메뉴 건너뛰기




Volumn 349, Issue 3, 2005, Pages 515-525

Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p

Author keywords

Complex; Importin; Nuclear import; Nuclear transport; Nucleoporin

Indexed keywords

KARYOPHERIN BETA; NUCLEOPORIN;

EID: 19444383899     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.003     Document Type: Article
Times cited : (109)

References (58)
  • 1
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • E. Conti, and E. Izaurralde Nucleocytoplasmic transport enters the atomic age Curr. Opin. Cell Biol. 13 2001 310 319
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 3
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle
    • K. Weis Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle Cell 112 2003 441 451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 4
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • N. Mosammaparast, and L.F. Pemberton Karyopherins: from nuclear-transport mediators to nuclear-function regulators Trends Cell Biol. 14 2004 547 556
    • (2004) Trends Cell Biol. , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 5
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • M. Rexach, and G. Blobel Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins Cell 83 1995 683 692
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 6
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTF2 and FxFG-containing nucleoporins is required to mediate nuclear import of RanGDP
    • R. Bayliss, K. Ribbeck, D. Akin, H.M. Kent, C.M. Feldherr, D. Görlich, and M. Stewart Interaction between NTF2 and FxFG-containing nucleoporins is required to mediate nuclear import of RanGDP J. Mol. Biol. 293 1999 579 593
    • (1999) J. Mol. Biol. , vol.293 , pp. 579-593
    • Bayliss, R.1    Ribbeck, K.2    Akin, D.3    Kent, H.M.4    Feldherr, C.M.5    Görlich, D.6    Stewart, M.7
  • 7
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking
    • R. Bayliss, T. Littlewood, and M. Stewart Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking Cell 102 2000 99 108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 8
    • 0037124352 scopus 로고    scopus 로고
    • Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats
    • R. Bayliss, S.W. Leung, R.P. Baker, B.B. Quimby, A.H. Corbett, and M. Stewart Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats EMBO J. 21 2002 2843 2853
    • (2002) EMBO J. , vol.21 , pp. 2843-2853
    • Bayliss, R.1    Leung, S.W.2    Baker, R.P.3    Quimby, B.B.4    Corbett, A.H.5    Stewart, M.6
  • 10
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • M. Suntharalingam, and S.R. Wente Peering through the pore: nuclear pore complex structure, assembly, and function Dev. Cell 4 2003 775 789
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 11
    • 0344827223 scopus 로고    scopus 로고
    • Nuclear trafficking
    • M. Stewart Nuclear trafficking Science 302 2003 1513 1514
    • (2003) Science , vol.302 , pp. 1513-1514
    • Stewart, M.1
  • 12
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • G. Cingolini, C. Petose, K. Weis, and C.W. Müller Structure of importin-β bound to the IBB domain of importin-α Nature 399 1999 221 229
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolini, G.1    Petose, C.2    Weis, K.3    Müller, C.W.4
  • 13
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 Å resolution
    • I. Vetter, A. Arndt, U. Kutay, D. Görlich, and A. Wittinghofer Structural view of the Ran-importin β interaction at 2.3 Å resolution Cell 97 1999 635 646
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.1    Arndt, A.2    Kutay, U.3    Görlich, D.4    Wittinghofer, A.5
  • 14
    • 0034622941 scopus 로고    scopus 로고
    • The adoption of a twisted structure by importin-β is essential for the protein-protein interaction required for nuclear transport
    • S.J. Lee, N. Imamoto, H. Sakai, A. Nakagawa, S. Kose, and M. Koike The adoption of a twisted structure by importin-β is essential for the protein-protein interaction required for nuclear transport J. Mol. Biol. 302 2000 251 264
    • (2000) J. Mol. Biol. , vol.302 , pp. 251-264
    • Lee, S.J.1    Imamoto, N.2    Sakai, H.3    Nakagawa, A.4    Kose, S.5    Koike, M.6
