메뉴 건너뛰기




Volumn 397, Issue 1, 2010, Pages 13-30

Molecular Analyses of an Unusual Translesion DNA Polymerase from Methanosarcina acetivorans C2A

Author keywords

Archaea; DinB; family Y polymerase; PCNA; translesion DNA synthesis

Indexed keywords

CYCLINE; DNA POLYMERASE; DNA POLYMERASE IV; REPLICATION FACTOR C; UNCLASSIFIED DRUG;

EID: 77249113717     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.007     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 0034720286 scopus 로고    scopus 로고
    • Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis
    • Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R., and Goodman M.F. Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis. Nature 404 (2000) 1014-1018
    • (2000) Nature , vol.404 , pp. 1014-1018
    • Tang, M.1    Pham, P.2    Shen, X.3    Taylor, J.S.4    O'Donnell, M.5    Woodgate, R.6    Goodman, M.F.7
  • 2
    • 24944543952 scopus 로고    scopus 로고
    • A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously
    • Indiani C., McInerney P., Georgescu R., Goodman M.F., and O'Donnell M. A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously. Mol. Cell 19 (2005) 805-815
    • (2005) Mol. Cell , vol.19 , pp. 805-815
    • Indiani, C.1    McInerney, P.2    Georgescu, R.3    Goodman, M.F.4    O'Donnell, M.5
  • 3
    • 24644443795 scopus 로고    scopus 로고
    • Distinct mechanisms of cis-syn thymine dimer bypass by Dpo4 and DNA polymerase eta
    • Johnson R.E., Prakash L., and Prakash S. Distinct mechanisms of cis-syn thymine dimer bypass by Dpo4 and DNA polymerase eta. Proc. Natl Acad. Sci. USA 102 (2005) 12359-12364
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12359-12364
    • Johnson, R.E.1    Prakash, L.2    Prakash, S.3
  • 7
    • 0033588043 scopus 로고    scopus 로고
    • Novel DNA polymerases offer clues to the molecular basis of mutagenesis
    • Friedberg E.C., and Gerlach V.L. Novel DNA polymerases offer clues to the molecular basis of mutagenesis. Cell 98 (1999) 413-416
    • (1999) Cell , vol.98 , pp. 413-416
    • Friedberg, E.C.1    Gerlach, V.L.2
  • 8
    • 9144264274 scopus 로고    scopus 로고
    • Defining the position of the switches between replicative and bypass DNA polymerases
    • Fujii S., and Fuchs R.P. Defining the position of the switches between replicative and bypass DNA polymerases. EMBO J. 23 (2004) 4342-4352
    • (2004) EMBO J. , vol.23 , pp. 4342-4352
    • Fujii, S.1    Fuchs, R.P.2
  • 9
    • 0035861667 scopus 로고    scopus 로고
    • Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C
    • Gruz P., Pisani F.M., Shimizu M., Yamada M., Hayashi I., Morikawa K., and Nohmi T. Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C. J. Biol. Chem. 276 (2001) 47394-47401
    • (2001) J. Biol. Chem. , vol.276 , pp. 47394-47401
    • Gruz, P.1    Pisani, F.M.2    Shimizu, M.3    Yamada, M.4    Hayashi, I.5    Morikawa, K.6    Nohmi, T.7
  • 10
    • 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., and 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
    • 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., and 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
  • 12
    • 0037019606 scopus 로고    scopus 로고
    • Pivotal role of the beta-clamp in translesion DNA synthesis and mutagenesis in E. coli cells
    • Becherel O.J., Fuchs R.P., and Wagner J. Pivotal role of the beta-clamp in translesion DNA synthesis and mutagenesis in E. coli cells. DNA Repair (Amst.) 1 (2002) 703-708
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 703-708
    • Becherel, O.J.1    Fuchs, R.P.2    Wagner, J.3
  • 13
    • 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., and 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
  • 14
    • 34248399044 scopus 로고    scopus 로고
    • New functions for Y family polymerases
    • Lehmann A.R. New functions for Y family polymerases. Mol. Cell 24 (2006) 493-495
    • (2006) Mol. Cell , vol.24 , pp. 493-495
    • Lehmann, A.R.1
  • 15
    • 34147135142 scopus 로고    scopus 로고
