메뉴 건너뛰기




Volumn 5, Issue 9, 2009, Pages

Global motions of the nuclear pore complex: Insights from elastic network models

Author keywords

[No Author keywords available]

Indexed keywords

COARSE-GRAINED MODELING;

EID: 70349661903     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000496     Document Type: Article
Times cited : (29)

References (62)
  • 2
    • 0029021928 scopus 로고
    • Structural plasticity of the nuclear pore complex
    • Akey CW (1995) Structural plasticity of the nuclear pore complex. J Mol Biol 248: 273-293.
    • (1995) J Mol Biol , vol.248 , pp. 273-293
    • Akey, C.W.1
  • 3
    • 0030593472 scopus 로고    scopus 로고
    • RNP export is mediated by structural reorganization of the nuclear pore basket
    • DOI 10.1006/jmbi.1996.0401
    • Kiseleva E, Goldberg MW, Daneholt B, Allen TD (1996) RNP export is mediated by structural reorganization of the nuclear pore basket. J Mol Biol 260: 304-311. (Pubitemid 26254111)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.3 , pp. 304-311
    • Kiseleva, E.1    Goldberg, M.W.2    Daneholt, B.3    Allen, T.D.4
  • 4
    • 0031907210 scopus 로고    scopus 로고
    • Active nuclear pore complexes in Chironomus: Visualization of transporter configurations related to mRNP export
    • Kiseleva E, Goldberg MW, Allen TD, Akey CW (1998) Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export. J Cell Sci 111 ( Pt2): 223-236. (Pubitemid 28064147)
    • (1998) Journal of Cell Science , vol.111 , Issue.2 , pp. 223-236
    • Kiseleva, E.1    Goldberg, M.W.2    Allen, T.D.3    Akey, C.W.4
  • 7
    • 0027439610 scopus 로고
    • Role of nuclear pore complex in simian virus 40 nuclear targeting
    • Yamada M, Kasamatsu H (1993) Role of nuclear pore complex in simian virus 40 nuclear targeting. J Virol 67: 119-130. (Pubitemid 23002971)
    • (1993) Journal of Virology , vol.67 , Issue.1 , pp. 119-130
    • Yamada, M.1    Kasamatsu, H.2
  • 10
    • 0033537992 scopus 로고    scopus 로고
    • Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy
    • DOI 10.1006/jmbi.1999.2637
    • Stoffler D, Goldie KN, Feja B, Aebi U (1999) Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J Mol Biol 287: 741-752. (Pubitemid 29176509)
    • (1999) Journal of Molecular Biology , vol.287 , Issue.4 , pp. 741-752
    • Stoffler, D.1    Goldie, K.N.2    Feja, B.3    Aebi, U.4
  • 14
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • DOI 10.1038/nature06170, PII NATURE06170
    • Beck M, Lucic V, Forster F, Baumeister W, Medalia O (2007) Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 449: 611-615. (Pubitemid 47525150)
    • (2007) Nature , vol.449 , Issue.7162 , pp. 611-615
    • Beck, M.1    Lui, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 15
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • DOI 10.1038/nrm2114, PII NRM2114
    • Stewart M (2007) Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 8: 195-208. (Pubitemid 46310545)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.3 , pp. 195-208
    • Stewart, M.1
  • 16
    • 33846270287 scopus 로고    scopus 로고
    • Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
    • Isgro TA, Schulten K (2007) Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J Mol Biol 366: 330-345.
    • (2007) J Mol Biol , vol.366 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 17
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-beta
    • Isgro TA, Schulten K (2005) Binding dynamics of isolated nucleoporin repeat regions to importin-beta. Structure 13: 1869-1879.
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 18
    • 34547657392 scopus 로고    scopus 로고
    • Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors
    • Isgro TA, Schulten K (2007) Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors. Structure 15: 977-991.
    • (2007) Structure , vol.15 , pp. 977-991
    • Isgro, T.A.1    Schulten, K.2
  • 19
    • 12344323514 scopus 로고    scopus 로고
    • Quantitative models of nuclear transport
    • Becskei A, Mattaj IW (2005) Quantitative models of nuclear transport. Curr Opin Cell Biol 17: 27-34.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 27-34
    • Becskei, A.1    Mattaj, I.W.2
  • 20
    • 1942455350 scopus 로고    scopus 로고
    • Metastable Network Model of Protein Transport through Nuclear Pores
