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Volumn 6, Issue , 2015, Pages

Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA; INTRINSICALLY DISORDERED PROTEIN; PROTEIN P15; CARRIER PROTEIN; KIAA0101 PROTEIN, HUMAN; PROTEASOME; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84924559516     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7439     Document Type: Article
Times cited : (64)

References (59)
  • 1
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan, G. L., Pfander, B. & Jentsch, S. PCNA, the maestro of the replication fork. Cell 129, 665-679 (2007).
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 2
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M. & Kuriyan, J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79, 1233-1243 (1994).
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 3
    • 0019331504 scopus 로고
    • Crystal structure analysis of a complete turn of B-DNA
    • Wing, R. et al. Crystal structure analysis of a complete turn of B-DNA. Nature 287, 755-758 (1980).
    • (1980) Nature , vol.287 , pp. 755-758
    • Wing, R.1
  • 4
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga, G. & Hubscher, U. Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci. 116, 3051-3060 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 5
    • 84879403234 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen structure and interactions: Too many partners for one dancer?
    • De Biasio, A. & Blanco, F. J. Proliferating cell nuclear antigen structure and interactions: too many partners for one dancer? Adv. Protein Chem. Struct. Biol. 91, 1-36 (2013).
    • (2013) Adv. Protein Chem. Struct. Biol. , vol.91 , pp. 1-36
    • De Biasio, A.1    Blanco, F.J.2
  • 6
    • 0039710446 scopus 로고    scopus 로고
    • Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen
    • Jonsson, Z. O., Hindges, R. & Hubscher, U. Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. EMBO J. 17, 2412-2425 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2412-2425
    • Jonsson, Z.O.1    Hindges, R.2    Hubscher, U.3
  • 7
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis, J. M., Kelman, Z., Hurwitz, J., O'Donnell, M. & Kuriyan, J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 87, 297-306 (1996).
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 8
    • 0033957787 scopus 로고    scopus 로고
    • Sliding clamps: A (tail)ored fit
    • Hingorani, M. M. & O'Donnell, M. Sliding clamps: a (tail)ored fit. Curr. Biol. 10, R25-R29 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. R25-R29
    • Hingorani, M.M.1    O'Donnell, M.2
  • 9
    • 0035945643 scopus 로고    scopus 로고
    • p15(PAF), a novel PCNA associated factor with increased expression in tumor tissues
    • Yu, P. et al. p15(PAF), a novel PCNA associated factor with increased expression in tumor tissues. Oncogene 20, 484-489 (2001).
    • (2001) Oncogene , vol.20 , pp. 484-489
    • Yu, P.1
  • 10
    • 79959968319 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15 protein is a cell cycle-regulated anaphase-promoting complex/cyclosome substrate
    • Emanuele, M. J., Ciccia, A., Elia, A. E. & Elledge, S. J. Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15 protein is a cell cycle-regulated anaphase-promoting complex/cyclosome substrate. Proc. Natl Acad. Sci. USA 108, 9845-9850 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9845-9850
    • Emanuele, M.J.1    Ciccia, A.2    Elia, A.E.3    Elledge, S.J.4
  • 11
    • 84867101049 scopus 로고    scopus 로고
    • Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass
    • Povlsen, L. K. et al. Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Nat. Cell Biol. 14, 1089-1098 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1089-1098
    • Povlsen, L.K.1
  • 12
    • 84897900852 scopus 로고    scopus 로고
    • Proliferating cell unclear antigen-associated factor (PAF15): A novel oncogene
    • Xie, C., Yao, M. & Dong, Q. Proliferating cell unclear antigen-associated factor (PAF15): a novel oncogene. Int. J. Biochem. Cell Biol. 50C, 127-131 (2014).
    • (2014) Int. J. Biochem. Cell Biol. , vol.50 C , pp. 127-131
    • Xie, C.1    Yao, M.2    Dong, Q.3
  • 13
    • 34047247407 scopus 로고    scopus 로고
    • Oncogenic role of KIAA0101 interacting with proliferating cell nuclear antigen in pancreatic cancer
    • Hosokawa, M. et al. Oncogenic role of KIAA0101 interacting with proliferating cell nuclear antigen in pancreatic cancer. Cancer Res. 67, 2568-2576 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 2568-2576
    • Hosokawa, M.1
  • 14
    • 80051973836 scopus 로고    scopus 로고
    • KIAA0101 interacts with BRCA1 and regulates centrosome number
    • Kais, Z. et al. KIAA0101 interacts with BRCA1 and regulates centrosome number. Mol. Cancer Res. 9, 1091-1099 (2011).