    • Proficient and accurate bypass of persistent DNA lesions by DinB DNA polymerases
    • Jarosz D.F., Godoy V.G., and Walker G.C. Proficient and accurate bypass of persistent DNA lesions by DinB DNA polymerases. Cell Cycle 6 (2007) 817-822
    • (2007) Cell Cycle , vol.6 , pp. 817-822
    • Jarosz, D.F.1    Godoy, V.G.2    Walker, G.C.3
  • 16
    • 0034596992 scopus 로고    scopus 로고
    • Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota
    • Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., and Woodgate R. Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota. EMBO J. 19 (2000) 5259-5266
    • (2000) EMBO J. , vol.19 , pp. 5259-5266
    • Tissier, A.1    Frank, E.G.2    McDonald, J.P.3    Iwai, S.4    Hanaoka, F.5    Woodgate, R.6
  • 17
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., and Hinkle D.C. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382 (1996) 729-731
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 18
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication
    • Ling H., Boudsocq F., Woodgate R., and Yang W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell 107 (2001) 91-102
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 19
    • 1642382214 scopus 로고    scopus 로고
    • Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts
    • Ling H., Boudsocq F., Woodgate R., and Yang W. Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts. Mol. Cell 13 (2004) 751-762
    • (2004) Mol. Cell , vol.13 , pp. 751-762
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 20
    • 33644872630 scopus 로고    scopus 로고
    • Novel thermostable Y-family polymerases: applications for the PCR amplification of damaged or ancient DNAs
    • McDonald J.P., Hall A., Gasparutto D., Cadet J., Ballantyne J., and Woodgate R. Novel thermostable Y-family polymerases: applications for the PCR amplification of damaged or ancient DNAs. Nucleic Acids Res. 34 (2006) 1102-1111
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1102-1111
    • McDonald, J.P.1    Hall, A.2    Gasparutto, D.3    Cadet, J.4    Ballantyne, J.5    Woodgate, R.6
  • 21
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta
    • Boudsocq F., Iwai S., Hanaoka F., and Woodgate R. Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta. Nucleic Acids Res. 29 (2001) 4607-4616
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4607-4616
    • Boudsocq, F.1    Iwai, S.2    Hanaoka, F.3    Woodgate, R.4
  • 23
    • 0032745320 scopus 로고    scopus 로고
    • Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea
    • Cann I.K., Ishino S., Hayashi I., Komori K., Toh H., Morikawa K., and Ishino Y. Functional interactions of a homolog of proliferating cell nuclear antigen with DNA polymerases in Archaea. J. Bacteriol. 181 (1999) 6591-6599
    • (1999) J. Bacteriol. , vol.181 , pp. 6591-6599
    • Cann, I.K.1    Ishino, S.2    Hayashi, I.3    Komori, K.4    Toh, H.5    Morikawa, K.6    Ishino, Y.7
  • 24
    • 0032564361 scopus 로고    scopus 로고
    • A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase
    • Cann I.K., Komori K., Toh H., Kanai S., and Ishino Y. A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase. Proc. Natl Acad. Sci. USA 95 (1998) 14250-14255
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14250-14255
    • Cann, I.K.1    Komori, K.2    Toh, H.3    Kanai, S.4    Ishino, Y.5
  • 25
    • 0032814005 scopus 로고    scopus 로고
    • Archaeal DNA replication: identifying the pieces to solve a puzzle
    • Cann I.K., and Ishino Y. Archaeal DNA replication: identifying the pieces to solve a puzzle. Genetics 152 (1999) 1249-1267
    • (1999) Genetics , vol.152 , pp. 1249-1267
    • Cann, I.K.1    Ishino, Y.2
  • 26
    • 39149118031 scopus 로고    scopus 로고
    • Mesophilic Crenarchaeota: proposal for a third archaeal phylum, the Thaumarchaeota
    • Brochier-Armanet C., Boussau B., Gribaldo S., and Forterre P. Mesophilic Crenarchaeota: proposal for a third archaeal phylum, the Thaumarchaeota. Nat. Rev. Microbiol. 6 (2008) 245-252
