메뉴 건너뛰기




Volumn 159, Issue 6, 2014, Pages 1447-1460

The structure and regulation of human muscle α-Actinin

(18)  Ribeiro, Euripedes De Almeida a   Pinotsis, Nikos a   Ghisleni, Andrea b   Salmazo, Anita a   Konarev, Petr V c   Kostan, Julius a   Sjöblom, Björn a   Schreiner, Claudia a   Polyansky, Anton A a,h   Gkougkoulia, Eirini A a   Holt, Mark R b   Aachmann, Finn L d   Žagrović, Bojan a   Bordignon, Enrica e,i   Pirker, Katharina F f   Svergun, Dmitri I c   Gautel, Mathias b   Djinović Carugo, Kristina a,g  

c DESY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ 2; CONNECTIN; PHOSPHATIDYLINOSITIDE; ACTININ; ACTN2 PROTEIN, HUMAN; LIGAND;

EID: 84925442965     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.10.056     Document Type: Article
Times cited : (164)

References (103)
  • 2
    • 0030008340 scopus 로고    scopus 로고
    • Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
    • P.M. Bayley, W.A. Findlay, and S.R. Martin Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences Protein Sci. 5 1996 1215 1228
    • (1996) Protein Sci. , vol.5 , pp. 1215-1228
    • Bayley, P.M.1    Findlay, W.A.2    Martin, S.R.3
  • 3
    • 80054713355 scopus 로고    scopus 로고
    • Structural characterization of the interactions between palladin and α-actinin
    • M.R. Beck, C.A. Otey, and S.L. Campbell Structural characterization of the interactions between palladin and α-actinin J. Mol. Biol. 413 2011 712 725
    • (2011) J. Mol. Biol. , vol.413 , pp. 712-725
    • Beck, M.R.1    Otey, C.A.2    Campbell, S.L.3
  • 4
    • 38049048081 scopus 로고    scopus 로고
    • Organizing the fluid membrane bilayer: Diseases linked to spectrin and ankyrin
    • V. Bennett, and J. Healy Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin Trends Mol. Med. 14 2008 28 36
    • (2008) Trends Mol. Med. , vol.14 , pp. 28-36
    • Bennett, V.1    Healy, J.2
  • 5
  • 7
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • D. Chin, and A.R. Means Calmodulin: a prototypical calcium sensor Trends Cell Biol. 10 2000 322 328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 9
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • K. Djinovic-Carugo, M. Gautel, J. Ylänne, and P. Young The spectrin repeat: a structural platform for cytoskeletal protein assemblies FEBS Lett. 513 2002 119 123
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylänne, J.3    Young, P.4
  • 11
    • 84896137232 scopus 로고    scopus 로고
    • The non-muscle functions of actinins: An update
    • K.S. Foley, and P.W. Young The non-muscle functions of actinins: an update Biochem. J. 459 2014 1 13
    • (2014) Biochem. J. , vol.459 , pp. 1-13
    • Foley, K.S.1    Young, P.W.2
  • 13
    • 16244409866 scopus 로고    scopus 로고
    • The crystal structure of the actin binding domain from α-actinin in its closed conformation: Structural insight into phospholipid regulation of α-actinin
    • G. Franzot, B. Sjöblom, M. Gautel, and K. Djinović Carugo The crystal structure of the actin binding domain from α-actinin in its closed conformation: structural insight into phospholipid regulation of α-actinin J. Mol. Biol. 348 2005 151 165
    • (2005) J. Mol. Biol. , vol.348 , pp. 151-165
    • Franzot, G.1    Sjöblom, B.2    Gautel, M.3    Djinović Carugo, K.4
  • 14
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function
    • K. Fukami, K. Furuhashi, M. Inagaki, T. Endo, S. Hatano, and T. Takenawa Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function Nature 359 1992 150 152
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 15
    • 0030043081 scopus 로고    scopus 로고
    • Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin
    • K. Fukami, N. Sawada, T. Endo, and T. Takenawa Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin J. Biol. Chem. 271 1996 2646 2650
    • (1996) J. Biol. Chem. , vol.271 , pp. 2646-2650
    • Fukami, K.1    Sawada, N.2    Endo, T.3    Takenawa, T.4
  • 16
    • 36448948628 scopus 로고    scopus 로고
    • Phosphoinositide binding regulates α-actinin CH2 domain structure: Analysis by hydrogen/deuterium exchange mass spectrometry
    • S.J. Full, M.L. Deinzer, P.S. Ho, and J.A. Greenwood Phosphoinositide binding regulates α-actinin CH2 domain structure: analysis by hydrogen/deuterium exchange mass spectrometry Protein Sci. 16 2007 2597 2604
    • (2007) Protein Sci. , vol.16 , pp. 2597-2604
    • Full, S.J.1    Deinzer, M.L.2    Ho, P.S.3    Greenwood, J.A.4
  • 18
    • 79951552050 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton: Who picks up the strain?