    • (2011) Mol. Cancer Res. , vol.9 , pp. 1091-1099
    • Kais, Z.1
  • 15
    • 83555166247 scopus 로고    scopus 로고
    • Overexpression of KIAA0101 predicts poor prognosis in primary lung cancer patients
    • Kato, T. et al. Overexpression of KIAA0101 predicts poor prognosis in primary lung cancer patients. Lung Cancer 75, 110-118 (2012).
    • (2012) Lung Cancer , vol.75 , pp. 110-118
    • Kato, T.1
  • 16
    • 84868192650 scopus 로고    scopus 로고
    • Variant 1 of KIAA0101, overexpressed in hepatocellular carcinoma, prevents doxorubicin-induced apoptosis by inhibiting p53 activation
    • Liu, L. et al. Variant 1 of KIAA0101, overexpressed in hepatocellular carcinoma, prevents doxorubicin-induced apoptosis by inhibiting p53 activation. Hepatology 56, 1760-1769 (2012).
    • (2012) Hepatology , vol.56 , pp. 1760-1769
    • Liu, L.1
  • 17
    • 84894502149 scopus 로고    scopus 로고
    • p15(PAF) is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins
    • De Biasio, A. et al. p15(PAF) is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins. Biophys. J. 106, 865-874 (2014).
    • (2014) Biophys. J. , vol.106 , pp. 865-874
    • De Biasio, A.1
  • 18
    • 84876427538 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA) interactions in solution studied by NMR
    • De Biasio, A. et al. Proliferating cell nuclear antigen (PCNA) interactions in solution studied by NMR. PLoS ONE 7, e48390 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e48390
    • De Biasio, A.1
  • 19
    • 0034720729 scopus 로고    scopus 로고
    • A quantitative study of the in vitro binding of the C-terminal domain of p21 to PCNA: Affinity, stoichiometry, and thermodynamics
    • Zheleva, D. I. et al. A quantitative study of the in vitro binding of the C-terminal domain of p21 to PCNA: affinity, stoichiometry, and thermodynamics. Biochemistry 39, 7388-7397 (2000).
    • (2000) Biochemistry , vol.39 , pp. 7388-7397
    • Zheleva, D.I.1
  • 21
    • 0029872236 scopus 로고    scopus 로고
    • NMR analysis of interacting soluble forms of the cell-cell recognition molecules CD2 and CD48
    • McAlister, M. S. et al. NMR analysis of interacting soluble forms of the cell-cell recognition molecules CD2 and CD48. Biochemistry 35, 5982-5991 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5982-5991
    • McAlister, M.S.1
  • 22
    • 79960698348 scopus 로고    scopus 로고
    • Dynamic interaction of Hsp90 with its client protein p53
    • Park, S. J., Kostic, M. & Dyson, H. J. Dynamic interaction of Hsp90 with its client protein p53. J. Mol. Biol. 411, 158-173 (2011).
    • (2011) J. Mol. Biol. , vol.411 , pp. 158-173
    • Park, S.J.1    Kostic, M.2    Dyson, H.J.3
  • 23
    • 0035966083 scopus 로고    scopus 로고
    • NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA
    • Klein, C. et al. NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA. J. Biol. Chem. 276, 49020-49027 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 49020-49027
    • Klein, C.1
  • 25
    • 37649016453 scopus 로고    scopus 로고
    • Structure of a sliding clamp on DNA
    • Georgescu, R. E. et al. Structure of a sliding clamp on DNA. Cell 132, 43-54 (2008).
    • (2008) Cell , vol.132 , pp. 43-54
    • Georgescu, R.E.1
  • 28
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41, 1-7 (2002).
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 29
    • 9944227232 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1
    • Bruning, J. B. & Shamoo, Y. Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1. Structure 12, 2209-2219 (2004).
