메뉴 건너뛰기




Volumn 408, Issue 5, 2011, Pages 863-878

Role of the tail in the regulated state of myosin 2

Author keywords

cross linking; electron microscopy; muscle myosin; muscle regulation; smooth muscle

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUTARALDEHYDE; LYSINE; MONOMER; MYOSIN; MYOSIN 2; UNCLASSIFIED DRUG;

EID: 79955482438     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.03.019     Document Type: Article
Times cited : (33)

References (54)
  • 1
    • 0021084640 scopus 로고
    • Electron microscopic studies of myosin molecules from chicken gizzard muscle II: The effect of thiophosphorylation of the 20K-dalton light chain on the ATP-induced change in the conformation of myosin monomers
    • Onishi H., Wakabayashi T., Kamata T., and Watanabe S. Electron microscopic studies of myosin molecules from chicken gizzard muscle II: the effect of thiophosphorylation of the 20K-Dalton light chain on the ATP-induced change in the conformation of myosin monomers J. Biochem. 94 1983 1147 1154 (Pubitemid 14227241)
    • (1983) Journal of Biochemistry , vol.94 , Issue.4 , pp. 1147-1154
    • Onishi, H.1    Wakabayashi, T.2    Kamata, T.3    Watanabe, S.4
  • 2
    • 0021250602 scopus 로고
    • Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength
    • Trybus K.M., and Lowey S. Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength J. Biol. Chem. 259 1984 8564 8571 (Pubitemid 14090619)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.13 , pp. 8564-8571
    • Trybus, K.M.1    Lowey, S.2
  • 4
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
    • DOI 10.1038/302436a0
    • Craig R., Smith R., and Kendrick-Jones J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules Nature 302 1983 436 439 (Pubitemid 13164332)
    • (1983) Nature , vol.302 , Issue.5907 , pp. 436-439
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 5
    • 0026035307 scopus 로고
    • A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity
    • Ankrett R.J., Rowe A.J., Cross R.A., Kendrick-Jones J., and Bagshaw C.R. A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity J. Mol. Biol. 217 1991 323 335 (Pubitemid 121003944)
    • (1991) Journal of Molecular Biology , vol.217 , Issue.2 , pp. 323-335
    • Ankrett, R.J.1    Rowe, A.J.2    Cross, R.A.3    Kendrick-Jones, J.4    Bagshaw, C.R.5
  • 7
    • 47049110451 scopus 로고    scopus 로고
    • Head-head and head-tail interaction: A general mechanism for switching off myosin II activity in cells
    • Jung H.S., Komatsu S., Ikebe M., and Craig R. Head-head and head-tail interaction: a general mechanism for switching off myosin II activity in cells Mol. Biol. Cell 19 2008 3234 3242
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3234-3242
    • Jung, H.S.1    Komatsu, S.2    Ikebe, M.3    Craig, R.4
  • 9
    • 0029833901 scopus 로고    scopus 로고
    • Structure and function of the 10 S conformation of smooth muscle myosin
    • DOI 10.1074/jbc.271.34.20375
    • Olney J.J., Sellers J.R., and Cremo C.R. Structure and function of the 10 S conformation of smooth muscle myosin J. Biol. Chem. 271 1996 20375 20384 (Pubitemid 26281805)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20375-20384
    • Olney, J.J.1    Sellers, J.R.2    Cremo, C.R.3
  • 10
    • 0023661201 scopus 로고
    • Polymerization of vertebrate non-muscle and smooth muscle myosins
    • Kendrick-Jones J., Smith R.C., Craig R., and Citi S. Polymerization of vertebrate non-muscle and smooth muscle myosins J. Mol. Biol. 198 1987 241 252
    • (1987) J. Mol. Biol. , vol.198 , pp. 241-252
    • Kendrick-Jones, J.1    Smith, R.C.2    Craig, R.3    Citi, S.4
  • 11
    • 27744598463 scopus 로고    scopus 로고
    • Myosin filament assembly in an ever-changing myofilament lattice of smooth muscle
    • Seow C.Y. Myosin filament assembly in an ever-changing myofilament lattice of smooth muscle Am. J. Physiol.: Cell Physiol. 289 2005 C1363 C1368