    • Kustanovich T, Rabin Y (2004) Metastable network model of protein transport through nuclear pores. Biophys J 86: 2008-2016. (Pubitemid 38524393)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2008-2016
    • Kustanovich, T.1    Rabin, Y.2
  • 21
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality
    • DOI 10.1111/j.1600-0854.2005.00287.x
    • Peters R (2005) Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality. Traffic 6: 421-427. (Pubitemid 40542768)
    • (2005) Traffic , vol.6 , Issue.5 , pp. 421-427
    • Peters, R.1
  • 22
    • 0025180782 scopus 로고
    • Visualization of transport-related configurations of the nuclear pore transporter
    • Akey CW (1990) Visualization of transport-related configurations of the nuclear pore transporter. Biophys J 58: 341-355.
    • (1990) Biophys J , vol.58 , pp. 341-355
    • Akey, C.W.1
  • 23
    • 34047159864 scopus 로고    scopus 로고
    • Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding
    • DOI 10.1126/science.1135730
    • Melcak I, Hoelz A, Blobel G (2007) Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding. Science 315: 1729-1732. (Pubitemid 46515630)
    • (2007) Science , vol.315 , Issue.5819 , pp. 1729-1732
    • Melcak, I.1    Hoelz, A.2    Blobel, G.3
  • 24
    • 36749088906 scopus 로고    scopus 로고
    • Determining the architectures of macromolecular assemblies
    • Alber F, Dokudovskaya S, Veenhoff LM, Zhang W, Kipper J, et al. (2007) Determining the architectures of macromolecular assemblies. Nature 450: 683-694.
    • (2007) Nature , vol.450 , pp. 683-694
    • Alber, F.1    Dokudovskaya, S.2    Veenhoff, L.M.3    Zhang, W.4    Kipper, J.5
  • 26
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • DOI 10.1016/j.sbi.2005.08.007, PII S0959440X05001557, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Bahar I, Rader AJ (2005) Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol 15: 586-592. (Pubitemid 41393491)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 27
    • 36549043024 scopus 로고    scopus 로고
    • Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
    • DOI 10.1016/j.sbi.2007.09.011, PII S0959440X07001534, Catalysis and Regulation /Protein
    • Bahar I, Chennubhotla C, Tobi D (2007) Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr Opin Struct Biol 17: 633-640. (Pubitemid 350180409)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.6 , pp. 633-640
    • Bahar, I.1    Chennubhotla, C.2    Tobi, D.3
  • 28
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • DOI 10.1038/nature06407, PII NATURE06407
    • Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, et al. (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450: 913-916. (Pubitemid 350231333)
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 30
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • DOI 10.1016/j.jsb.2004.01.005, PII S1047847704000061
    • Wang Y, Rader AJ, Bahar I, Jernigan RL (2004) Global ribosome motions revealed with elastic network model. J Struct Biol 147: 302-314. (Pubitemid 39140737)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 302-314
    • Wang, Y.1    Rader, A.J.2    Bahar, I.3    Jernigan, R.L.4
  • 31
    • 14844300852 scopus 로고    scopus 로고
    • Maturation dynamics of bacteriophage HK97 capsid
    • Rader AJ, Vlad DH, Bahar I (2005) Maturation dynamics of bacteriophage HK97 capsid. Structure 13: 413-421.
    • (2005) Structure , vol.13 , pp. 413-421
    • Rader, A.J.1    Vlad, D.H.2    Bahar, I.3
  • 32
    • 9644266693 scopus 로고    scopus 로고
    • Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis
    • DOI 10.1016/j.jmb.2004.10.054, PII S0022283604013609
    • Tama F, Brooks CL III (2005) Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis. J Mol Biol 345: 299-314. (Pubitemid 39574852)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.2 , pp. 299-314
    • Tama, F.1    Brooks III, C.L.2
  • 33
    • 2342518038 scopus 로고    scopus 로고
    • On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models
    • DOI 10.1073/pnas.0400301101
    • Delarue M, Dumas P (2004) On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models. Proc Natl Acad Sci U S A 101: 6957-6962. (Pubitemid 38596425)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.18 , pp. 6957-6962
    • Delarue, M.1    Dumas, P.2
  • 34
    • 41449111298 scopus 로고    scopus 로고
    • Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data
    • Gorba C, Miyashita O, Tama F (2008) Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data. Biophys J 94: 1589-1599.
    • (2008) Biophys J , vol.94 , pp. 1589-1599
    • Gorba, C.1    Miyashita, O.2    Tama, F.3
  • 35
    • 35549005432 scopus 로고    scopus 로고
    • Nautilus pompilius Hemocyanin: 9 A Cryo-EM Structure and Molecular Model Reveal the Subunit Pathway and the Interfaces between the 70 Functional Units
    • DOI 10.1016/j.jmb.2007.09.036, PII S0022283607012247
    • Gatsogiannis C, Moeller A, Depoix F, Meissner U, Markl J (2007) Nautilus pompilius hemocyanin: 9 A cryo-EM structure and molecular model reveal the subunit pathway and the interfaces between the 70 functional units. J Mol Biol 374: 465-486. (Pubitemid 350007652)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.2 , pp. 465-486
    • Gatsogiannis, C.1    Moeller, A.2    Depoix, F.3    Meissner, U.4    Markl, J.5
  • 36
    • 34548214633 scopus 로고    scopus 로고
    • Structure of the chloroplast ribosome: Novel domains for translation regulation
    • DOI 10.1371/journal.pbio.0050209
    • Manuell AL, Quispe J, Mayfield SP (2007) Structure of the chloroplast ribosome: novel domains for translation regulation. PLoS Biol 5: e209. (Pubitemid 47328281)
    • (2007) PLoS Biology , vol.5 , Issue.8 , pp. 1785-1797
    • Manuell, A.L.1    Quispe, J.2    Mayfield, S.P.3
  • 37
    • 65449189123 scopus 로고    scopus 로고
    • Structural basis for HIV-1 DNA integration in the human genome, role of the LEDGF/P75 cofactor
    • Michel F, Crucifix C, Granger F, Eiler S, Mouscadet JF, et al. (2009) Structural basis for HIV-1 DNA integration in the human genome, role of the LEDGF/P75 cofactor. EMBO J 28: 980-991.
    • (2009) EMBO J , vol.28 , pp. 980-991
    • Michel, F.1    Crucifix, C.2    Granger, F.3    Eiler, S.4    Mouscadet, J.F.5
  • 38
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux JP, Edelstein SJ (2005) Allosteric mechanisms of signal transduction. Science 308: 1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 39
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O (1966) Simple allosteric model for membrane pumps. Nature 211: 969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 40
    • 0037221524 scopus 로고    scopus 로고
    • Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating
    • DOI 10.1128/MCB.23.2.534-542.2003
    • Shulga N, Goldfarb DS (2003) Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating. Mol Cell Biol 23: 534-542. (Pubitemid 36050547)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.2 , pp. 534-542
    • Shulga, N.1    Goldfarb, D.S.2
  • 41
    • 0032576573 scopus 로고    scopus 로고
    • Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p
    • DOI 10.1083/jcb.143.7.1813
    • Marelli M, Aitchison JD, Wozniak RW (1998) Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J Cell Biol 143: 1813-1830. (Pubitemid 29022606)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1813-1830
    • Marelli, M.1    Aitchison, J.D.2    Wozniak, R.W.3
  • 42
    • 0037049550 scopus 로고    scopus 로고
    • The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint
    • DOI 10.1083/jcb.200205068
    • Iouk T, Kerscher O, Scott RJ, Basrai MA, Wozniak RW (2002) The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J Cell Biol 159: 807-819. (Pubitemid 36008363)
    • (2002) Journal of Cell Biology , vol.159 , Issue.5 , pp. 807-819
    • Iouk, T.1    Kerscher, O.2    Scott, R.J.3    Basrai, M.A.4    Wozniak, R.W.5
  • 43
    • 0029664656 scopus 로고    scopus 로고
    • Yeast N1e3p/Nup170p is required for normal stoichiometry of FG nucleoporins within the nuclear pore complex
    • Kenna MA, Petranka JG, Reilly JL, Davis LI (1996) Yeast N1e3p/Nup170p is required for normal stoichiometry of FG nucleoporins within the nuclear pore complex. Mol Cell Biol 16: 2025-2036.
    • (1996) Mol Cell Biol , vol.16 , pp. 2025-2036
    • Kenna, M.A.1    Petranka, J.G.2    Reilly, J.L.3    Davis, L.I.4
  • 44
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel SS, Belmont BJ, Sante JM, Rexach MF (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129: 83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 45
    • 0034729194 scopus 로고    scopus 로고
    • Yeast nucleoporins involved in passive nuclear envelope permeability