  • 15
    • 0345374584 scopus 로고    scopus 로고
    • The structure of importin-β bound to SREBP-2: Nuclear import of a transcription factor
    • S.J. Lee, T. Sekimoto, E. Yamashita, E. Nagoshi, A. Nakagawa, and N. Imamoto The structure of importin-β bound to SREBP-2: nuclear import of a transcription factor Science 302 2003 1571 1575
    • (2003) Science , vol.302 , pp. 1571-1575
    • Lee, S.J.1    Sekimoto, T.2    Yamashita, E.3    Nagoshi, E.4    Nakagawa, A.5    Imamoto, N.6
  • 16
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2- Ran·GppNHp
    • Y.M. Chook, and G. Blobel Structure of the nuclear transport complex karyopherin-β2-Ran·GppNHp Nature 399 1999 230 237
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 17
    • 9744248734 scopus 로고    scopus 로고
    • Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex
    • C. Petosa, G. Schoehn, P. Askjaer, U. Bauer, M. Moulin, and U. Steuerwald Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex Mol. Cell 16 2004 761 775
    • (2004) Mol. Cell , vol.16 , pp. 761-775
    • Petosa, C.1    Schoehn, G.2    Askjaer, P.3    Bauer, U.4    Moulin, M.5    Steuerwald, U.6
  • 18
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the formation of a nuclear export complex
    • Y. Matsuura, and M. Stewart Structural basis for the formation of a nuclear export complex Nature 432 2004 872 877
    • (2004) Nature , vol.432 , pp. 872-877
    • Matsuura, Y.1    Stewart, M.2
  • 19
    • 0034634450 scopus 로고    scopus 로고
    • Nuclear import factors importin-α and importin-β undergo mutually induced conformational changes upon association
    • G. Cingolani, H.A. Lashuel, L. Gerace, and C.W. Müller Nuclear import factors importin-α and importin-β undergo mutually induced conformational changes upon association FEBS Letters 484 2000 291 298
    • (2000) FEBS Letters , vol.484 , pp. 291-298
    • Cingolani, G.1    Lashuel, H.A.2    Gerace, L.3    Müller, C.W.4
  • 20
    • 0346457106 scopus 로고    scopus 로고
    • Conformational variability of nucleo-cytoplasmic transport factors
    • N. Fukuhara, E. Fernandez, J. Ebert, E. Conti, and D. Svergun Conformational variability of nucleo-cytoplasmic transport factors J. Biol. Chem. 279 2004 2176 2181
    • (2004) J. Biol. Chem. , vol.279 , pp. 2176-2181
    • Fukuhara, N.1    Fernandez, E.2    Ebert, J.3    Conti, E.4    Svergun, D.5
  • 21
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell cytoplasm and the nucleus
    • D. Görlich, and U. Kutay Transport between the cell cytoplasm and the nucleus Annu. Rev. Cell Dev. Biol. 15 1999 607 660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 22
    • 1842813943 scopus 로고    scopus 로고
    • The nuclear pore complex: A jack of all trades?
    • B. Fahrenkrog, J. Koser, and U. Aebi The nuclear pore complex: a jack of all trades? Trends Biochem. Sci. 29 2004 175 182
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 175-182
    • Fahrenkrog, B.1    Koser, J.2    Aebi, U.3
  • 23
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • B. Fahrenkrog, and U. Aebi The nuclear pore complex: nucleocytoplasmic transport and beyond Nature Rev. Mol. Cell. Biol. 4 2003 757 766
    • (2003) Nature Rev. Mol. Cell. Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 24
  • 27
    • 0033966543 scopus 로고    scopus 로고
    • Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex
    • M. Damelin, and P.A. Silver Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex Mol. Cell 5 2000 133 140
    • (2000) Mol. Cell , vol.5 , pp. 133-140
    • Damelin, M.1    Silver, P.A.2
  • 28
    • 0034800318 scopus 로고    scopus 로고
    • Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like Domain of the TAP/p15 mRNA nuclear export factor
    • S. Fribourg, I.C. Braun, E. Izaurralde, and E. Conti Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like Domain of the TAP/p15 mRNA nuclear export factor Mol. Cell 8 2001 645 656
    • (2001) Mol. Cell , vol.8 , pp. 645-656
    • Fribourg, S.1    Braun, I.C.2    Izaurralde, E.3    Conti, E.4
  • 29
    • 0037459067 scopus 로고    scopus 로고
    • Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1 Å resolution