    • M. Gautel The sarcomeric cytoskeleton: who picks up the strain? Curr. Opin. Cell Biol. 23 2011 39 46
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 39-46
    • Gautel, M.1
  • 19
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
    • M. Gautel, D. Goulding, B. Bullard, K. Weber, and D.O. Fürst The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers J. Cell Sci. 109 1996 2747 2754
    • (1996) J. Cell Sci. , vol.109 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Fürst, D.O.5
  • 21
    • 0023805249 scopus 로고
    • Structural states in the Z band of skeletal muscle correlate with states of active and passive tension
    • M.A. Goldstein, L.H. Michael, J.P. Schroeter, and R.L. Sass Structural states in the Z band of skeletal muscle correlate with states of active and passive tension J. Gen. Physiol. 92 1988 113 119
    • (1988) J. Gen. Physiol. , vol.92 , pp. 113-119
    • Goldstein, M.A.1    Michael, L.H.2    Schroeter, J.P.3    Sass, R.L.4
  • 23
    • 33947306552 scopus 로고    scopus 로고
    • Novel structures for α-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton
    • C.M. Hampton, D.W. Taylor, and K.A. Taylor Novel structures for α-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton J. Mol. Biol. 368 2007 92 104
    • (2007) J. Mol. Biol. , vol.368 , pp. 92-104
    • Hampton, C.M.1    Taylor, D.W.2    Taylor, K.A.3
  • 24
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 25
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • K.P. Hoeflich, and M. Ikura Calmodulin in action: diversity in target recognition and activation mechanisms Cell 108 2002 739 742
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 26
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • G. Jones, P. Willett, R.C. Glen, A.R. Leach, and R. Taylor Development and validation of a genetic algorithm for flexible docking J. Mol. Biol. 267 1997 727 748
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 28
    • 2942735211 scopus 로고    scopus 로고
    • The ZASP-like motif in actinin-associated LIM protein is required for interaction with the α-actinin rod and for targeting to the muscle Z-line
    • T. Klaavuniemi, A. Kelloniemi, and J. Ylänne The ZASP-like motif in actinin-associated LIM protein is required for interaction with the α-actinin rod and for targeting to the muscle Z-line J. Biol. Chem. 279 2004 26402 26410
    • (2004) J. Biol. Chem. , vol.279 , pp. 26402-26410
    • Klaavuniemi, T.1    Kelloniemi, A.2    Ylänne, J.3
  • 30
    • 77957744370 scopus 로고    scopus 로고
    • The carboxyterminal EF domain of erythroid α-spectrin is necessary for optimal spectrin-actin binding
    • C. Korsgren, and S.E. Lux The carboxyterminal EF domain of erythroid α-spectrin is necessary for optimal spectrin-actin binding Blood 116 2010 2600 2607
    • (2010) Blood , vol.116 , pp. 2600-2607
    • Korsgren, C.1    Lux, S.E.2
  • 31
    • 77951167838 scopus 로고    scopus 로고
    • Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid α-spectrin in a calcium- and calmodulin-dependent manner
    • C. Korsgren, L.L. Peters, and S.E. Lux Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid α-spectrin in a calcium- and calmodulin-dependent manner J. Biol. Chem. 285 2010 4757 4770
    • (2010) J. Biol. Chem. , vol.285 , pp. 4757-4770
    • Korsgren, C.1    Peters, L.L.2    Lux, S.E.3
  • 32
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 84888876223 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates CapZβ1 and actin dynamics in response to mechanical strain
    • J. Li, and B. Russell Phosphatidylinositol 4,5-bisphosphate regulates CapZβ1 and actin dynamics in response to mechanical strain Am. J. Physiol. Heart Circ. Physiol. 305 2013 H1614 H1623
    • (2013) Am. J. Physiol. Heart Circ. Physiol. , vol.305 , pp. H1614-H1623
    • Li, J.1    Russell, B.2
  • 35