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 245-252
    • Brochier-Armanet, C.1    Boussau, B.2    Gribaldo, S.3    Forterre, P.4
  • 27
    • 33748743530 scopus 로고    scopus 로고
    • Insights into extreme thermoacidophily based on genome analysis of Picrophilus torridus and other thermoacidophilic archaea
    • Angelov A., and Liebl W. Insights into extreme thermoacidophily based on genome analysis of Picrophilus torridus and other thermoacidophilic archaea. J. Biotechnol. 126 (2006) 3-10
    • (2006) J. Biotechnol. , vol.126 , pp. 3-10
    • Angelov, A.1    Liebl, W.2
  • 28
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou B.L., Pata J.D., and Steitz T.A. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol. Cell 8 (2001) 427-437
    • (2001) Mol. Cell , vol.8 , pp. 427-437
    • Zhou, B.L.1    Pata, J.D.2    Steitz, T.A.3
  • 29
    • 0032031972 scopus 로고    scopus 로고
    • PCNA binding through a conserved motif
    • Warbrick E. PCNA binding through a conserved motif. BioEssays 20 (1998) 195-199
    • (1998) BioEssays , vol.20 , pp. 195-199
    • Warbrick, E.1
  • 30
    • 29644432041 scopus 로고    scopus 로고
    • Biochemical and mutational analyses of a unique clamp loader complex in the archaeon Methanosarcina acetivorans
    • Chen Y.H., Kocherginskaya S.A., Lin Y., Sriratana B., Lagunas A.M., Robbins J.B., et al. Biochemical and mutational analyses of a unique clamp loader complex in the archaeon Methanosarcina acetivorans. J. Biol. Chem. 280 (2005) 41852-41863
    • (2005) J. Biol. Chem. , vol.280 , pp. 41852-41863
    • Chen, Y.H.1    Kocherginskaya, S.A.2    Lin, Y.3    Sriratana, B.4    Lagunas, A.M.5    Robbins, J.B.6
  • 31
    • 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., and 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
  • 32
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity
    • Hosfield D.J., Mol C.D., Shen B., and Tainer J.A. Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell 95 (1998) 135-146
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 33
    • 40549087271 scopus 로고    scopus 로고
    • On the mechanism of loading the PCNA sliding clamp by RFC
    • Dionne I., Brown N.J., Woodgate R., and Bell S.D. On the mechanism of loading the PCNA sliding clamp by RFC. Mol. Microbiol. 68 (2008) 216-222
    • (2008) Mol. Microbiol. , vol.68 , pp. 216-222
    • Dionne, I.1    Brown, N.J.2    Woodgate, R.3    Bell, S.D.4
  • 34
    • 0037008746 scopus 로고    scopus 로고
    • The mutational specificity of the Dbh lesion bypass polymerase and its implications
    • Potapova O., Grindley N.D., and Joyce C.M. The mutational specificity of the Dbh lesion bypass polymerase and its implications. J. Biol. Chem. 277 (2002) 28157-28166
    • (2002) J. Biol. Chem. , vol.277 , pp. 28157-28166
    • Potapova, O.1    Grindley, N.D.2    Joyce, C.M.3
  • 35
    • 0026111317 scopus 로고
    • The 'A rule' of mutagen specificity: a consequence of DNA polymerase bypass of non-instructional lesions?
    • Strauss B.S. The 'A rule' of mutagen specificity: a consequence of DNA polymerase bypass of non-instructional lesions?. BioEssays 13 (1991) 79-84
    • (1991) BioEssays , vol.13 , pp. 79-84
    • Strauss, B.S.1
  • 36
    • 2242420935 scopus 로고    scopus 로고
    • Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis
    • Maga G., Villani G., Ramadan K., Shevelev I., Tanguy Le Gac N., Blanco L., et al. Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis. J. Biol. Chem. 277 (2002) 48434-48440
    • (2002) J. Biol. Chem. , vol.277 , pp. 48434-48440
    • Maga, G.1    Villani, G.2    Ramadan, K.3    Shevelev, I.4    Tanguy Le Gac, N.5    Blanco, L.6
  • 39
    • 12844271626 scopus 로고    scopus 로고
    • A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis
    • Haracska L., Acharya N., Unk I., Johnson R.E., Hurwitz J., Prakash L., and Prakash S. A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis. Mol. Cell. Biol. 25 (2005) 1183-1190