    • R.P. Grant, D. Neuhaus, and M. Stewart Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1 Å resolution J. Mol. Biol. 326 2003 849 858
    • (2003) J. Mol. Biol. , vol.326 , pp. 849-858
    • Grant, R.P.1    Neuhaus, D.2    Stewart, M.3
  • 30
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • K. Ribbeck, and D. Görlich Kinetic analysis of translocation through nuclear pore complexes EMBO J. 20 2001 1320 1330
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Görlich, D.2
  • 32
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • L.A. Strawn, T. Shen, N. Shulga, D.S. Goldfarb, and S.R. Wente Minimal nuclear pore complexes define FG repeat domains essential for transport Nature Cell Biol. 6 2004 197 206
    • (2004) Nature Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.A.1    Shen, T.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 33
    • 0041731883 scopus 로고    scopus 로고
    • Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • J. Bednenko, G. Cingolani, and L. Gerace Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport J. Cell Biol. 162 2003 391 401
    • (2003) J. Cell Biol. , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 34
    • 0142180053 scopus 로고    scopus 로고
    • A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex
    • B. Pyhtila, and M. Rexach A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex J. Biol. Chem. 278 2003 42699 42709
    • (2003) J. Biol. Chem. , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 35
    • 0033766479 scopus 로고    scopus 로고
    • Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin α
    • J. Solsbacher, P. Maurer, F. Vogel, and G. Schlenstedt Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin α Mol. Cell. Biol. 20 2000 8468 8479
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8468-8479
    • Solsbacher, J.1    Maurer, P.2    Vogel, F.3    Schlenstedt, G.4
  • 36
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • D.P. Denning, V. Uversky, S.S. Patel, A.L. Fink, and M. Rexach The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein J. Biol. Chem. 277 2002 33447 33455
    • (2002) J. Biol. Chem. , vol.277 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 37
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • D.P. Denning, S.S. Patel, V. Uversky, A.L. Fink, and M. Rexach Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded Proc. Natl Acad. Sci. USA 100 2003 2450 2455
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 38
    • 0027944460 scopus 로고
    • Nup1 mutants exhibit pleiotropic defects in nuclear pore complex function
    • A.M. Bogerd, J.A. Hoffman, D.C. Amberg, G.R. Fink, and L.I. Davis Nup1 mutants exhibit pleiotropic defects in nuclear pore complex function J. Cell Biol. 127 1994 319 332
    • (1994) J. Cell Biol. , vol.127 , pp. 319-332
    • Bogerd, A.M.1    Hoffman, J.A.2    Amberg, D.C.3    Fink, G.R.4    Davis, L.I.5
  • 39
    • 0027405398 scopus 로고
    • NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex
    • J.D. Loeb, L.I. Davis, and G.R. Fink NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex Mol. Biol. Cell 4 1993 209 222
    • (1993) Mol. Biol. Cell , vol.4 , pp. 209-222
    • Loeb, J.D.1    Davis, L.I.2    Fink, G.R.3
  • 40
    • 0028064385 scopus 로고
    • Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p
    • K.D. Belanger, M.A. Kenna, S. Wei, and L.I. Davis Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p J. Cell Biol. 126 1994 619 630
    • (1994) J. Cell Biol. , vol.126 , pp. 619-630
    • Belanger, K.D.1    Kenna, M.A.2    Wei, S.3    Davis, L.I.4
  • 41
    • 0030851465 scopus 로고    scopus 로고
    • Disassembly of RanGTP-karyopherin β complex, an intermediate in nuclear protein import
    • M. Floer, G. Blobel, and M. Rexach Disassembly of RanGTP-karyopherin β complex, an intermediate in nuclear protein import J. Biol. Chem. 272 1997 19538 19546
    • (1997) J. Biol. Chem. , vol.272 , pp. 19538-19546
    • Floer, M.1    Blobel, G.2    Rexach, M.3
  • 42
    • 0037124045 scopus 로고    scopus 로고
    • Accelerating the rate of disassembly of karyopherin:cargo complexes
    • D. Gilchrist, B. Mykytka, and M. Rexach Accelerating the rate of disassembly of karyopherin:cargo complexes J. Biol. Chem. 277 2002 18161 18172
