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Volumn 38, Issue 1, 2009, Pages

Profiling the selectivity of DNA ligases in an array format with mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; TAQ POLYMERASE;

EID: 75649114954     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp827     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 0035526174 scopus 로고    scopus 로고
    • DNA ligases and ligase-based technologies
    • Cao, W. (2001) DNA ligases and ligase-based technologies. Clin. Appl. Immunol. Rev., 2, 33-43.
    • (2001) Clin. Appl. Immunol. Rev. , vol.2 , pp. 33-43
    • Cao, W.1
  • 2
    • 0036301423 scopus 로고    scopus 로고
    • DNA ligases: Structure, function and mechanism
    • Cao, W. (2002) DNA ligases: Structure, function and mechanism. Curr. Org. Chem., 6, 827-839.
    • (2002) Curr. Org. Chem. , vol.6 , pp. 827-839
    • Cao, W.1
  • 4
    • 0033080784 scopus 로고    scopus 로고
    • Biochemical properties of a high fidelity DNA ligase from thermus species AK16D
    • Tong, J., Cao, W. and Barany, F. (1999) Biochemical properties of a high fidelity DNA ligase from thermus species AK16D. Nucleic Acids Res., 27, 788-794.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 788-794
    • Tong, J.1    Cao, W.2    Barany, F.3
  • 5
    • 0016273515 scopus 로고
    • DNA ligase: structure, mechanism, and function
    • Lehman, I.R. (1974) DNA ligase: structure, mechanism, and function. Science, 186, 790-797.
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 6
    • 33747177904 scopus 로고    scopus 로고
    • Direct comparison of nick-joining activity of the nucleic acid ligases from bacteriophage T4
    • Bullard, D.R. and Bowater, R.P. (2006) Direct comparison of nick-joining activity of the nucleic acid ligases from bacteriophage T4. Biochem. J., 398, 135-144.
    • (2006) Biochem. J. , vol.398 , pp. 135-144
    • Bullard, D.R.1    Bowater, R.P.2
  • 7
    • 0024559478 scopus 로고
    • Specificity of the nick-closing activity of bacteriophage T4 DNA ligase
    • Wu, D.Y. and Wallace, R.B. (1989) Specificity of the nick-closing activity of bacteriophage T4 DNA ligase. Gene, 76, 245-254.
    • (1989) Gene. , vol.76 , pp. 245-254
    • Wu, D.Y.1    Wallace, R.B.2
  • 8
    • 0032518177 scopus 로고    scopus 로고
    • Chlorella virus DNA ligase: nick recognition and mutational analysis
    • Sriskanda, V. and Shuman, S. (1998) Chlorella virus DNA ligase: nick recognition and mutational analysis. Nucleic Acids Res., 26, 525-531.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 525-531
    • Sriskanda, V.1    Shuman, S.2
  • 9
    • 0026661136 scopus 로고
    • Molecular characterization of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases
    • Kletzin, A. (1992) Molecular characterization of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases. Nucleic Acids Res., 20, 5389-5396.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5389-5396
    • Kletzin, A.1
  • 10
    • 0030816328 scopus 로고    scopus 로고
    • Two distinct DNA ligase activities in mitotic extracts of the yeast Saccharomyces cerevisiae
    • Ramos, W., Tappe, N., Talamantez, J., Friedberg, E.C. and Tomkinson, A.E. (1997) Two distinct DNA ligase activities in mitotic extracts of the yeast Saccharomyces cerevisiae. Nucleic Acids Res., 25, 1485-1492.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1485-1492
    • Ramos, W.1    Tappe, N.2    Talamantez, J.3    Friedberg, E.C.4    Tomkinson, A.E.5
  • 11
    • 0033569841 scopus 로고    scopus 로고
    • Delayed DNA joining at 3' mismatches by human DNA ligases
    • Bhagwat, A.S., Sanderson, R.J. and Lindahl, T. (1999) Delayed DNA joining at 3' mismatches by human DNA ligases. Nucleic Acids Res., 27, 4028-4033.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4028-4033
    • Bhagwat, A.S.1    Sanderson, R.J.2    Lindahl, T.3
  • 13
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophase T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996) Crystal structure of an ATP-dependent DNA ligase from bacteriophase T7. Cell, 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 15
    • 67650538051 scopus 로고    scopus 로고
    • DNA ligases: progress and prospects
    • Shuman, S. (2009) DNA ligases: progress and prospects. J. Biol. Chem., 284, 17365-17369.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17365-17369
    • Shuman, S.1
  • 16
    • 33749433610 scopus 로고    scopus 로고
    • Immobilized DNA hairpins for assay of sequential breaking and joining of DNA backbones
    • Scott, B.O.S., Lavesa-Curto, M., Bullard, D.R., Butt, J.N. and Bowater, R.P. (2006) Immobilized DNA hairpins for assay of sequential breaking and joining of DNA backbones. Anal. Biochem., 358, 90-98.