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: Sarcomere anchor for structure and signalling
    • P.K. Luther The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling J. Muscle Res. Cell Motil. 30 2009 171 185
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 171-185
    • Luther, P.K.1
  • 36
    • 0014151715 scopus 로고
    • Localization of 6S component of α-actinin at Z-band
    • T. Masaki, M. Endo, and S. Ebashi Localization of 6S component of α-actinin at Z-band J. Biochem. 62 1967 630 632
    • (1967) J. Biochem. , vol.62 , pp. 630-632
    • Masaki, T.1    Endo, M.2    Ebashi, S.3
  • 37
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • R.K. Meyer, and U. Aebi Bundling of actin filaments by α-actinin depends on its molecular length J. Cell Biol. 110 1990 2013 2024
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 40
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • J.S. Saad, J. Miller, J. Tai, A. Kim, R.H. Ghanam, and M.F. Summers Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly Proc. Natl. Acad. Sci. USA 103 2006 11364 11369
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 41
    • 53749089626 scopus 로고    scopus 로고
    • The dynamic Z bands of striated muscle cells
    • J.M. Sanger, and J.W. Sanger The dynamic Z bands of striated muscle cells Sci. Signal. 1 2008 pe37
    • (2008) Sci. Signal. , vol.1 , pp. pe37
    • Sanger, J.M.1    Sanger, J.W.2
  • 42
    • 0017130387 scopus 로고
    • Inhibition by neomycin of polyphosphoinositide turnover in subcellular fractions of guinea-pig cerebral cortex in vitro
    • J. Schacht Inhibition by neomycin of polyphosphoinositide turnover in subcellular fractions of guinea-pig cerebral cortex in vitro J. Neurochem. 27 1976 1119 1124
    • (1976) J. Neurochem. , vol.27 , pp. 1119-1124
    • Schacht, J.1
  • 45
    • 0029882295 scopus 로고    scopus 로고
    • Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications for binding IQ-motifs
    • M.B. Swindells, and M. Ikura Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications for binding IQ-motifs Nat. Struct. Biol. 3 1996 501 504
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 501-504
    • Swindells, M.B.1    Ikura, M.2
  • 46
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • S. Takeda, A. Yamashita, K. Maeda, and Y. Maéda Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form Nature 424 2003 35 41
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maéda, Y.4
  • 47
    • 0035919832 scopus 로고    scopus 로고
    • The three-dimensional structure of α-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding
    • J. Tang, D.W. Taylor, and K.A. Taylor The three-dimensional structure of α-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding J. Mol. Biol. 310 2001 845 858
    • (2001) J. Mol. Biol. , vol.310 , pp. 845-858
    • Tang, J.1    Taylor, D.W.2    Taylor, K.A.3
  • 48
    • 0027474019 scopus 로고
    • Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers
    • K.A. Taylor, and D.W. Taylor Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers J. Mol. Biol. 230 1993 196 205
    • (1993) J. Mol. Biol. , vol.230 , pp. 196-205
    • Taylor, K.A.1    Taylor, D.W.2
  • 50
    • 77955397887 scopus 로고    scopus 로고
    • Roles of titin in the structure and elasticity of the sarcomere
    • L. Tskhovrebova, and J. Trinick Roles of titin in the structure and elasticity of the sarcomere J. Biomed. Biotechnol. 2010 2010 612482
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 612482
    • Tskhovrebova, L.1    Trinick, J.2
  • 51
    • 0030740644 scopus 로고    scopus 로고
    • Flexibility and fine structure of smooth-muscle α-actinin
    • J. Winkler, H. Lünsdorf, and B.M. Jockusch Flexibility and fine structure of smooth-muscle α-actinin Eur. J. Biochem. 248 1997 193 199
    • (1997) Eur. J. Biochem. , vol.248 , pp. 193-199
