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Volumn 450, Issue 7170, 2007, Pages 695-701

The molecular architecture of the nuclear pore complex

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PROTEIN;

EID: 36749045172     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06405     Document Type: Article
Times cited : (875)

References (57)
  • 1
    • 33646519676 scopus 로고    scopus 로고
    • The nuclear pore complex up close
    • Lim, R. Y. & Fahrenkrog, B. The nuclear pore complex up close. Curr. Opin. Cell Biol. 18, 342-347 (2006).
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 342-347
    • Lim, R.Y.1    Fahrenkrog, B.2
  • 2
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I. G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65, 570-594 (2001).
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 3
    • 0036591883 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Cargo trafficking across the border
    • Weis, K. Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14, 328-335 (2002).
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 328-335
    • Weis, K.1
  • 4
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function, and dynamics of the nuclear periphery
    • Hetzer, M., Walther, T. C. & Mattaj, I. W. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21, 347-380 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 347-380
    • Hetzer, M.1    Walther, T.C.2    Mattaj, I.W.3
  • 5
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic nuclear pore complexes: Life on the edge
    • Tran, E. J. & Wente, S. R. Dynamic nuclear pore complexes: life on the edge. Cell 125, 1041-1053 (2006).
    • (2006) Cell , vol.125 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 6
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651 (2000).
    • (2000) J. Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1
  • 8
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey, C. W. & Radermacher, M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1-19 (1993).
    • (1993) J. Cell Biol , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 9
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • Beck, M. et al. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306, 1387-1390 (2004).
    • (2004) Science , vol.306 , pp. 1387-1390
    • Beck, M.1
  • 10
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw, J. E., Carragher, B. O. & Milligan, R. A. Architecture and design of the nuclear pore complex. Cell 69, 1133-1141 (1992).
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 11
    • 1042267370 scopus 로고    scopus 로고
    • Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments
    • Kiseleva, E. et al. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J. Struct. Biol. 145, 272-288 (2004).
    • (2004) J. Struct. Biol , vol.145 , pp. 272-288
    • Kiseleva, E.1
  • 12
    • 0037453221 scopus 로고    scopus 로고
    • Cryo-electron tomography provides novel insights into nuclear pore architecture: Implications for nucleocytoplasmic transport
    • Stoffler, D. et al. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328, 119-130 (2003).
    • (2003) J. Mol. Biol , vol.328 , pp. 119-130
    • Stoffler, D.1
  • 13
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang, Q., Rout, M. P. & Akey, C. W. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1, 223-234 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 14
    • 36749088906 scopus 로고    scopus 로고
    • Determining the architectures of macromolecular assemblies
    • doi:10.1038/nature06404 this issue
    • Alber, F. et al. Determining the architectures of macromolecular assemblies. Nature doi:10.1038/nature06404 (this issue).
    • Nature
    • Alber, F.1
  • 15
    • 4344700329 scopus 로고    scopus 로고
    • Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket
    • Krull, S., Thyberg, J., Bjorkroth, B., Rackwitz, H. R. & Cordes, V. C. Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Mol. Biol. Cell 15, 4261-4277 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4261-4277
    • Krull, S.1    Thyberg, J.2    Bjorkroth, B.3    Rackwitz, H.R.4    Cordes, V.C.5
  • 16
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Pante, N. & Kann, M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 13, 425-434 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 17
    • 9444273167 scopus 로고    scopus 로고
    • Components of coated vesicles and nuclear pore complexes share a common molecular architecture
    • Devos, D. et al. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol. 2, e380 (2004).
    • (2004) PLoS Biol , vol.2
    • Devos, D.1
  • 18
    • 33144488960 scopus 로고    scopus 로고
    • Simple fold composition and modular architecture of the nuclear pore complex
    • Devos, D. et al. Simple fold composition and modular architecture of the nuclear pore complex. Proc. Natl Acad. Sci. USA 103, 2172-2177 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2172-2177
    • Devos, D.1
  • 19
    • 10344262047 scopus 로고    scopus 로고
    • Molecular model for a complete clathrin lattice from electron cryomicroscopy
    • Fotin, A. et al. Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature 432, 573-579 (2004).
    • (2004) Nature , vol.432 , pp. 573-579
    • Fotin, A.1
  • 20
    • 30544436808 scopus 로고    scopus 로고
    • Structure of the Sec13/31 COPII coat cage