    • (2006) Anal. Biochem. , vol.358 , pp. 90-98
    • Scott, B.O.S.1    Lavesa-Curto, M.2    Bullard, D.R.3    Butt, J.N.4    Bowater, R.P.5
  • 17
    • 9144226894 scopus 로고    scopus 로고
    • Staphylococcus aureus DNA ligase: characterization of its kinetics of catalysis and development of a high-throughput screening compatible chemiluminescent hybridization protection assay
    • Gul, S., Brown, R., May, E., Mazzulla, M., Smyth, M.G., Berry, C., Morby, A. and Powell, D.J. (2004) Staphylococcus aureus DNA ligase: characterization of its kinetics of catalysis and development of a high-throughput screening compatible chemiluminescent hybridization protection assay. Biochem. J., 383, 551-559.
    • (2004) Biochem. J. , vol.383 , pp. 551-559
    • Gul, S.1    Brown, R.2    May, E.3    Mazzulla, M.4    Smyth, M.G.5    Berry, C.6    Morby, A.7    Powell, D.J.8
  • 18
    • 0038243876 scopus 로고    scopus 로고
    • Genotyping single nucleotide polymorphisms by mass spectrometry
    • Tost, J. and Gut, I.G. (2002) Genotyping single nucleotide polymorphisms by mass spectrometry. Mass Spectrom. Rev., 21, 388-418.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 388-418
    • Tost, J.1    Gut, I.G.2
  • 21
    • 35648937679 scopus 로고    scopus 로고
    • Genomic profiling of CpG methylation and allelic specificity using quantitative high-throughput mass spectrometry: critical evaluation and improvements
    • Coolen, M.W., Statham, A.L., Gardiner-Garden, M. and Clark, S.J. (2007) Genomic profiling of CpG methylation and allelic specificity using quantitative high-throughput mass spectrometry: critical evaluation and improvements. Nucleic Acids Res., 35, e119.
    • (2007) Nucleic Acids Res. , vol.35
    • Coolen, M.W.1    Statham, A.L.2    Gardiner-Garden, M.3    Clark, S.J.4
  • 22
    • 0348202422 scopus 로고    scopus 로고
    • Analysis and accurate analysis of CpG methylation by MALDI mass spectrometry
    • Tost, J., Schatz, P., Schuster, M., Berlin, K. and Gut, I.G. (2003) Analysis and accurate analysis of CpG methylation by MALDI mass spectrometry. Nucleic Acids Res., 31, e50.
    • (2003) Nucleic Acids Res. , vol.31
    • Tost, J.1    Schatz, P.2    Schuster, M.3    Berlin, K.4    Gut, I.G.5
  • 23
    • 0037379922 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry-based detection of microsatellite instabilities in coding DNA sequences: a novel approach to identify DNA-mismatch repair-deficient cancer cells
    • Bonk, T., Humeny, A., Gebert, J., Sutter, C., von Knebel Doeberitz, M. and Becker, C.-M. (2003) Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry-based detection of microsatellite instabilities in coding DNA sequences: a novel approach to identify DNA-mismatch repair-deficient cancer cells. Clin. Chem., 49, 552-561.
    • (2003) Clin. Chem. , vol.49 , pp. 552-561
    • Bonk, T.1    Humeny, A.2    Gebert, J.3    Sutter, C.4    von Knebel Doeberitz, M.5    Becker, C.-M.6
  • 24
    • 44949156111 scopus 로고    scopus 로고
    • Combining self-assembled monolayers and mass spectrometry for applications in biochips
    • Gurard-Levin, Z.A. and Mrksich, M. (2008) Combining self-assembled monolayers and mass spectrometry for applications in biochips. Annu. Rev. Anal. Chem., 1, 767-800.
