메뉴 건너뛰기




Volumn 108, Issue 9, 2015, Pages 2322-2332

Molecular Investigations into the Mechanics of a Muscle Anchoring Complex

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; MUSCLE PROTEIN; PROTEIN BINDING; TELETHONIN PROTEIN, RAT;

EID: 84929660623     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.03.036     Document Type: Article
Times cited : (2)

References (50)
  • 1
    • 1842858197 scopus 로고    scopus 로고
    • Striated muscle cytoarchitecture: An intricate web of form and function
    • K.A. Clark, and A.S. McElhinny C.C. Gregorio Striated muscle cytoarchitecture: an intricate web of form and function Annu. Rev. Cell Dev. Biol. 18 2002 637 706
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 637-706
    • Clark, K.A.1    McElhinny, A.S.2    Gregorio, C.C.3
  • 2
    • 30544435275 scopus 로고    scopus 로고
    • Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk
    • P. Zou, and N. Pinotsis M. Wilmanns Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk Nature 439 2006 229 233
    • (2006) Nature , vol.439 , pp. 229-233
    • Zou, P.1    Pinotsis, N.2    Wilmanns, M.3
  • 3
    • 0034776199 scopus 로고    scopus 로고
    • Telethonin and other new proteins of the Z-disc of skeletal muscle
    • G. Faulkner, G. Lanfranchi, and G. Valle Telethonin and other new proteins of the Z-disc of skeletal muscle IUBMB Life 51 2001 275 282
    • (2001) IUBMB Life , vol.51 , pp. 275-282
    • Faulkner, G.1    Lanfranchi, G.2    Valle, G.3
  • 4
    • 33748331350 scopus 로고    scopus 로고
    • The Ig doublet Z1Z2: A model system for the hybrid analysis of conformational dynamics in Ig tandems from titin
    • M. Marino, and P. Zou O. Mayans The Ig doublet Z1Z2: a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin Structure 14 2006 1437 1447
    • (2006) Structure , vol.14 , pp. 1437-1447
    • Marino, M.1    Zou, P.2    Mayans, O.3
  • 5
    • 69449083856 scopus 로고    scopus 로고
    • The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk
    • M. Bertz, M. Wilmanns, and M. Rief The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk Proc. Natl. Acad. Sci. USA 106 2009 13307 133310
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13307-133310
    • Bertz, M.1    Wilmanns, M.2    Rief, M.3
  • 6
    • 33644846751 scopus 로고    scopus 로고
    • Mechanical strength of the titin Z1Z2-telethonin complex
    • E.H. Lee, and M. Gao K. Schulten Mechanical strength of the titin Z1Z2-telethonin complex Structure 14 2006 497 509
    • (2006) Structure , vol.14 , pp. 497-509
    • Lee, E.H.1    Gao, M.2    Schulten, K.3
  • 7
    • 34548645722 scopus 로고    scopus 로고
    • Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model
    • E.H. Lee, and J. Hsin K. Schulten Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model Biophys. J. 93 2007 1719 1735
    • (2007) Biophys. J. , vol.93 , pp. 1719-1735
    • Lee, E.H.1    Hsin, J.2    Schulten, K.3
  • 8
    • 11344285181 scopus 로고    scopus 로고
    • Study of the Villin headpiece folding dynamics by combining coarse-grained Monte Carlo evolution and all-atom molecular dynamics
    • G.M. De Mori, G. Colombo, and C. Micheletti Study of the Villin headpiece folding dynamics by combining coarse-grained Monte Carlo evolution and all-atom molecular dynamics Proteins 58 2005 459 471
    • (2005) Proteins , vol.58 , pp. 459-471
    • De Mori, G.M.1    Colombo, G.2    Micheletti, C.3
  • 9
    • 28844494903 scopus 로고    scopus 로고
    • Coarse-grained model of proteins incorporating atomistic detail of the active site
    • M. Neri, and C. Anselmi P. Carloni Coarse-grained model of proteins incorporating atomistic detail of the active site Phys. Rev. Lett. 95 2005 218102
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 218102
    • Neri, M.1    Anselmi, C.2    Carloni, P.3
  • 10
    • 27144440086 scopus 로고    scopus 로고
    • Efficient sampling of protein structures by model hopping
    • W. Kwak, and U.H.E. Hansmann Efficient sampling of protein structures by model hopping Phys. Rev. Lett. 95 2005 138102
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 138102
    • Kwak, W.1    Hansmann, U.H.E.2
  • 11
    • 34547926023 scopus 로고    scopus 로고
