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Volumn 335, Issue 5, 2004, Pages 1187-1197

Structural and Biochemical Analysis of Sliding Clamp/Ligand Interactions Suggest a Competition between Replicative and Translesion DNA Polymerases

Author keywords

DNA polymerase IV; Peptide inhibition; Processivity factors; Sliding clamp; Translesion synthesis

Indexed keywords

DNA POLYMERASE; PEPTIDE DERIVATIVE; PEPTIDE P16; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 0346654081     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.049     Document Type: Article
Times cited : (87)

References (55)
  • 2
    • 0034705095 scopus 로고    scopus 로고
    • The many faces of DNA polymerases: Strategies for mutagenesis and for mutational avoidance
    • Friedberg E.C., Feaver W.J., Gerlach V.L. The many faces of DNA polymerases: strategies for mutagenesis and for mutational avoidance. Proc. Natl Acad. Sci. USA. 97:2000;5681-5683.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5681-5683
    • Friedberg, E.C.1    Feaver, W.J.2    Gerlach, V.L.3
  • 3
    • 0037205001 scopus 로고    scopus 로고
    • Specialized DNA polymerases, cellular survival, and the genesis of mutations
    • Friedberg E., Wagner R., Radman M. Specialized DNA polymerases, cellular survival, and the genesis of mutations. Science. 296:2002;1627-1630.
    • (2002) Science , vol.296 , pp. 1627-1630
    • Friedberg, E.1    Wagner, R.2    Radman, M.3
  • 4
    • 0032703301 scopus 로고    scopus 로고
    • Replication of damaged DNA: Molecular defect in xeroderma pigmentosum variant cells
    • Cordonnier A.M., Fuchs R.P. Replication of damaged DNA: molecular defect in xeroderma pigmentosum variant cells. Mutat. Res. 435:1999;111-119.
    • (1999) Mutat. Res. , vol.435 , pp. 111-119
    • Cordonnier, A.M.1    Fuchs, R.P.2
  • 5
    • 0037115955 scopus 로고    scopus 로고
    • How DNA lesions are turned into mutations within cells?
    • Pagès V., Fuchs R.P. How DNA lesions are turned into mutations within cells? Oncogene. 21:2002;8957-8966.
    • (2002) Oncogene , vol.21 , pp. 8957-8966
    • Pagès, V.1    Fuchs, R.P.2
  • 6
    • 0347079244 scopus 로고    scopus 로고
    • Pivotal role of the β-clamp in translesion DNA synthesis and mutagenesis in E. coli cells
    • Becherel O., Fuchs R.P.P., Wagner J. Pivotal role of the β-clamp in translesion DNA synthesis and mutagenesis in E. coli cells. DNA Repair. 68:2002;1-6.
    • (2002) DNA Repair , vol.68 , pp. 1-6
    • Becherel, O.1    Fuchs, R.P.P.2    Wagner, J.3
  • 9
    • 0034852569 scopus 로고    scopus 로고
    • Interaction with PCNA is essential for yeast DNA polymerase eta function
    • Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Interaction with PCNA is essential for yeast DNA polymerase eta function. Mol. Cell. 8:2001;407-415.
    • (2001) Mol. Cell , vol.8 , pp. 407-415
    • Haracska, L.1    Kondratick, C.M.2    Unk, I.3    Prakash, S.4    Prakash, L.5
  • 11
    • 0036171550 scopus 로고    scopus 로고
    • The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo
    • Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P. The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo. EMBO Rep. 3:2002;45-49.
    • (2002) EMBO Rep. , vol.3 , pp. 45-49
    • Lenne-Samuel, N.1    Wagner, J.2    Etienne, H.3    Fuchs, R.P.4
  • 12
    • 0035949599 scopus 로고    scopus 로고
    • A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems
    • Dalrymple B.P., Kongsuwan K., Wijffels G., Dixon N.E., Jennings P.A. A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems. Proc. Natl Acad. Sci. USA. 98:2001;11627-11632.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11627-11632
    • Dalrymple, B.P.1    Kongsuwan, K.2    Wijffels, G.3    Dixon, N.E.4    Jennings, P.A.5
  • 13
    • 0034574554 scopus 로고    scopus 로고
    • The beta clamp targets DNA polymerase IV to DNA and strongly increases its processivity
    • Wagner J., Fujii S., Gruz P., Nohmi T., Fuchs R.P. The beta clamp targets DNA polymerase IV to DNA and strongly increases its processivity. EMBO Rep. 1:2000;484-488.
    • (2000) EMBO Rep. , vol.1 , pp. 484-488
    • Wagner, J.1    Fujii, S.2    Gruz, P.3    Nohmi, T.4    Fuchs, R.P.5
  • 14
    • 0035110865 scopus 로고    scopus 로고
    • The ring-type polymerase sliding clamp family
    • Bruck I., O'Donnell M. The ring-type polymerase sliding clamp family. Genome Biol. 2:2001;3001.1-3001.3.
    • (2001) Genome Biol. , vol.2 , pp. 30011-30013
    • Bruck, I.1    O'Donnell, M.2
  • 15
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp
    • Ason B., Handayani R., Williams C.R., Bertram J.G., Hingorani M.M., O'Donnell M., et al. Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp. J. Biol. Chem. 278:2003;10033-10040.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10033-10040
    • Ason, B.1    Handayani, R.2    Williams, C.R.3    Bertram, J.G.4    Hingorani, M.M.5    O'Donnell, M.6
  • 16
    • 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. 87:1996;297-306.
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 17
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong X.P., Onrust R., O'Donnell M., Kuriyan J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell. 69:1992;425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 18
    • 0347709578 scopus 로고    scopus 로고
    • Towards an understanding of protein-protein interaction network hierarchies. Analysis of DnaN (β)-binding peptide motifs in members of protein families interacting with the eubacterial processivity clamp, the β subunit of DNA polymerase III
    • Australian Computer Society, Inc., Darlinghurst, Australia
    • Dalrymple, B. P., Wijffels, G., Kongsuwan, K. Jennings, P. A. (2003). Towards an understanding of protein-protein interaction network hierarchies. Analysis of DnaN (β)-binding peptide motifs in members of protein families interacting with the eubacterial processivity clamp, the β subunit of DNA polymerase III. In Conferences in Research and Practice in Information Technology Series, vol. 19, pp. 153-162, Australian Computer Society, Inc., Darlinghurst, Australia.
    • (2003) Conferences in Research and Practice in Information Technology Series , vol.19 , pp. 153-162
    • Dalrymple, B.P.1    Wijffels, G.2    Kongsuwan, K.3    Jennings, P.A.4
  • 19
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga G., Hübscher U. Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci. 116:2003;3051-3060.
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hübscher, U.2
  • 20
    • 0034669125 scopus 로고    scopus 로고
    • All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis
    • Napolitano R., Janel-Bintz R., Wagner J., Fuchs R.P. All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis. EMBO J. 19:2000;6259-6265.
    • (2000) EMBO J. , vol.19 , pp. 6259-6265
    • Napolitano, R.1    Janel-Bintz, R.2    Wagner, J.3    Fuchs, R.P.4
  • 21
    • 0035902484 scopus 로고    scopus 로고
    • Mechanism of DNA polymerase II-mediated frameshift mutagenesis
    • Becherel O.J., Fuchs R.P. Mechanism of DNA polymerase II-mediated frameshift mutagenesis. Proc. Natl Acad. Sci. USA. 98:2001;8566-8571.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8566-8571
    • Becherel, O.J.1    Fuchs, R.P.2
  • 22
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • Wagner J., Gruz P., Kim S.R., Yamada M., Matsui K., Fuchs R.P., Nohmi T. The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis. Mol. Cell. 4:1999;281-286.
    • (1999) Mol. Cell , vol.4 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.R.3    Yamada, M.4    Matsui, K.5    Fuchs, R.P.6    Nohmi, T.7
  • 24
    • 0033527533 scopus 로고    scopus 로고
    • The mutagenesis protein UmuC is a DNA polymerase activated by UmuD', RecA, and SSB and is specialized for translesion replication
    • Reuven N.B., Arad G., Maor-Shoshani A., Livneh Z. The mutagenesis protein UmuC is a DNA polymerase activated by UmuD', RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274:1999;31763-31766.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31763-31766
    • Reuven, N.B.1    Arad, G.2    Maor-Shoshani, A.3    Livneh, Z.4
  • 25
    • 0024244830 scopus 로고
    • Purification and characterization of an inducible Escherichia coli DNA polymerase capable of insertion and bypass at abasic lesions in DNA
    • Bonner C.A., Randall S.K., Rayssiguier C., Radman M., Eritja R., Kaplan B.E., et al. Purification and characterization of an inducible Escherichia coli DNA polymerase capable of insertion and bypass at abasic lesions in DNA. J. Biol. Chem. 263:1988;18946-18952.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18946-18952
    • Bonner, C.A.1    Randall, S.K.2    Rayssiguier, C.3    Radman, M.4    Eritja, R.5    Kaplan, B.E.6
  • 26
    • 0026725774 scopus 로고
    • Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins
    • Bonner C.A., Stukenberg P.T., Rajagopalan M., Eritja R., O'Donnell M., McEntee K., et al. Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. J. Biol. Chem. 267:1992;11431-11438.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11431-11438