    • (2002) J. Biol. Chem. , vol.277 , pp. 18161-18172
    • Gilchrist, D.1    Mykytka, B.2    Rexach, M.3
  • 43
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import
    • I. Ben-Efraim, and L. Gerace Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import J. Cell Biol. 152 2001 411 417
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 44
    • 0035794237 scopus 로고    scopus 로고
    • The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex
    • L.A. Strawn, T. Shen, and S. Wente The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex J. Biol. Chem. 276 2001 6445 6452
    • (2001) J. Biol. Chem. , vol.276 , pp. 6445-6452
    • Strawn, L.A.1    Shen, T.2    Wente, S.3
  • 46
    • 0035800787 scopus 로고    scopus 로고
    • Proteomic analysis of nucleoporin interacting proteins
    • N.P. Allen, L. Huang, A. Burlingame, and M. Rexach Proteomic analysis of nucleoporin interacting proteins J. Biol. Chem. 276 2001 29268 29274
    • (2001) J. Biol. Chem. , vol.276 , pp. 29268-29274
    • Allen, N.P.1    Huang, L.2    Burlingame, A.3    Rexach, M.4
  • 47
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • D. Görlich, M.J. Seewald, and K. Ribbeck Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation EMBO J. 22 2003 1088 1100
    • (2003) EMBO J. , vol.22 , pp. 1088-1100
    • Görlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 48
    • 9444254054 scopus 로고    scopus 로고
    • The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo
    • B. Zeitler, and K. Weis The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo J. Cell Biol. 167 2004 583 590
    • (2004) J. Cell Biol. , vol.167 , pp. 583-590
    • Zeitler, B.1    Weis, K.2
  • 49
    • 0035802121 scopus 로고    scopus 로고
    • The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex
    • D. Denning, B. Mykytka, N.P. Allen, L. Huang, B. Al, and M. Rexach The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex J. Cell Biol. 154 2001 937 950
    • (2001) J. Cell Biol. , vol.154 , pp. 937-950
    • Denning, D.1    Mykytka, B.2    Allen, N.P.3    Huang, L.4    Al, B.5    Rexach, M.6
  • 50
    • 0034090947 scopus 로고    scopus 로고
    • Nup2p is located on the nuclear side of the nuclear pore complex and coordinates Srp1p/importin-α export
    • J.K. Hood, J.M. Casolari, and P.A. Silver Nup2p is located on the nuclear side of the nuclear pore complex and coordinates Srp1p/importin-α export J. Cell Sci. 113 2000 1471 1480
    • (2000) J. Cell Sci. , vol.113 , pp. 1471-1480
    • Hood, J.K.1    Casolari, J.M.2    Silver, P.A.3
  • 51
    • 0032950628 scopus 로고    scopus 로고
    • Autoinhibition by an internal nuclear localisation signal revealed by the crystal structure of mammalian importin-α
    • B. Kobe Autoinhibition by an internal nuclear localisation signal revealed by the crystal structure of mammalian importin-α Nature Struct. Biol. 6 1999 388 397
    • (1999) Nature Struct. Biol. , vol.6 , pp. 388-397
    • Kobe, B.1
  • 52
    • 0142073738 scopus 로고    scopus 로고
    • Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import
    • Y. Matsuura, A. Lange, M.T. Harreman, A.H. Corbett, and M. Stewart Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import EMBO J. 22 2003 5358 5369
    • (2003) EMBO J. , vol.22 , pp. 5358-5369
    • Matsuura, Y.1    Lange, A.2    Harreman, M.T.3    Corbett, A.H.4    Stewart, M.5
  • 53
    • 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
  • 54
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project Number 4
    • Collaborative Computing Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 55
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and for locating errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and for locating errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 56
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
    • R.M. Esnouf An extensively modified version of MolScript that includes greatly enhanced colouring capabilities J. Mol. Graph. Model. 15 1997 132 136
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-136
    • Esnouf, R.M.1
  • 58
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.