    • Multigraining: An algorithm for simultaneous fine-grained and coarse-grained simulation of molecular systems
    • M. Christen, and W.F. van Gunsteren Multigraining: an algorithm for simultaneous fine-grained and coarse-grained simulation of molecular systems J. Chem. Phys. 124 2006 154106
    • (2006) J. Chem. Phys. , vol.124 , pp. 154106
    • Christen, M.1    Van Gunsteren, W.F.2
  • 12
    • 33646123091 scopus 로고    scopus 로고
    • Coarse-grained modeling of the actin filament derived from atomistic-scale simulations
    • J.-W. Chu, and G.A. Voth Coarse-grained modeling of the actin filament derived from atomistic-scale simulations Biophys. J. 90 2006 1572 1582
    • (2006) Biophys. J. , vol.90 , pp. 1572-1582
    • Chu, J.-W.1    Voth, G.A.2
  • 13
    • 36849057606 scopus 로고    scopus 로고
    • Coarse-grained free energy functions for studying protein conformational changes: A double-well network model
    • J.-W. Chu, and G.A. Voth Coarse-grained free energy functions for studying protein conformational changes: a double-well network model Biophys. J. 93 2007 3860 3871
    • (2007) Biophys. J. , vol.93 , pp. 3860-3871
    • Chu, J.-W.1    Voth, G.A.2
  • 14
    • 34548304871 scopus 로고    scopus 로고
    • Protein conformational transitions explored by mixed elastic network models
    • W. Zheng, B.R. Brooks, and G. Hummer Protein conformational transitions explored by mixed elastic network models Proteins 69 2007 43 57
    • (2007) Proteins , vol.69 , pp. 43-57
    • Zheng, W.1    Brooks, B.R.2    Hummer, G.3
  • 15
    • 33846193288 scopus 로고    scopus 로고
    • Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins
    • C. Hyeon, R.I. Dima, and D. Thirumalai Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins Structure 14 2006 1633 1645
    • (2006) Structure , vol.14 , pp. 1633-1645
    • Hyeon, C.1    Dima, R.I.2    Thirumalai, D.3
  • 16
    • 38049119865 scopus 로고    scopus 로고
    • Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations
    • M. Mickler, and R.I. Dima M. Rief Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations Proc. Natl. Acad. Sci. USA 104 2007 20268 20273
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20268-20273
    • Mickler, M.1    Dima, R.I.2    Rief, M.3
  • 17
    • 57349100824 scopus 로고    scopus 로고
    • Probing the origin of tubulin rigidity with molecular simulations
    • R.I. Dima, and H. Joshi Probing the origin of tubulin rigidity with molecular simulations Proc. Natl. Acad. Sci. USA 105 2008 15743 15748
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15743-15748
    • Dima, R.I.1    Joshi, H.2
  • 18
    • 80855133530 scopus 로고    scopus 로고
    • Mechanism of fibrin(ogen) forced unfolding
    • A. Zhmurov, and A.E. Brown V. Barsegov Mechanism of fibrin(ogen) forced unfolding Structure 19 2011 1615 1624
    • (2011) Structure , vol.19 , pp. 1615-1624
    • Zhmurov, A.1    Brown, A.E.2    Barsegov, V.3
  • 19
    • 84864192760 scopus 로고    scopus 로고
    • Multiscale modeling of the nanomechanics of microtubule protofilaments
    • K.E. Theisen, and A. Zhmurov R.I. Dima Multiscale modeling of the nanomechanics of microtubule protofilaments J. Phys. Chem. B 116 2012 8545 8555
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8545-8555
    • Theisen, K.E.1    Zhmurov, A.2    Dima, R.I.3
  • 20
    • 84885464577 scopus 로고    scopus 로고
    • Mechanics of severing for large microtubule complexes revealed by coarse-grained simulations
    • K.E. Theisen, and N.J. Desai R.I. Dima Mechanics of severing for large microtubule complexes revealed by coarse-grained simulations J. Chem. Phys. 139 2013 121926
    • (2013) J. Chem. Phys. , vol.139 , pp. 121926
    • Theisen, K.E.1    Desai, N.J.2    Dima, R.I.3
  • 21
    • 33847770916 scopus 로고    scopus 로고
    • Internal strain regulates the nucleotide binding site of the kinesin leading head
    • C. Hyeon, and J.N. Onuchic Internal strain regulates the nucleotide binding site of the kinesin leading head Proc. Natl. Acad. Sci. USA 104 2007 2175 2180
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2175-2180
    • Hyeon, C.1    Onuchic, J.N.2
  • 22
    • 84859417131 scopus 로고    scopus 로고