    • DOI 10.1083/jcb.149.5.1027
    • Shulga N, Mosammaparast N, Wozniak R, Goldfarb DS (2000) Yeast nucleoporins involved in passive nuclear envelope permeability. J Cell Biol 149: 1027-1038. (Pubitemid 30354253)
    • (2000) Journal of Cell Biology , vol.149 , Issue.5 , pp. 1027-1038
    • Shulga, N.1    Mosammaparast, N.2    Wozniak, R.3    Goldfarb, D.S.4
  • 46
    • 0033529625 scopus 로고    scopus 로고
    • Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane
    • Kosova B, Pante N, Rollenhagen C, Hurt E (1999) Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane. J Biol Chem 274: 22646-22651. (Pubitemid 129529285)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.32 , pp. 22646-22651
    • Kosova, B.1    Pante, N.2    Rollenhagen, C.3    Hurt, E.4
  • 47
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • DOI 10.1016/S0092-8674(00)80981-2
    • Siniossoglou S, Wimmer C, Rieger M, Doye V, Tekotte H, et al. (1996) A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84: 265-275. (Pubitemid 26040845)
    • (1996) Cell , vol.84 , Issue.2 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 50
    • 0036469369 scopus 로고    scopus 로고
    • Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins
    • DOI 10.1093/emboj/21.3.387
    • Lutzmann M, Kunze R, Buerer A, Aebi U, Hurt E (2002) Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J 21: 387-397. (Pubitemid 34137300)
    • (2002) EMBO Journal , vol.21 , Issue.3 , pp. 387-397
    • Lutzmann, M.1    Kunze, R.2    Buerer, A.3    Aebi, U.4    Hurt, E.5
  • 54
    • 0027978528 scopus 로고
    • Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif
    • DOI 10.1016/0092-8674(94)90297-6
    • Fabre E, Boelens WC, Wimmer C, Mattaj IW, Hurt EC (1994) Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 78: 275-289. (Pubitemid 24241095)
    • (1994) Cell , vol.78 , Issue.2 , pp. 275-289
    • Fabre, E.1    Boelens, W.C.2    Wimmer, C.3    Mattaj, I.W.4    Hurt, E.C.5
  • 56
    • 0031453253 scopus 로고    scopus 로고
    • Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking
    • DOI 10.1146/annurev.genet.31.1.277
    • Fabre E, Hurt E (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31: 277-313. (Pubitemid 28023709)
    • (1997) Annual Review of Genetics , vol.31 , pp. 277-313
    • Fabre, E.1    Hurt, E.2
  • 57
    • 0031038521 scopus 로고    scopus 로고
    • C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure
    • Dockendorff TC, Heath CV, Goldstein AL, Snay CA, Cole CN (1997) C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure. Mol Cell Biol 17: 906-920.
    • (1997) Mol Cell Biol , vol.17 , pp. 906-920
    • Dockendorff, T.C.1    Heath, C.V.2    Goldstein, A.L.3    Snay, C.A.4    Cole, C.N.5
  • 59
    • 0032483483 scopus 로고    scopus 로고
    • Vibrational dynamics of transfer RNAs: Comparison of the free and synthetase-bound forms
    • DOI 10.1006/jmbi.1998.1978
    • Bahar I, Jernigan RL (1998) Vibrational dynamics of transfer RNAs: comparison of the free and synthetase-bound forms. J Mol Biol 281: 871-884. (Pubitemid 28408435)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.5 , pp. 871-884
    • Bahar, I.1    Jernigan, R.L.2
  • 60
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: Systematic evaluation and a new web interface
    • DOI 10.1093/bioinformatics/btl448
    • Eyal E, Yang LW, Bahar I (2006) Anisotropic network model: systematic evaluation and a new web interface. Bioinformatics 22: 2619-2627. (Pubitemid 44642600)
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2619-2627
    • Eyal, E.1    Yang, L.-W.2    Bahar, I.3
  • 61
    • 28844456158 scopus 로고    scopus 로고
    • Allostery in a coarse-grained model of protein dynamics
    • Ming D, Wall ME (2005) Allostery in a coarse-grained model of protein dynamics. Phys Rev Lett 95: 198103.
    • (2005) Phys Rev Lett , vol.95 , pp. 198103
    • Ming, D.1    Wall, M.E.2
  • 62
    • 23244442698 scopus 로고    scopus 로고
    • Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: Myosin versus kinesin
    • DOI 10.1529/biophysj.105.063305
    • Zheng W, Brooks BR (2005) Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: myosin versus kinesin. Biophys J 89: 167-178. (Pubitemid 41098273)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 167-178
    • Zheng, W.1    Brooks, B.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.