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1183-1190
    • Haracska, L.1    Acharya, N.2    Unk, I.3    Johnson, R.E.4    Hurwitz, J.5    Prakash, L.6    Prakash, S.7
  • 40
    • 1342346599 scopus 로고    scopus 로고
    • Functional analysis of multiple single-stranded DNA-binding proteins from Methanosarcina acetivorans and their effects on DNA synthesis by DNA polymerase BI
    • Robbins J.B., Murphy M.C., White B.A., Mackie R.I., Ha T., and Cann I.K. Functional analysis of multiple single-stranded DNA-binding proteins from Methanosarcina acetivorans and their effects on DNA synthesis by DNA polymerase BI. J. Biol. Chem. 279 (2004) 6315-6326
    • (2004) J. Biol. Chem. , vol.279 , pp. 6315-6326
    • Robbins, J.B.1    Murphy, M.C.2    White, B.A.3    Mackie, R.I.4    Ha, T.5    Cann, I.K.6
  • 41
    • 19944424477 scopus 로고    scopus 로고
    • Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A
    • Pritchett M.A., and Metcalf W.W. Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A. Mol. Microbiol. 56 (2005) 1183-1194
    • (2005) Mol. Microbiol. , vol.56 , pp. 1183-1194
    • Pritchett, M.A.1    Metcalf, W.W.2
  • 42
    • 57449120302 scopus 로고    scopus 로고
    • New method for tightly regulated gene expression and highly efficient chromosomal integration of cloned genes for Methanosarcina species
    • Guss A.M., Rother M., Zhang J.K., Kulkarni G., and Metcalf W.W. New method for tightly regulated gene expression and highly efficient chromosomal integration of cloned genes for Methanosarcina species. Archaea 2 (2008) 193-203
    • (2008) Archaea , vol.2 , pp. 193-203
    • Guss, A.M.1    Rother, M.2    Zhang, J.K.3    Kulkarni, G.4    Metcalf, W.W.5
  • 43
    • 33749022503 scopus 로고    scopus 로고
    • Methanosarcina acetivorans flap endonuclease 1 activity is inhibited by a cognate single-stranded-DNA-binding protein
    • Lin Y., Guzman C.E., McKinney M.C., Nair S.K., Ha T., and Cann I.K. Methanosarcina acetivorans flap endonuclease 1 activity is inhibited by a cognate single-stranded-DNA-binding protein. J. Bacteriol. 188 (2006) 6153-6167
    • (2006) J. Bacteriol. , vol.188 , pp. 6153-6167
    • Lin, Y.1    Guzman, C.E.2    McKinney, M.C.3    Nair, S.K.4    Ha, T.5    Cann, I.K.6
  • 45
    • 0025667322 scopus 로고
    • Synthesis and characterization of a substrate for T4 endonuclease V containing a phosphorodithioate linkage at the thymine dimer site
    • Murata T., Iwai S., and Ohtsuka E. Synthesis and characterization of a substrate for T4 endonuclease V containing a phosphorodithioate linkage at the thymine dimer site. Nucleic Acids Res. 18 (1990) 7279-7286
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7279-7286
    • Murata, T.1    Iwai, S.2    Ohtsuka, E.3
  • 46
    • 0029777391 scopus 로고    scopus 로고
    • Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides
    • Iwai S., Shimizu M., Kamiya H., and Ohtsuka E. Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides. J. Am. Chem. Soc. 118 (1996) 7642-7643
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7642-7643
    • Iwai, S.1    Shimizu, M.2    Kamiya, H.3    Ohtsuka, E.4
  • 47
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara Y., Masutani C., Mizukoshi T., Kondo J., Hanaoka F., and Iwai S. Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J. Biol. Chem. 274 (1999) 20027-20033
    • (1999) J. Biol. Chem. , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 48
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., and Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 (1985) 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 50
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 51
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: an on-line retrieval system for biological sequence banks
    • Perriere G., and Gouy M. WWW-query: an on-line retrieval system for biological sequence banks. Biochimie 78 (1996) 364-369
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perriere, G.1    Gouy, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.