    • Dissecting the kinematics of the kinesin step
    • Z. Zhang, and D. Thirumalai Dissecting the kinematics of the kinesin step Structure 20 2012 628 640
    • (2012) Structure , vol.20 , pp. 628-640
    • Zhang, Z.1    Thirumalai, D.2
  • 24
    • 79956370148 scopus 로고    scopus 로고
    • Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins
    • Z. Liu, and G. Reddy D. Thirumalai Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins Proc. Natl. Acad. Sci. USA 108 2011 7787 7792
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7787-7792
    • Liu, Z.1    Reddy, G.2    Thirumalai, D.3
  • 26
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, and M. Gautel H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 1109 1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Gaub, H.E.3
  • 27
    • 77958019726 scopus 로고    scopus 로고
    • Sop-GPU: Accelerating biomolecular simulations in the centisecond timescale using graphics processors
    • A. Zhmurov, and R.I. Dima V. Barsegov Sop-GPU: accelerating biomolecular simulations in the centisecond timescale using graphics processors Proteins 78 2010 2984 2999
    • (2010) Proteins , vol.78 , pp. 2984-2999
    • Zhmurov, A.1    Dima, R.I.2    Barsegov, V.3
  • 28
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • V. Sobolev, and A. Sorokine M. Edelman Automated analysis of interatomic contacts in proteins Bioinformatics 15 1999 327 332
    • (1999) Bioinformatics , vol.15 , pp. 327-332
    • Sobolev, V.1    Sorokine, A.2    Edelman, M.3
  • 29
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • D. Qiu, and P.S. Shenkin W.C. Still The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii J. Phys. Chem. A 101 1997 3005 3014
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Still, W.C.3
  • 30
    • 0036138028 scopus 로고    scopus 로고
    • Evaluation of a fast implicit solvent model for molecular dynamics simulations
    • P. Ferrara, J. Apostolakis, and A. Caflisch Evaluation of a fast implicit solvent model for molecular dynamics simulations Proteins 46 2002 24 33
    • (2002) Proteins , vol.46 , pp. 24-33
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 31
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • D. Eisenberg, and A.D. McLachlan Solvation energy in protein folding and binding Nature 319 1986 199 203
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 32
    • 77249096356 scopus 로고    scopus 로고
    • Exploring the contribution of collective motions to the dynamics of forced-unfolding in tubulin
    • H. Joshi, and F. Momin R.I. Dima Exploring the contribution of collective motions to the dynamics of forced-unfolding in tubulin Biophys. J. 98 2010 657 666
    • (2010) Biophys. J. , vol.98 , pp. 657-666
    • Joshi, H.1    Momin, F.2    Dima, R.I.3
  • 34
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • G.I. Bell Models for the specific adhesion of cells to cells Science 200 1978 618 627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 35
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • E. Evans, and K. Ritchie Dynamic strength of molecular adhesion bonds Biophys. J. 72 1997 1541 1555
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 36
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - and chemistry in single molecular bonds
    • E. Evans Probing the relation between force - lifetime - and chemistry in single molecular bonds Annu. Rev. Biophys. Biomol. Struct. 30 2001 105 128
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 38
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • R. Knöll, and M. Hoshijima K.R. Chien The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy Cell 111 2002 943 955
    • (2002) Cell , vol.111 , pp. 943-955
    • Knöll, R.1    Hoshijima, M.2    Chien, K.R.3
  • 39
    • 80053046816 scopus 로고    scopus 로고
    • Telethonin deficiency is associated with maladaptation to biomechanical stress in the mammalian heart
    • R. Knöll, and W.A. Linke K.R. Chien Telethonin deficiency is associated with maladaptation to biomechanical stress in the mammalian heart Circ. Res. 109 2011 758 769
    • (2011) Circ. Res. , vol.109 , pp. 758-769
    • Knöll, R.1    Linke, W.A.2    Chien, K.R.3
  • 40