    • Winkler, J.1    Lünsdorf, H.2    Jockusch, B.M.3
  • 52
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the α-actinin rod reveals an extensive torsional twist
    • J. Ylänne, K. Scheffzek, P. Young, and M. Saraste Crystal structure of the α-actinin rod reveals an extensive torsional twist Structure 9 2001 597 604
    • (2001) Structure , vol.9 , pp. 597-604
    • Ylänne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 53
    • 0034383951 scopus 로고    scopus 로고
    • The interaction of titin and α-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism
    • P. Young, and M. Gautel The interaction of titin and α-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism EMBO J. 19 2000 6331 6340
    • (2000) EMBO J. , vol.19 , pp. 6331-6340
    • Young, P.1    Gautel, M.2
  • 54
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • P. Young, C. Ferguson, S. Bañuelos, and M. Gautel Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin EMBO J. 17 1998 1614 1624
    • (1998) EMBO J. , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Bañuelos, S.3    Gautel, M.4
  • 61
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • K. Djinovic-Carugo, M. Gautel, J. Ylänne, and P. Young The spectrin repeat: a structural platform for cytoskeletal protein assemblies FEBS Lett. 513 2002 119 123
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylänne, J.3    Young, P.4
  • 62
    • 33845917564 scopus 로고    scopus 로고
    • Why molecules move along a temperature gradient
    • S. Duhr, and D. Braun Why molecules move along a temperature gradient Proc. Natl. Acad. Sci. USA 103 2006 19678 19682
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19678-19682
    • Duhr, S.1    Braun, D.2
  • 65
    • 17644402480 scopus 로고    scopus 로고
    • Phosphoinositide binding regulates α-actinin dynamics: Mechanism for modulating cytoskeletal remodeling
    • T.S. Fraley, C.B. Pereira, T.C. Tran, C. Singleton, and J.A. Greenwood Phosphoinositide binding regulates α-actinin dynamics: mechanism for modulating cytoskeletal remodeling J. Biol. Chem. 280 2005 15479 15482
    • (2005) J. Biol. Chem. , vol.280 , pp. 15479-15482
    • Fraley, T.S.1    Pereira, C.B.2    Tran, T.C.3    Singleton, C.4    Greenwood, J.A.5
  • 66
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • D.O. Fürst, M. Osborn, R. Nave, and K. Weber The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line J. Cell Biol. 106 1988 1563 1572
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 73
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 76
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 77
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 80
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • W.E. Meador, A.R. Means, and F.A. Quiocho Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures Science 262 1993 1718 1721
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 81
    • 33847012205 scopus 로고    scopus 로고
    • Profilin binding to sub-micellar concentrations of phosphatidylinositol (4,5) bisphosphate and phosphatidylinositol (3,4,5) trisphosphate
    • P.D.J. Moens, and L.A. Bagatolli Profilin binding to sub-micellar concentrations of phosphatidylinositol (4,5) bisphosphate and phosphatidylinositol (3,4,5) trisphosphate Biochim Biophys Acta 1768 2007 439 449
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 439-449
    • Moens, P.D.J.1    Bagatolli, L.A.2
  • 82
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 83
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 85
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Y. Polyhach, E. Bordignon, and G. Jeschke Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2011 2356 2366
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 86
    • 84863966856 scopus 로고    scopus 로고
    • High sensitivity and versatility of the DEER experiment on nitroxide radical pairs at Q-band frequencies