    • (2005) Am. J. Physiol.: Cell Physiol. , vol.289
    • Seow, C.Y.1
  • 12
    • 34548478783 scopus 로고    scopus 로고
    • Structures of Smooth Muscle Myosin and Heavy Meromyosin in the Folded, Shutdown State
    • DOI 10.1016/j.jmb.2007.07.014, PII S0022283607009412
    • Burgess S.A., Yu S., Walker M.L., Hawkins R.J., Chalovich J.M., and Knight P.J. Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state J. Mol. Biol. 372 2007 1165 1178 (Pubitemid 47374715)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.5 , pp. 1165-1178
    • Burgess, S.A.1    Yu, S.2    Walker, M.L.3    Hawkins, R.J.4    Chalovich, J.M.5    Knight, P.J.6
  • 13
    • 0038545279 scopus 로고    scopus 로고
    • Refined model of the 10 S conformation of smooth muscle myosin by cryo-electron microscopy 3D image reconstruction
    • DOI 10.1016/S0022-2836(03)00516-3
    • Liu J., Wendt T., Taylor D., and Taylor K. Refined model of the 10 S conformation of smooth muscle myosin by cryo-electron microscopy 3D image reconstruction J. Mol. Biol. 329 2003 963 972 (Pubitemid 36683153)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.5 , pp. 963-972
    • Liu, J.1    Wendt, T.2    Taylor, D.3    Taylor, K.4
  • 14
    • 0035836733 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
    • DOI 10.1073/pnas.071051098
    • Wendt T., Taylor D., Trybus K.M., and Taylor K. Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2 Proc. Natl Acad. Sci. USA 98 2001 4361 4366 (Pubitemid 32294982)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.8 , pp. 4361-4366
    • Wendt, T.1    Taylor, D.2    Trybus, K.M.3    Taylor, K.4
  • 15
    • 24144484776 scopus 로고    scopus 로고
    • Atomic model of a myosin filament in the relaxed state
    • DOI 10.1038/nature03920
    • Woodhead J.L., Zhao F.Q., Craig R., Egelman E.H., Alamo L., and Padrón R. Atomic model of a myosin filament in the relaxed state Nature 436 2005 1195 1199 (Pubitemid 41232301)
    • (2005) Nature , vol.436 , Issue.7054 , pp. 1195-1199
    • Woodhead, J.L.1    Zhao, F.-Q.2    Craig, R.3    Egelman, E.H.4    Alamo, L.5    Padron, R.6
  • 17
    • 47049110051 scopus 로고    scopus 로고
    • 2+-regulated myosin filaments upon relaxation
    • 2+-regulated myosin filaments upon relaxation J. Mol. Biol. 381 2008 256 260
    • (2008) J. Mol. Biol. , vol.381 , pp. 256-260
    • Zhao, F.Q.1    Craig, R.2
  • 18
    • 10044234207 scopus 로고    scopus 로고
    • The requirement for mechanical coupling between head and S2 domains in smooth muscle myosin ATPase regulation and its implications for dimeric motor function
    • DOI 10.1016/j.jmb.2004.10.084, PII S0022283604014056
    • Tama F., Feig M., Liu J., Brooks C.L., and Taylor K.A. The requirement for mechanical coupling between head and S2 domains in smooth muscle myosin ATPase regulation and its implications for dimeric motor function J. Mol. Biol. 345 2005 837 854 (Pubitemid 39600937)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.4 , pp. 837-854
    • Tama, F.1    Feig, M.2    Liu, J.3    Brooks III, C.L.4    Taylor, K.A.5
  • 19
    • 56249115186 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of Tarantula myosin filaments suggests how phosphorylation may regulate myosin activity
    • Alamo L., Wriggers W., Pinto A., Bartoli F., Salazar L., and Zhao F.Q. Three-dimensional reconstruction of Tarantula myosin filaments suggests how phosphorylation may regulate myosin activity J. Mol. Biol. 384 2008 780 797
    • (2008) J. Mol. Biol. , vol.384 , pp. 780-797
    • Alamo, L.1    Wriggers, W.2    Pinto, A.3    Bartoli, F.4    Salazar, L.5    Zhao, F.Q.6
  • 20
    • 0016695131 scopus 로고
    • Diversity of cross-bridge configurations in invertebrate muscles
    • Wray J.S., Vibert P.J., and Cohen C. Diversity of cross-bridge configurations in invertebrate muscles Nature 257 1975 561 564
    • (1975) Nature , vol.257 , pp. 561-564