    • Bonner, C.A.1    Stukenberg, P.T.2    Rajagopalan, M.3    Eritja, R.4    O'Donnell, M.5    McEntee, K.6
  • 27
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions
    • Johnson R.E., Washington M.T., Haracska L., Prakash S., Prakash L. Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions. Nature. 406:2000;1015-1019.
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 29
    • 0036012786 scopus 로고    scopus 로고
    • Genetics of mutagenesis in E. coli: Various combinations of translesion polymerases (Pol II, IV and V) deal with lesion/sequence context diversity
    • Wagner J., Etienne H., Janel-Bintz R., Fuchs R.P. Genetics of mutagenesis in E. coli: various combinations of translesion polymerases (Pol II, IV and V) deal with lesion/sequence context diversity. DNA Repair. 1:2002;159-167.
    • (2002) DNA Repair , vol.1 , pp. 159-167
    • Wagner, J.1    Etienne, H.2    Janel-Bintz, R.3    Fuchs, R.P.4
  • 30
    • 0037099578 scopus 로고    scopus 로고
    • Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process
    • Bresson A., Fuchs R.P. Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process. EMBO J. 21:2002;3881-3887.
    • (2002) EMBO J. , vol.21 , pp. 3881-3887
    • Bresson, A.1    Fuchs, R.P.2
  • 31
    • 0037226587 scopus 로고    scopus 로고
    • Yeast DNA polymerase zeta (zeta) is essential for error-free replication past thymine glycol
    • Johnson R.E., Yu S.L., Prakash S., Prakash L. Yeast DNA polymerase zeta (zeta) is essential for error-free replication past thymine glycol. Genes Dev. 17:2003;77-87.
    • (2003) Genes Dev. , vol.17 , pp. 77-87
    • Johnson, R.E.1    Yu, S.L.2    Prakash, S.3    Prakash, L.4
  • 32
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 33
    • 0036734527 scopus 로고    scopus 로고
    • Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus
    • Matsumiya S., Ishino S., Ishino Y., Morikawa K. Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus. Genes Cells. 7:2002;911-922.
    • (2002) Genes Cells , vol.7 , pp. 911-922
    • Matsumiya, S.1    Ishino, S.2    Ishino, Y.3    Morikawa, K.4
  • 34
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi D., Yurieva O., Zhao Y., Young M., Stewart J., Hingorani M., et al. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell. 106:2001;417-428.
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6
  • 35
    • 0030070111 scopus 로고    scopus 로고
    • A molecular switch in a replication machine defined by an internal competition for protein rings
    • Naktinis V., Turner J., O'Donnell M. A molecular switch in a replication machine defined by an internal competition for protein rings. Cell. 84:1996;137-145.
    • (1996) Cell , vol.84 , pp. 137-145
    • Naktinis, V.1    Turner, J.2    O'Donnell, M.3
  • 36
    • 0141959300 scopus 로고    scopus 로고
    • Mechanism of the δ wrench in opening the β sliding clamp
    • Indiani C., O'Donnell M. Mechanism of the δ wrench in opening the β sliding clamp. J. Biol. Chem. 278:2003;40272-40281.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40272-40281
    • Indiani, C.1    O'Donnell, M.2
  • 37
    • 0031892179 scopus 로고    scopus 로고
    • Role of the core DNA polymerase III subunits at the replication fork
    • Marians K.J., Hiasa H., Kim D.R., McHenry C.S. Role of the core DNA polymerase III subunits at the replication fork. J. Biol. Chem. 273:1998;2452-2457.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2452-2457
    • Marians, K.J.1    Hiasa, H.2    Kim, D.R.3    McHenry, C.S.4
  • 38
    • 0029665235 scopus 로고    scopus 로고
    • *, a UV-inducible smaller form of the β subunit sliding clamp of DNA polymerase II of E. coli
    • *, a UV-inducible smaller form of the β subunit sliding clamp of DNA polymerase II of E. coli. J. Biol. Chem. 271:1996;2482-2490.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2482-2490
    • Paz-Elizur, T.1    Skaliter, R.2    Blumenstein, S.3    Livneh, Z.4
  • 39
    • 0029665233 scopus 로고    scopus 로고
    • *, a UV-inducible shorter form of the β subunit of DNA polymerase II of Escherichia coli
    • *, a UV-inducible shorter form of the β subunit of DNA polymerase II of Escherichia coli. J. Biol. Chem. 271:1996;2491-2496.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2491-2496
    • Skaliter, R.1    Bergstein, M.2    Livneh, Z.3
  • 40
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archeon Sulfolobus sulfataricus
    • Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D. A heterotrimeric PCNA in the hyperthermophilic archeon Sulfolobus sulfataricus. Mol. Cell. 11:2003;275-282.
    • (2003) Mol. Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.K.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 41
    • 0025809742 scopus 로고
    • Mechanism of the sliding b clamp of DNA polymerase III holoenzyme
    • Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M. Mechanism of the sliding b clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 266:1991;11328-11334.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    O'Donnell, M.3
  • 43
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Shamoo Y., Steitz T.A. Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell. 99:1999;155-166.
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 44
    • 0042161860 scopus 로고    scopus 로고
    • Evolutionnary clues to DNA ploymerase III β clamp structural mechanisms
    • Neuwald A.F. Evolutionnary clues to DNA ploymerase III β clamp structural mechanisms. Nucl. Acids Res. 31:2003;4503-4516.
    • (2003) Nucl. Acids Res. , vol.31 , pp. 4503-4516
    • Neuwald, A.F.1
  • 45
    • 0038813750 scopus 로고    scopus 로고
    • The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation
    • Yokota A., Tsumoto K., Shiroishi M., Kondo H., Kumagai I. The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. J. Biol. Chem. 278:2003;5410-5418.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5410-5418
    • Yokota, A.1    Tsumoto, K.2    Shiroishi, M.3    Kondo, H.4    Kumagai, I.5
  • 46
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution X-ray crystal structures of human γd cristallin (1.25 Å) and the R58H mutant (1.15 Å) associated with aculeiform cataract
    • Basak A., Bateman O., Slingsby C., Pande A., Asherie N., Ogun O., et al. High-resolution X-ray crystal structures of human γD cristallin (1.25 Å) and the R58H mutant (1.15 Å) associated with aculeiform cataract. J. Mol. Biol. 328:2003;1137-1147.
    • (2003) J. Mol. Biol. , vol.328 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3    Pande, A.4    Asherie, N.5    Ogun, O.6
  • 47
    • 0029163487 scopus 로고
    • Structural and functional similarities of prokaryotic and eukaryotic DNA plymerase sliding clamps
    • Kelman Z., O'Donnell M. Structural and functional similarities of prokaryotic and eukaryotic DNA plymerase sliding clamps. Nucl. Acids Res. 23:1995;3613-3620.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 3613-3620
    • Kelman, Z.1    O'Donnell, M.2
  • 48
    • 0031038379 scopus 로고    scopus 로고
    • Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen
    • Mossi R., Jonsson Z., Allen B., Hardin S., Hübscher U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J. Biol. Chem. 272:1997;1769-1776.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1769-1776
    • Mossi, R.1    Jonsson, Z.2    Allen, B.3    Hardin, S.4    Hübscher, U.5
  • 49
    • 0022999955 scopus 로고
    • Chemical characterization and purification of the beta subunit of the DNA polymerase III holoenzyme from an overproducing strain
    • Johanson K.O., Haynes T.E., McHenry C.S. Chemical characterization and purification of the beta subunit of the DNA polymerase III holoenzyme from an overproducing strain. J. Biol. Chem. 261:1986;11460-11465.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11460-11465
    • Johanson, K.O.1    Haynes, T.E.2    McHenry, C.S.3
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter, Sweet R.M. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter C.W., Sweet R.M. Methods in Enzymology. vol. 276:1996;307-326 Academic Press, New York.
    • (1996) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 51
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 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
  • 52
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zhou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of 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    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 54
    • 0034255358 scopus 로고    scopus 로고
    • DbClustal: Rapid and reliable global multiple alignments of protein sequences detected by database searches
    • Thompson J.D., Plewniak F., Thierry J.C., Poch O. DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches. Nucl. Acids Res. 28:2000;2919-2926.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2919-2926
    • Thompson, J.D.1    Plewniak, F.2    Thierry, J.C.3    Poch, O.4


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