    • Stagg, S. M. et al. Structure of the Sec13/31 COPII coat cage. Nature 439, 234-238 (2006).
    • (2006) Nature , vol.439 , pp. 234-238
    • Stagg, S.M.1
  • 21
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A β propeller terminal domain joins an α zigzag linker
    • ter Haar, E., Musacchio, A., Harrison, S. C. & Kirchhausen, T. Atomic structure of clathrin: a β propeller terminal domain joins an α zigzag linker. Cell 95, 563-573 (1998).
    • (1998) Cell , vol.95 , pp. 563-573
    • ter Haar, E.1    Musacchio, A.2    Harrison, S.C.3    Kirchhausen, T.4
  • 22
    • 33646351295 scopus 로고    scopus 로고
    • Protease accessibility laddering: A proteomic tool for probing protein structure
    • Dokudovskaya, S. et al. Protease accessibility laddering: a proteomic tool for probing protein structure. Structure 14, 653-660 (2006).
    • (2006) Structure , vol.14 , pp. 653-660
    • Dokudovskaya, S.1
  • 23
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath, S., Mancias, J. D., Bi, X. & Goldberg, J. Structure and organization of coat proteins in the COPII cage. Cell 129, 1325-1336 (2007).
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 24
    • 12344317884 scopus 로고    scopus 로고
    • Nuclear pore complexes: Round the bend?
    • Antonin, W. & Mattaj, I. W. Nuclear pore complexes: round the bend? Nature Cell Biol. 7, 10-12 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 10-12
    • Antonin, W.1    Mattaj, I.W.2
  • 25
    • 33846956769 scopus 로고    scopus 로고
    • A general amphipathic α-helical motif for sensing membrane curvature
    • Drin, G. et al. A general amphipathic α-helical motif for sensing membrane curvature. Nature Struct. Mol. Biol. 14, 138-146 (2007).
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 138-146
    • Drin, G.1
  • 26
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti, E., Muller, C. W. & Stewart, M. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 16, 237-244 (2006).
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 237-244
    • Conti, E.1    Muller, C.W.2    Stewart, M.3
  • 27
    • 0029021928 scopus 로고
    • Structural plasticity of the nuclear pore complex
    • Akey, C. W. Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248, 273-293 (1995).
    • (1995) J. Mol. Biol , vol.248 , pp. 273-293
    • Akey, C.W.1
  • 28
    • 0037340827 scopus 로고    scopus 로고
    • Nuclear pore complexes exceeding eightfold rotational symmetry
    • Hinshaw, J. E. & Milligan, R. A. Nuclear pore complexes exceeding eightfold rotational symmetry. J. Struct. Biol. 141, 259-268 (2003).
    • (2003) J. Struct. Biol , vol.141 , pp. 259-268
    • Hinshaw, J.E.1    Milligan, R.A.2
  • 29
    • 4143146438 scopus 로고    scopus 로고
    • The ins and outs of E-cadherin trafficking
    • Bryant, D. M. & Stow, J. L. The ins and outs of E-cadherin trafficking. Trends Cell Biol. 14, 427-434 (2004).
    • (2004) Trends Cell Biol , vol.14 , pp. 427-434
    • Bryant, D.M.1    Stow, J.L.2
  • 30
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S. & Wente, S. R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nature Cell Biol. 6, 197-206 (2004).
    • (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
  • 32
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L. & Rexach, M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl Acad. Sci. USA 100, 2450-2455 (2003).
    • (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
  • 33
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • Liu, S. M. & Stewart, M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349, 515-525 (2005).
    • (2005) J. Mol. Biol , vol.349 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 34
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality
    • Peters, R. Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality. Traffic 6, 421-427 (2005).
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 35
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck, K. & Gorlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (2001).
    • (2001) EMBO J , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 36
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-β
    • Isgro, T. A. & Schulten, K. Binding dynamics of isolated nucleoporin repeat regions to importin-β. Structure 13, 1869-1879 (2005).
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 37
    • 33846270287 scopus 로고    scopus 로고
    • Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
    • Isgro, T. A. & Schulten, K. Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J. Mol. Biol. 366, 330-345 (2007).
    • (2007) J. Mol. Biol , vol.366 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 38
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. Molecular mechanism of the nuclear protein import cycle. Nature Rev. Mol. Cell Biol. 8, 195-208 (2007).
    • (2007) Nature Rev. Mol. Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 40
    • 23444435454 scopus 로고    scopus 로고
    • Nucleoporin domain topology is linked to the transport status of the nuclear pore complex
    • Paulillo, S. M. et al. Nucleoporin domain topology is linked to the transport status of the nuclear pore complex. J. Mol. Biol. 351, 784-798 (2005).
    • (2005) J. Mol. Biol , vol.351 , pp. 784-798
    • Paulillo, S.M.1
  • 41
    • 33745451968 scopus 로고    scopus 로고
    • Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport
    • Lim, R. Y. et al. Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA 103, 9512-9517 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9512-9517
    • Lim, R.Y.1
  • 42
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • Hawryluk-Gara, L. A., Shibuya, E. K. & Wozniak, R. W. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol. Biol. Cell 16, 2382-2394 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3
  • 43
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • King, M. C., Lusk, C. P. & Blobel, G. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 442, 1003-1007 (2006).
    • (2006) Nature , vol.442 , pp. 1003-1007
    • King, M.C.1    Lusk, C.P.2    Blobel, G.3
  • 44
    • 33744915536 scopus 로고    scopus 로고
    • Importin-α-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope
    • Saksena, S., Summers, M. D., Burks, J. K., Johnson, A. E. & Braunagel, S. C. Importin-α-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope. Nature Struct. Mol. Biol. 13, 500-508 (2006).
    • (2006) Nature Struct. Mol. Biol , vol.13 , pp. 500-508
    • Saksena, S.1    Summers, M.D.2    Burks, J.K.3    Johnson, A.E.4    Braunagel, S.C.5
  • 45
    • 0028819762 scopus 로고
    • Two novel related yeast nucleoporins Nup170p and Nup157p: Complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p
    • Aitchison, J. D., Rout, M. P., Marelli, M., Blobel, G. & Wozniak, R. W. Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. J. Cell Biol. 131, 1133-1148 (1995).
    • (1995) J. Cell Biol , vol.131 , pp. 1133-1148
    • Aitchison, J.D.1    Rout, M.P.2    Marelli, M.3    Blobel, G.4    Wozniak, R.W.5
  • 46
    • 0032576573 scopus 로고    scopus 로고
    • Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p
    • Marelli, M., Aitchison, J. D. & Wozniak, R. W. 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 (1998).
    • (1998) J. Cell Biol , vol.143 , pp. 1813-1830
    • Marelli, M.1    Aitchison, J.D.2    Wozniak, R.W.3
  • 47
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou, S. et al. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84, 265-275 (1996).
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1
  • 48
    • 0026463881 scopus 로고
    • A new family of yeast nuclear pore complex proteins
    • Wente, S. R., Rout, M. P. & Blobel, G. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119, 705-723 (1992).
    • (1992) J. Cell Biol , vol.119 , pp. 705-723
    • Wente, S.R.1    Rout, M.P.2    Blobel, G.3
  • 49
    • 0020472010 scopus 로고    scopus 로고
    • Unwin, P. N. & Milligan, R. A. A large particle associated with the perimeter of the nuclear pore complex. J. Cell Biol. 93, 63-75 (1982).
    • Unwin, P. N. & Milligan, R. A. A large particle associated with the perimeter of the nuclear pore complex. J. Cell Biol. 93, 63-75 (1982).
  • 50
    • 70449590619 scopus 로고    scopus 로고
    • Yeast genome evolution-the origin of the species
    • in the press
    • Scannell, D. R., Butler, G. & Wolfe, K. H. Yeast genome evolution-the origin of the species. Yeast. (in the press).
    • Yeast
    • Scannell, D.R.1    Butler, G.2    Wolfe, K.H.3
  • 51
    • 0032998442 scopus 로고    scopus 로고
    • Phylogenetic analysis of components of the eukaryotic vesicle transport system reveals a common origin of adaptor protein complexes 1, 2, and 3 and the F subcomplex of the coatomer COPI
    • Schledzewski, K., Brinkmann, H. & Mendel, R. R. Phylogenetic analysis of components of the eukaryotic vesicle transport system reveals a common origin of adaptor protein complexes 1, 2, and 3 and the F subcomplex of the coatomer COPI. J. Mol. Evol. 48, 770-778 (1999).
    • (1999) J. Mol. Evol , vol.48 , pp. 770-778
    • Schledzewski, K.1    Brinkmann, H.2    Mendel, R.R.3
  • 52
    • 0029129566 scopus 로고
    • A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p
    • Grandi, P. et al. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J. Cell Biol. 130, 1263-1273 (1995).
    • (1995) J. Cell Biol , vol.130 , pp. 1263-1273
    • Grandi, P.1
  • 53
    • 0031797358 scopus 로고    scopus 로고
    • Functional characterization of a Nup159p-containing nuclear pore subcomplex
    • Belgareh, N. et al. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol. Biol. Cell 9, 3475-3492 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3475-3492
    • Belgareh, N.1
  • 54
    • 0034604646 scopus 로고    scopus 로고
    • Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex
    • Bailer, S. M. et al. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J. Biol. Chem. 275, 23540-23548 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 23540-23548
    • Bailer, S.M.1
  • 55
    • 0035158475 scopus 로고    scopus 로고
    • The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport
    • Bailer, S. M., Balduf, C. & Hurt, E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol. Cell. Biol. 21, 7944-7955(2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 7944-7955
    • Bailer, S.M.1    Balduf, C.2    Hurt, E.3
  • 56
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 57
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding, J., Biegert, A. & Lupas, A. N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248 (2005).
    • (2005) Nucleic Acids Res , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3


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