    • Y. Polyhach, E. Bordignon, R. Tschaggelar, S. Gandra, A. Godt, and G. Jeschke High sensitivity and versatility of the DEER experiment on nitroxide radical pairs at Q-band frequencies Phys. Chem. Chem. Phys. 14 2012 10762 10773
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 10762-10773
    • Polyhach, Y.1    Bordignon, E.2    Tschaggelar, R.3    Gandra, S.4    Godt, A.5    Jeschke, G.6
  • 87
    • 65449186590 scopus 로고    scopus 로고
    • PLATINUM: A web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes
    • T.V. Pyrkov, A.O. Chugunov, N.A. Krylov, D.E. Nolde, and R.G. Efremov PLATINUM: a web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes Bioinformatics 25 2009 1201 1202
    • (2009) Bioinformatics , vol.25 , pp. 1201-1202
    • Pyrkov, T.V.1    Chugunov, A.O.2    Krylov, N.A.3    Nolde, D.E.4    Efremov, R.G.5
  • 88
    • 2542469965 scopus 로고    scopus 로고
    • Origin of the anomalous circular dichroism spectra of many apomyoglobin mutants
    • E.A. Ribeiro Jr.; and C.H. Ramos Origin of the anomalous circular dichroism spectra of many apomyoglobin mutants Anal. Biochem. 329 2004 300 306
    • (2004) Anal. Biochem. , vol.329 , pp. 300-306
    • Ribeiro, Jr.E.A.1    Ramos, C.H.2
  • 89
    • 0035425883 scopus 로고    scopus 로고
    • An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase
    • L.D. Schuler, X. Daura, and W.F. van Gunsteren An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase J. Comput. Chem. 22 2001 1205 1218
    • (2001) J. Comput. Chem. , vol.22 , pp. 1205-1218
    • Schuler, L.D.1    Daura, X.2    Van Gunsteren, W.F.3
  • 92
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • J.A. Spudich, and S. Watt The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin J. Biol. Chem. 246 1971 4866 4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 93
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 94
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 95
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 96
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • V.N. Uversky Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule Biochemistry 32 1993 13288 13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 97
    • 0028879489 scopus 로고
    • Arachidonoyl-diacylglycerol kinase. Specific in vitro inhibition by polyphosphoinositides suggests a mechanism for regulation of phosphatidylinositol biosynthesis
    • J.P. Walsh, R. Suen, and J.A. Glomset Arachidonoyl-diacylglycerol kinase. Specific in vitro inhibition by polyphosphoinositides suggests a mechanism for regulation of phosphatidylinositol biosynthesis J. Biol. Chem. 270 1995 28647 28653
    • (1995) J. Biol. Chem. , vol.270 , pp. 28647-28653
    • Walsh, J.P.1    Suen, R.2    Glomset, J.A.3
  • 100
    • 0000330205 scopus 로고    scopus 로고
    • On the use of the merging R factor as a quality indicator for X-ray data
    • M.S. Weiss, and R. Hilgenfeld On the use of the merging R factor as a quality indicator for X-ray data J. Appl. Crystallogr. 30 1997 203 205
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 203-205
    • Weiss, M.S.1    Hilgenfeld, R.2
  • 101
    • 20544464108 scopus 로고    scopus 로고
    • IP-COSY, a totally in-phase and sensitive COSY experiment
    • Y. Xia, G. Legge, K.Y. Jun, Y. Qi, H. Lee, and X. Gao IP-COSY, a totally in-phase and sensitive COSY experiment Magn. Reson. Chem. 43 2005 372 379
    • (2005) Magn. Reson. Chem. , vol.43 , pp. 372-379
    • Xia, Y.1    Legge, G.2    Jun, K.Y.3    Qi, Y.4    Lee, H.5    Gao, X.6
  • 103
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • M. Zhang, T. Tanaka, and M. Ikura Calcium-induced conformational transition revealed by the solution structure of apo calmodulin Nat. Struct. Biol. 2 1995 758 767
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.