    • (2004) Structure , vol.12 , pp. 2209-2219
    • Bruning, J.B.1    Shamoo, Y.2
  • 31
    • 67649424560 scopus 로고    scopus 로고
    • p21 in cancer: Intricate networks and multiple activities
    • Abbas, T. & Dutta, A. p21 in cancer: intricate networks and multiple activities. Nat. Rev. Cancer 9, 400-414 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 400-414
    • Abbas, T.1    Dutta, A.2
  • 32
    • 0029873287 scopus 로고    scopus 로고
    • A 39 amino acid fragment of the cell cycle regulator p21 is sufficient to bind PCNA and partially inhibit DNA replication in vivo
    • Chen, J. et al. A 39 amino acid fragment of the cell cycle regulator p21 is sufficient to bind PCNA and partially inhibit DNA replication in vivo. Nucleic Acids Res. 24, 1727-1733 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1727-1733
    • Chen, J.1
  • 33
    • 67449103688 scopus 로고    scopus 로고
    • Structural basis for novel interactions between human translesion synthesis polymerases and proliferating cell nuclear antigen
    • Hishiki, A. et al. Structural basis for novel interactions between human translesion synthesis polymerases and proliferating cell nuclear antigen. J. Biol. Chem. 284, 10552-10560 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 10552-10560
    • Hishiki, A.1
  • 34
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman, G. D., O'Donnell, M. & Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429, 724-730 (2004).
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 35
    • 79955993911 scopus 로고    scopus 로고
    • PCNA directs type 2 RNase H activity on DNA replication and repair substrates
    • Bubeck, D. et al. PCNA directs type 2 RNase H activity on DNA replication and repair substrates. Nucleic Acids Res. 39, 3652-3666 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3652-3666
    • Bubeck, D.1
  • 36
    • 77950517365 scopus 로고    scopus 로고
    • Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange
    • Freudenthal, B. D., Gakhar, L., Ramaswamy, S. & Washington, M. T. Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange. Nat. Struct. Mol. Biol. 17, 479-484 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 479-484
    • Freudenthal, B.D.1    Gakhar, L.2    Ramaswamy, S.3    Washington, M.T.4
  • 37
    • 0035872863 scopus 로고    scopus 로고
    • A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome
    • Touitou, R. et al. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J. 20, 2367-2375 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2367-2375
    • Touitou, R.1
  • 38
    • 0024841735 scopus 로고
    • 'SPKK' motifs prefer to bind to DNA at A/T-rich sites
    • Churchill, M. E. & Suzuki, M. 'SPKK' motifs prefer to bind to DNA at A/T-rich sites. EMBO J. 8, 4189-4195 (1989).
    • (1989) EMBO J. , vol.8 , pp. 4189-4195
    • Churchill, M.E.1    Suzuki, M.2
  • 39
    • 65649099698 scopus 로고    scopus 로고
    • A tale of tails: How histone tails mediate chromatin compaction in different salt and linker histone environments
    • Arya, G. & Schlick, T. A tale of tails: how histone tails mediate chromatin compaction in different salt and linker histone environments. J. Phys. Chem. A 113, 4045-4059 (2009).
    • (2009) J. Phys. Chem. A , vol.113 , pp. 4045-4059
    • Arya, G.1    Schlick, T.2
  • 40
    • 67650531111 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen uses two distinct modes to move along DNA
    • Kochaniak, A. B. et al. Proliferating cell nuclear antigen uses two distinct modes to move along DNA. J. Biol. Chem. 284, 17700-17710 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17700-17710
    • Kochaniak, A.B.1
  • 41
    • 53149086698 scopus 로고    scopus 로고
    • Motion of a DNA sliding clamp observed by single molecule fluorescence spectroscopy
    • Laurence, T. A. et al. Motion of a DNA sliding clamp observed by single molecule fluorescence spectroscopy. J. Biol. Chem. 283, 22895-22906 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 22895-22906
    • Laurence, T.A.1
  • 42
    • 0034753799 scopus 로고    scopus 로고
    • Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor
    • Randell, J. C. & Coen, D. M. Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor. Mol. Cell 8, 911-920 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 911-920
    • Randell, J.C.1    Coen, D.M.2
  • 43
    • 84875223664 scopus 로고    scopus 로고
    • Small molecule inhibitors of PCNA/PIP-box interaction suppress translesion DNA synthesis
    • Actis, M. et al. Small molecule inhibitors of PCNA/PIP-box interaction suppress translesion DNA synthesis. Bioorg. Med. Chem. 21, 1972-1977 (2013).
