2
  • 5
    • 33745893239 scopus 로고    scopus 로고
    • Thermal fluctuations of grafted microtubules provide evidence of a length-dependent persistence length
    • Pampaloni F, et al. (2006) Thermal fluctuations of grafted microtubules provide evidence of a length-dependent persistence length. Proc Natl Acad Sci USA 103:10248-10253.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10248-10253
    • Pampaloni, F.1
  • 8
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker RA, et al. (1988) Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies. J Cell Biol 107:1437-1448.
    • (1988) J Cell Biol , vol.107 , pp. 1437-1448
    • Walker, R.A.1
  • 9
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analog of GTP, guanylyl (α,β) methylenediphosphonate
    • Muller-Reichert T, Chretien D, Severin F, Hyman AA (1998) Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analog of GTP, guanylyl (α,β) methylenediphosphonate. Proc Natl Acad Sci USA 95:3661-3666.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3661-3666
    • Muller-Reichert, T.1    Chretien, D.2    Severin, F.3    Hyman, A.A.4
  • 11
    • 33846669353 scopus 로고    scopus 로고
    • Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation
    • Kortazar D, et al. (2007) Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation. Exp Cell Res 313:425-436.
    • (2007) Exp Cell Res , vol.313 , pp. 425-436
    • Kortazar, D.1
  • 12
    • 12344320203 scopus 로고    scopus 로고
    • Microtubules plus-end-tracking proteins: Mechanisms and functions
    • Akhmanova A, Hoogenraad CC (2005) Microtubules plus-end-tracking proteins: Mechanisms and functions. Curr Opin Cell Biol 17:47-54.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 47-54
    • Akhmanova, A.1    Hoogenraad, C.C.2
  • 13
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak A, Vale RD (2008) Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451:363-368.
    • (2008) Nature , vol.451 , pp. 363-368
    • Roll-Mecak, A.1    Vale, R.D.2
  • 14
    • 33646494080 scopus 로고    scopus 로고
    • Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives
    • Nogales E, Wang H (2006) Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives. Curr Opin Struct Biol 16:221-229.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 221-229
    • Nogales, E.1    Wang, H.2
  • 15
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations- The Brownian ratchet
    • Peskin C, ODell G, Oster G (1993) Cellular motions and thermal fluctuations- The Brownian ratchet. Biophys J 65:316-324.
    • (1993) Biophys J , vol.65 , pp. 316-324
    • Peskin, C.1    ODell, G.2    Oster, G.3
  • 17
    • 0036591961 scopus 로고    scopus 로고
    • Tensile stress stimulates microtubule outgrowth in living cells
    • Kaverina I, et al. (2002) Tensile stress stimulates microtubule outgrowth in living cells. J Cell Sci 115:2283-2291.
    • (2002) J Cell Sci , vol.115 , pp. 2283-2291
    • Kaverina, I.1
  • 18
    • 0347362783 scopus 로고    scopus 로고
    • Regulation of tension-induced mechanotranscriptional signals by the microtubule network in fibroblasts
    • D'Addario M, Arora P, Ellen R, McCulloch C (2003) Regulation of tension-induced mechanotranscriptional signals by the microtubule network in fibroblasts. J Biol Chem 278:53090-53097.
    • (2003) J Biol Chem , vol.278 , pp. 53090-53097
    • D'Addario, M.1    Arora, P.2    Ellen, R.3    McCulloch, C.4
  • 19
    • 27744548870 scopus 로고    scopus 로고
    • Mechanochemical model of microtubule structure and self-assembly kinetics
    • VanBuren V, Cassimeris L, Odde D (2005) Mechanochemical model of microtubule structure and self-assembly kinetics. Biophys J 89:2911-2926.
    • (2005) Biophys J , vol.89 , pp. 2911-2926
    • VanBuren, V.1    Cassimeris, L.2    Odde, D.3
  • 20
    • 33746784797 scopus 로고    scopus 로고
    • Elastic response, buckling, and instability of microtubules under radial indentation
    • Schaap IAT, Carrasco C, de Pablo PJ, MacKintosh FC, Schmidt CF (2006) Elastic response, buckling, and instability of microtubules under radial indentation. Biophys J 91:1521-1531.
    • (2006) Biophys J , vol.91 , pp. 1521-1531
    • Schaap, I.A.T.1    Carrasco, C.2    de Pablo, P.J.3    MacKintosh, F.C.4    Schmidt, C.F.5
  • 21
    • 35248883959 scopus 로고    scopus 로고
    • Antal T, Krapivsky PL, Redner S, Mailman M, Chakraborty B (2007) Dynamics of an idealized model of microtubule growth and catastrophe. Phys Rev E 76:0419071-04190712.
    • Antal T, Krapivsky PL, Redner S, Mailman M, Chakraborty B (2007) Dynamics of an idealized model of microtubule growth and catastrophe. Phys Rev E 76:0419071-04190712.
  • 22
    • 10244229625 scopus 로고    scopus 로고
    • Deformation and collapse of microtubules on the nanometer scale
    • 91:098101.1-4
    • de Pablo P, Schaap I, MacKintosh F, Schmidt C (2003) Deformation and collapse of microtubules on the nanometer scale. Phys Rev Lett 91:098101.1-4.
    • (2003) Phys Rev Lett
    • de Pablo, P.1    Schaap, I.2    MacKintosh, F.3    Schmidt, C.4
  • 23
    • 0037049681 scopus 로고    scopus 로고
    • Nanomechanics of microtubules, 89:248101.1-4
    • Kis A, et al. (2002) Nanomechanics of microtubules. Phys Rev Lett 89:248101.1-4.