    • Wray, J.S.1    Vibert, P.J.2    Cohen, C.3
  • 21
    • 85010249552 scopus 로고
    • Low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley H.E., and Brown W. Low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor J. Mol. Biol. 30 1967 383 434
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 22
    • 0032496165 scopus 로고    scopus 로고
    • Skeletal muscle myosin monomer in equilibrium with filaments forms a folded conformation
    • DOI 10.1074/jbc.273.19.11436
    • Katoh T., Konishi K., and Yazawa M. Skeletal muscle myosin monomer in equilibrium with filaments forms a folded conformation J. Biol. Chem. 273 1998 11436 11439 (Pubitemid 28272035)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.19 , pp. 11436-11439
    • Katoh, T.1    Konishi, K.2    Yazawa, M.3
  • 23
    • 0032859877 scopus 로고    scopus 로고
    • Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments
    • Takahashi T., Fukukawa C., Naraoka C., Katoh T., and Yazawa M. Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments J. Biochem. 126 1999 34 40 (Pubitemid 29355390)
    • (1999) Journal of Biochemistry , vol.126 , Issue.1 , pp. 34-40
    • Takahashi, T.1    Fukukawa, C.2    Naraoka, C.3    Katoh, T.4    Yazawa, M.5
  • 24
    • 55949133242 scopus 로고    scopus 로고
    • Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state
    • Zhao F.Q., Padron R., and Craig R. Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state Biophys. J. 95 2008 3322 3329
    • (2008) Biophys. J. , vol.95 , pp. 3322-3329
    • Zhao, F.Q.1    Padron, R.2    Craig, R.3
  • 25
    • 4444346487 scopus 로고    scopus 로고
    • Helical order in tarantula thick filaments requires the "closed" conformation of the myosin head
    • DOI 10.1016/j.jmb.2004.07.037, PII S0022283604008666
    • Zoghbi M.E., Woodhead J.L., Craig R., and Padron R. Helical order in tarantula thick filaments requires the "closed" conformation of the myosin head J. Mol. Biol. 342 2004 1223 1236 (Pubitemid 39207899)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.4 , pp. 1223-1236
    • Zoghbi, M.E.1    Woodhead, J.L.2    Craig, R.3    Padron, R.4
  • 26
    • 0022240738 scopus 로고
    • Structural changes that occur in scallop myosin filaments upon activation
    • DOI 10.1083/jcb.101.3.830
    • Vibert P., and Craig R. Structural changes that occur in scallop myosin filaments upon activation J. Cell Biol. 101 1985 830 837 (Pubitemid 16256836)
    • (1985) Journal of Cell Biology , vol.101 , Issue.3 , pp. 830-837
    • Vibert, P.1    Craig, R.2
  • 27
    • 76249092553 scopus 로고    scopus 로고
    • Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers
    • Stewart M.A., Franks-Skiba K., Chen S., and Cooke R. Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers Proc. Natl Acad. Sci. USA 107 2010 430 435
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 430-435
    • Stewart, M.A.1    Franks-Skiba, K.2    Chen, S.3    Cooke, R.4
  • 28
    • 33846020959 scopus 로고    scopus 로고
    • The N-terminal lobes of both regulatory light chains interact with the tail domain in the 10 S-inhibited conformation of smooth muscle myosin
    • DOI 10.1074/jbc.M606555200
    • Salzameda B., Facemyer K.C., Beck B.W., and Cremo C.R. The N-terminal lobes of both regulatory light chains interact with the tail domain in the 10 S inhibited conformation of smooth muscle myosin J. Biol. Chem. 281 2006 38801 38811 (Pubitemid 46042007)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38801-38811
    • Salzameda, B.1    Facemyer, K.C.2    Beck, B.W.3    Cremo, C.R.4
  • 29
    • 0037285299 scopus 로고    scopus 로고
    • Capturing time-resolved changes in molecular structure by negative staining
    • DOI 10.1016/S1047-8477(02)00546-4, PII S1047847702005464
    • Zhao F.Q., and Craig R. Capturing time-resolved changes in molecular structure by negative staining J. Struct. Biol. 141 2003 43 52 (Pubitemid 36269105)