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 1972-1977
    • Actis, M.1
  • 44
    • 84859965553 scopus 로고    scopus 로고
    • Identification of small molecule proliferating cell nuclear antigen (PCNA) inhibitor that disrupts interactions with PIP-box proteins and inhibits DNA replication
    • Punchihewa, C. et al. Identification of small molecule proliferating cell nuclear antigen (PCNA) inhibitor that disrupts interactions with PIP-box proteins and inhibits DNA replication. J. Biol. Chem. 287, 14289-14300 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 14289-14300
    • Punchihewa, C.1
  • 45
    • 79951996226 scopus 로고    scopus 로고
    • Reduced stability and increased dynamics in the human proliferating cell nuclear antigen (PCNA) relative to the yeast homolog
    • De Biasio, A. et al. Reduced stability and increased dynamics in the human proliferating cell nuclear antigen (PCNA) relative to the yeast homolog. PLoS ONE 6, e16600 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e16600
    • De Biasio, A.1
  • 46
    • 0029364052 scopus 로고
    • 15N chemical shift referencing in biomolecular NMR
    • 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6, 135-140 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 135-140
    • Wishart, D.S.1
  • 47
    • 77649273247 scopus 로고    scopus 로고
    • The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin
    • Palacios, A. et al. The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin. J. Mol. Biol. 396, 1117-1127 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 1117-1127
    • Palacios, A.1
  • 48
    • 47049087662 scopus 로고    scopus 로고
    • Molecular basis of histone H3K4me3 recognition by ING4
    • Palacios, A. et al. Molecular basis of histone H3K4me3 recognition by ING4. J. Biol. Chem. 283, 15956-15964 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 15956-15964
    • Palacios, A.1
  • 50
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 52
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 53
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 54
    • 28044458515 scopus 로고    scopus 로고
    • A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering
    • Bernadó, P. et al. A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proc. Natl Acad. Sci. USA 102, 17002-17007 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17002-17007
    • Bernadó, P.1
  • 55
    • 1842788912 scopus 로고    scopus 로고
    • Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins
    • Eyal, E., Najmanovich, R., McConkey, B. J., Edelman, M. & Sobolev, V. Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins. J. Comput. Chem. 25, 712-724 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 712-724
    • Eyal, E.1    Najmanovich, R.2    McConkey, B.J.3    Edelman, M.4    Sobolev, V.5
  • 56
    • 33746285812 scopus 로고    scopus 로고
    • Information-driven protein-DNA docking using HADDOCK: It is a matter of flexibility
    • van Dijk, M., van Dijk, A. D., Hsu, V., Boelens, R. & Bonvin, A. M. Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility. Nucleic Acids Res. 34, 3317-3325 (2006).
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3317-3325
    • Van Dijk, M.1    Van Dijk, A.D.2    Hsu, V.3    Boelens, R.4    Bonvin, A.M.5
  • 57
    • 0027981476 scopus 로고
    • Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase delta holoenzyme
    • Flores-Rozas, H. et al. Cdk-interacting protein 1 directly binds with proliferating cell nuclear antigen and inhibits DNA replication catalyzed by the DNA polymerase delta holoenzyme. Proc. Natl Acad. Sci. USA 91, 8655-8659 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8655-8659
    • Flores-Rozas, H.1
  • 58
    • 5144235316 scopus 로고    scopus 로고
    • XMIPP: A new generation of an open-source image processing package for electron microscopy
    • Sorzano, C. O. et al. XMIPP: a new generation of an open-source image processing package for electron microscopy. J. Struct. Biol. 148, 194-204 (2004).
    • (2004) J. Struct. Biol. , vol.148 , pp. 194-204
    • Sorzano, C.O.1
  • 59
    • 0035783286 scopus 로고    scopus 로고
    • A novel neural network technique for analysis and classification of EM single-particle images
    • Pascual-Montano, A. et al. A novel neural network technique for analysis and classification of EM single-particle images. J. Struct. Biol. 133, 233-245 (2001).
    • (2001) J. Struct. Biol. , vol.133 , pp. 233-245
    • Pascual-Montano, A.1


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