    • (2002) Phys Rev Lett
    • Kis, A.1
  • 24
  • 25
    • 0141634366 scopus 로고    scopus 로고
    • The physical basis of microtubule structure and stability
    • Sept D, Baker NA, McCammon JA (2003) The physical basis of microtubule structure and stability. Prot Sci 12:2257-2261.
    • (2003) Prot Sci , vol.12 , pp. 2257-2261
    • Sept, D.1    Baker, N.A.2    McCammon, J.A.3
  • 26
    • 33846411078 scopus 로고    scopus 로고
    • Microtubule stability studied by three-dimensional molecular theory of solvation
    • Drabik P, Gusarov S, Kovalenko A (2007) Microtubule stability studied by three-dimensional molecular theory of solvation. Biophys J 92:394-403.
    • (2007) Biophys J , vol.92 , pp. 394-403
    • Drabik, P.1    Gusarov, S.2    Kovalenko, A.3
  • 27
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief M, Pascual J, Saraste M, Gaub H (1999) Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles. J Mol Biol 286:553-561.
    • (1999) J Mol Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.4
  • 28
    • 0033523904 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates in titin modules
    • Marszalek P, et al. (1999) Mechanical unfolding intermediates in titin modules. Nature 402:100-103.
    • (1999) Nature , vol.402 , pp. 100-103
    • Marszalek, P.1
  • 29
    • 38049119865 scopus 로고    scopus 로고
    • Revealing the bifurcation in the unfolding pathways of GFP using single molecule experiments and simulations
    • Mickler M, et al. (2007) Revealing the bifurcation in the unfolding pathways of GFP using single molecule experiments and simulations. Proc Natl Acad Sci USA 104:20268-20273.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20268-20273
    • Mickler, M.1
  • 30
    • 33846193288 scopus 로고    scopus 로고
    • Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins
    • Hyeon C, Dima RI, Thirumalai D (2006) Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins. Structure 14:1633-1645.
    • (2006) Structure , vol.14 , pp. 1633-1645
    • Hyeon, C.1    Dima, R.I.2    Thirumalai, D.3
  • 31
    • 33750447980 scopus 로고    scopus 로고
    • Unusual mechanical stability of a minimal RNA kissing complex
    • Li PTX, Bustamante C, Tinoco I (2006) Unusual mechanical stability of a minimal RNA kissing complex. Proc Natl Acad Sci USA 103:15847-15852.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15847-15852
    • Li, P.T.X.1    Bustamante, C.2    Tinoco, I.3
  • 32
    • 0030687570 scopus 로고    scopus 로고
    • The alpha- and beta-tubulin folding pathways
    • Lewis S, Tian G, Cowan N (1997) The alpha- and beta-tubulin folding pathways. Trends Cell Biol 7:479-484.
    • (1997) Trends Cell Biol , vol.7 , pp. 479-484
    • Lewis, S.1    Tian, G.2    Cowan, N.3
  • 34
    • 0033954256 scopus 로고    scopus 로고
    • The protein databank
    • Berman HM, et al. (2000) The protein databank. Nucleic Acids Res 28:235-242.
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 36
    • 0242585007 scopus 로고    scopus 로고
    • Protein-protein unbinding induced by force: Single-molecule studies
    • Weisel J, Shuman H, Litvinov R (2003) Protein-protein unbinding induced by force: Single-molecule studies. Curr Opin Struct Biol 13:227-235.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 227-235
    • Weisel, J.1    Shuman, H.2    Litvinov, R.3
  • 37
    • 0022180080 scopus 로고
    • The interaction between subunits in the tubulin dimer
    • Serrano L, Avila J (1985) The interaction between subunits in the tubulin dimer. Biochem J 230:551-556.
    • (1985) Biochem J , vol.230 , pp. 551-556
    • Serrano, L.1    Avila, J.2
  • 38
    • 33646203784 scopus 로고    scopus 로고
    • Forced-unfolding and force-quench refolding of RNA hairpins
    • Hyeon C, Thirumalai D (2006) Forced-unfolding and force-quench refolding of RNA hairpins. Biophys J 90:3410-3427.
    • (2006) Biophys J , vol.90 , pp. 3410-3427
    • Hyeon, C.1    Thirumalai, D.2
  • 39
    • 0035957361 scopus 로고    scopus 로고
    • Chemically distinct transition states govern rapid dissociation of single L-selectin bonds under force
    • Evans E, Leung A, Hammer D, Simon S (2001) Chemically distinct transition states govern rapid dissociation of single L-selectin bonds under force. Proc Natl Acad Sci USA 98:3784-3789.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3784-3789
    • Evans, E.1    Leung, A.2    Hammer, D.3    Simon, S.4
  • 40
    • 0347363907 scopus 로고    scopus 로고
    • Tubulin equilibrium unfolding followed by time-resolved fluorescence correlation spectroscopy
    • Sanchez SA, Brunet JE, Jameson DM, Lagos R, Monasterio O (2004) Tubulin equilibrium unfolding followed by time-resolved fluorescence correlation spectroscopy. Prot Sci 13:81-88.
    • (2004) Prot Sci , vol.13 , pp. 81-88
    • Sanchez, S.A.1    Brunet, J.E.2    Jameson, D.M.3    Lagos, R.4    Monasterio, O.5
  • 41
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • Veitshans T, Klimov DK, Thirumalai D (1996) Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties. Folding Des 2:1-22.
    • (1996) Folding Des , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.K.2    Thirumalai, D.3


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