    • (2003) Journal of Structural Biology , vol.141 , Issue.1 , pp. 43-52
    • Zhao, F.-Q.1    Craig, R.2
  • 30
    • 0022370052 scopus 로고
    • A conformational transition in gizzard heavy meromyosin involving the head-tail junction, resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads
    • Suzuki H., Stafford W.F. III, Slayter H.S., and Seidel J.C. A conformational transition in gizzard heavy meromyosin involving the head-tail junction, resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads J. Biol. Chem. 260 1985 14810 14817 (Pubitemid 16211018)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.27 , pp. 14810-14817
    • Suzuki, H.1    Stafford III, W.F.2    Slayter, H.S.3    Seidel, J.C.4
  • 33
    • 0023738921 scopus 로고
    • The regulatory light chain is required for folding of smooth muscle myosin
    • Trybus K.M., and Lowey S. The regulatory light chain is required for folding of smooth muscle myosin J. Biol. Chem. 263 1988 16485 16492 (Pubitemid 18262069)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.31 , pp. 16485-16492
    • Trybus, K.M.1    Lowey, S.2
  • 35
    • 0027433622 scopus 로고
    • The C-terminal helix in subdomain 4 of the regulatory light chain is essential for myosin regulation
    • Rowe T., and Kendrick-Jones J. The C-terminal helix in subdomain 4 of the regulatory light chain is essential for myosin regulation EMBO J. 12 1993 4877 4884 (Pubitemid 23330294)
    • (1993) EMBO Journal , vol.12 , Issue.12 , pp. 4877-4884
    • Rowe, T.1    Kendrick-Jones, J.2
  • 36
    • 0028556494 scopus 로고
    • Involvement of the C-terminal residues of the 20,000-dalton light chain of myosin on the regulation of smooth muscle actomyosin
    • Ikebe M., Reardon S., Mitani Y., Kamisoyama H., Matsuura M., and Ikebe R. Involvement of the C-terminal residues of the 20,000-dalton light chain of myosin on the regulation of smooth muscle actomyosin Proc. Natl Acad. Sci. USA 91 1994 9096 9100
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9096-9100
    • Ikebe, M.1    Reardon, S.2    Mitani, Y.3    Kamisoyama, H.4    Matsuura, M.5    Ikebe, R.6
  • 37
    • 0027419741 scopus 로고
    • Chimeric regulatory light chains as probes of smooth muscle myosin function
    • Trybus K.M., and Chatman T.A. Chimeric regulatory light chains as probes of smooth muscle myosin function J. Biol. Chem. 268 1993 4412 4419 (Pubitemid 23072987)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.6 , pp. 4412-4419
    • Trybus, K.M.1    Chatman, T.A.2
  • 38
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and α-helical bundles: A close relationship between sequence and structure
    • Parry D.A.D., Fraser R.D.B., and Squire J.M. Fifty years of coiled-coils and α-helical bundles: a close relationship between sequence and structure J. Struct. Biol. 163 2008 258 269
    • (2008) J. Struct. Biol. , vol.163 , pp. 258-269
    • Parry, D.A.D.1    Fraser, R.D.B.2    Squire, J.M.3
  • 41
    • 34548736602 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin
    • DOI 10.1529/biophysj.106.095802
    • Espinoza-Fonseca L.M., Kast D., and Thomas D.D. Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin Biophys. J. 93 2007 2083 2090 (Pubitemid 47437590)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2083-2090
    • Espinoza-Fonseca, L.M.1    Kast, D.2    Thomas, D.D.3
  • 42
    • 51949096545 scopus 로고    scopus 로고
    • Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin
    • Espinoza-Fonseca L.M., Kast D., and Thomas D.D. Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin J. Am. Chem. Soc. 130 2008 12208 12209
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12208-12209
    • Espinoza-Fonseca, L.M.1    Kast, D.2    Thomas, D.D.3
  • 43
    • 77952395653 scopus 로고    scopus 로고
    • Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain
    • Kast D., Espinoza-Fonseca L.M., Yi C., and Thomas D.D. Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain Proc. Natl Acad. Sci. USA 107 2010 8207 8212
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8207-8212
    • Kast, D.1    Espinoza-Fonseca, L.M.2    Yi, C.3    Thomas, D.D.4
  • 44
    • 4544308614 scopus 로고    scopus 로고
    • Novel sensors of the regulatory switch on the regulatory light chain of smooth muscle myosin
    • DOI 10.1074/jbc.M407062200
    • Mazhari S.M., Selser C.T., and Cremo C.R. Novel sensors of the regulatory switch on the regulatory light chain of smooth muscle myosin J. Biol. Chem. 279 2004 39905 39914 (Pubitemid 39258263)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39905-39914
    • Mazhari, S.M.1    Selser, C.T.2    Cremo, C.R.3
  • 45
    • 0036238517 scopus 로고    scopus 로고
    • Low-density DNA microarrays are versatile tools to screen for known mutations in hypertrophic cardiomyopathy
    • DOI 10.1002/humu.10074
    • Waldmüller S., Freund P., Mauch S., Toder R., and Vosberg H.P. Low-density DNA microarrays are versatile tools to screen for known mutations in hypertrophic cardiomyopathy Hum. Mutat. 19 2002 560 569 (Pubitemid 34461630)
    • (2002) Human Mutation , vol.19 , Issue.5 , pp. 560-569
    • Waldmuller, S.1    Freund, P.2    Mauch, S.3    Toder, R.4    Vosberg, H.-P.5
  • 47
    • 0022419381 scopus 로고
    • Negative staining of myosin molecules
    • Walker M., Knight P., and Trinick J. Negative staining of myosin molecules J. Mol. Biol. 184 1985 535 542
    • (1985) J. Mol. Biol. , vol.184 , pp. 535-542
    • Walker, M.1    Knight, P.2    Trinick, J.3
  • 49
    • 0020680292 scopus 로고
    • Ordered phosphorylation of the two 20,000 molecular weight light chains of smooth muscle myosin
    • Persechini A., and Hartshorne D.J. Ordered phosphorylation of the two 20 000 molecular weight light chains of smooth muscle myosin Biochemistry 22 1983 470 476 (Pubitemid 13146578)
    • (1983) Biochemistry , vol.22 , Issue.2 , pp. 470-476
    • Persechini, A.1    Hartshorne, D.J.2
  • 50
    • 26244466046 scopus 로고    scopus 로고
    • Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing
    • DOI 10.1016/j.jmb.2005.08.010, PII S0022283605009332
    • Straussman R., Squire J.M., Ben-Ya'acov A., and Ravid S. Skip residues and charge interactions in myosin II coiled-coils: implications for molecular packing J. Mol. Biol. 353 2005 613 628 (Pubitemid 41414735)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.3 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya'acov, A.3    Ravid, S.4
  • 51
    • 4344620779 scopus 로고    scopus 로고
    • Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules
    • DOI 10.1016/j.jsb.2004.04.004, PII S104784770400098X
    • Burgess S.A., Walker M.L., Thirumurugan K., Trinick J., and Knight P.J. Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules J. Struct. Biol. 147 2004 247 258 (Pubitemid 39140732)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 247-258
    • Burgess, S.A.1    Walker, M.L.2    Thirumurugan, K.3    Trinick, J.4    Knight, P.J.5
  • 52
    • 0017229778 scopus 로고
    • Electron microscopy of myosin molecules from muscle and non-muscle sources
    • Elliott A., Offer G., and Burridge K. Electron microscopy of myosin molecules from muscle and non-muscle sources Proc. R. Soc. London, Ser. B 193 1976 45 53
    • (1976) Proc. R. Soc. London, Ser. B , vol.193 , pp. 45-53
    • Elliott, A.1    Offer, G.2    Burridge, K.3
  • 53
    • 0036444017 scopus 로고    scopus 로고
    • Generalized Crick equations for modeling noncanonical coiled coils
    • DOI 10.1006/jsbi.2002.4448
    • Offer G., Hicks M.R., and Woolfson D.N. Generalized Crick equations for modeling noncanonical coiled coils J. Struct. Biol. 137 2002 41 53 (Pubitemid 35430420)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 41-53
    • Offer, G.1    Hicks, M.R.2    Woolfson, D.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.