    • 9644281144 scopus 로고    scopus 로고
    • Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy
    • T. Hayashi, and T. Arimura A. Kimura Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy J. Am. Coll. Cardiol. 44 2004 2192 2201
    • (2004) J. Am. Coll. Cardiol. , vol.44 , pp. 2192-2201
    • Hayashi, T.1    Arimura, T.2    Kimura, A.3
  • 41
    • 84891724611 scopus 로고    scopus 로고
    • Structure of giant muscle proteins
    • L.C. Meyer, and N.T. Wright Structure of giant muscle proteins Front. Physiol 4 2013 368
    • (2013) Front. Physiol , vol.4 , pp. 368
    • Meyer, L.C.1    Wright, N.T.2
  • 42
    • 84905640736 scopus 로고    scopus 로고
    • E pluribus unum, no more: From one crystal, many conformations
    • R.A. Woldeyes, D.A. Sivak, and J.S. Fraser E pluribus unum, no more: from one crystal, many conformations Curr. Opin. Struct. Biol. 28 2014 56 62
    • (2014) Curr. Opin. Struct. Biol. , vol.28 , pp. 56-62
    • Woldeyes, R.A.1    Sivak, D.A.2    Fraser, J.S.3
  • 43
    • 84885861180 scopus 로고    scopus 로고
    • Impact and progress in small and wide angle x-ray scattering (SAXS and WAXS)
    • M.A. Graewert, and D.I. Svergun Impact and progress in small and wide angle x-ray scattering (SAXS and WAXS) Curr. Opin. Struct. Biol. 23 2013 748 754
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 748-754
    • Graewert, M.A.1    Svergun, D.I.2
  • 44
    • 84865525834 scopus 로고    scopus 로고
    • Integrative structural modeling with small angle x-ray scattering profiles
    • D. Schneidman-Duhovny, S.J. Kim, and A. Sali Integrative structural modeling with small angle x-ray scattering profiles BMC Struct. Biol. 12 2012 17
    • (2012) BMC Struct. Biol. , vol.12 , pp. 17
    • Schneidman-Duhovny, D.1    Kim, S.J.2    Sali, A.3
  • 45
    • 84907251322 scopus 로고    scopus 로고
    • Combining single-molecule manipulation and single-molecule detection
    • J.C. Cordova, and D.K. Das M.J. Lang Combining single-molecule manipulation and single-molecule detection Curr. Opin. Struct. Biol. 28 2014 142 148
    • (2014) Curr. Opin. Struct. Biol. , vol.28 , pp. 142-148
    • Cordova, J.C.1    Das, D.K.2    Lang, M.J.3
  • 46
    • 40849142370 scopus 로고    scopus 로고
    • Elastic bond network model for protein unfolding mechanics
    • H. Dietz, and M. Rief Elastic bond network model for protein unfolding mechanics Phys. Rev. Lett. 100 2008 098101
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 098101
    • Dietz, H.1    Rief, M.2
  • 47
    • 84897387243 scopus 로고    scopus 로고
    • Evidence of disorder in biological molecules from single-molecule pulling experiments
    • C. Hyeon, M. Hinczewski, and D. Thirumalai Evidence of disorder in biological molecules from single-molecule pulling experiments Phys. Rev. Lett. 112 2014 138101
    • (2014) Phys. Rev. Lett. , vol.112 , pp. 138101
    • Hyeon, C.1    Hinczewski, M.2    Thirumalai, D.3
  • 48
    • 84908234815 scopus 로고    scopus 로고
    • Conformational state distributions and catalytically relevant dynamics of a hinge-bending enzyme studied by single-molecule FRET and a coarse-grained simulation
    • M. Gabba, and S. Poblete J. Fitter Conformational state distributions and catalytically relevant dynamics of a hinge-bending enzyme studied by single-molecule FRET and a coarse-grained simulation Biophys. J. 107 2014 1913 1923
    • (2014) Biophys. J. , vol.107 , pp. 1913-1923
    • Gabba, M.1    Poblete, S.2    Fitter, J.3
  • 49
    • 84860420412 scopus 로고    scopus 로고
    • Exploring the mechanical stability of the C2 domains in human synaptotagmin 1
    • L. Duan, and A. Zhmurov R.I. Dima Exploring the mechanical stability of the C2 domains in human synaptotagmin 1 J. Phys. Chem. B 115 2011 10133 10146
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10133-10146
    • Duan, L.1    Zhmurov, A.2    Dima, R.I.3
  • 50
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • T. Veitshans, D. Klimov, and D. Thirumalai Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties Fold. Des. 2 1997 1 22
    • (1997) Fold. Des. , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.2    Thirumalai, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.