    • (2008) Annu. Rev. Anal. Chem. , vol.1 , pp. 767-800
    • Gurard-Levin, Z.A.1    Mrksich, M.2
  • 25
    • 9244243049 scopus 로고    scopus 로고
    • Profiling kinase activities by using a peptide chip and mass spectrometry
    • Min, D., Su, J. and Mrksich, M. (2004) Profiling kinase activities by using a peptide chip and mass spectrometry. Angew. Chem. Int. Ed., 43, 5973-5977.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 5973-5977
    • Min, D.1    Su, J.2    Mrksich, M.3
  • 26
    • 33746263948 scopus 로고    scopus 로고
    • Assays of endogenous caspase activities: a comparison of mass spectrometry and fluorescence formats
    • Su, J., Rajapaksha, T.W., Peter, M.E. and Mrksich, M. (2006) Assays of endogenous caspase activities: a comparison of mass spectrometry and fluorescence formats. Anal. Chem., 78, 4945-4951.
    • (2006) Anal. Chem. , vol.78 , pp. 4945-4951
    • Su, J.1    Rajapaksha, T.W.2    Peter, M.E.3    Mrksich, M.4
  • 27
    • 3242659948 scopus 로고    scopus 로고
    • A method for connecting solution-phase enzyme activity assays with immobilized format analysis by mass spectrometry
    • Min, D., Yeo, W. and Mrksich, M. (2004) A method for connecting solution-phase enzyme activity assays with immobilized format analysis by mass spectrometry. Anal. Chem., 76, 3923-3929.
    • (2004) Anal. Chem. , vol.76 , pp. 3923-3929
    • Min, D.1    Yeo, W.2    Mrksich, M.3
  • 28
    • 0033559562 scopus 로고    scopus 로고
    • The role of ligand density in the enzymatic glycosylation of carbohydrates presented on self-assembled monolayers of alkanethiolates on gold
    • Houseman, B.T. and Mrksich, M. (1999) The role of ligand density in the enzymatic glycosylation of carbohydrates presented on self-assembled monolayers of alkanethiolates on gold. Angew. Chem. Int. Ed., 38, 782-785.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 782-785
    • Houseman, B.T.1    Mrksich, M.2
  • 29
    • 2542627454 scopus 로고    scopus 로고
    • Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor
    • Min, D., Tang, W. and Mrksich, M. (2004) Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nat. Biotechnol., 22, 717-723.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 717-723
    • Min, D.1    Tang, W.2    Mrksich, M.3
  • 30
    • 44649125503 scopus 로고    scopus 로고
    • Biochemical assays of immobilized oligonucleotides with mass spectrometry
    • Tsubery, H. and Mrksich, M. (2008) Biochemical assays of immobilized oligonucleotides with mass spectrometry. Langmuir, 24, 5433-5438.
    • (2008) Langmuir , vol.24 , pp. 5433-5438
    • Tsubery, H.1    Mrksich, M.2
  • 31
    • 0037418506 scopus 로고    scopus 로고
    • Maleimide-functionalized self-assembled monolayers for the preparation of peptide and carbohydrate biochips
    • Houseman, B.T., Gawalt, E.S. and Mrksich, M. (2003) Maleimide-functionalized self-assembled monolayers for the preparation of peptide and carbohydrate biochips. Langmuir, 19, 1522-1531.
    • (2003) Langmuir , vol.19 , pp. 1522-1531
    • Houseman, B.T.1    Gawalt, E.S.2    Mrksich, M.3
  • 32
    • 0030000062 scopus 로고    scopus 로고
    • Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells
    • Mrksich, M. and Whitesides, G.M. (1996) Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells. Annu. Rev. Biophys. Biomol. Struct., 25, 55-78.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 55-78
    • Mrksich, M.1    Whitesides, G.M.2
  • 33
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: a surface engineering approach
    • Houseman, B.T. and Mrksich, M. (2002) Towards quantitative assays with peptide chips: a surface engineering approach. Trends Biotechnol., 20, 279-281.
    • (2002) Trends Biotechnol. , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 34
    • 33646744791 scopus 로고    scopus 로고
    • Surface coverage and structure of mixed DNA/alkylthiol monolayers on gold: Characterization by XPS, NEXAFS, and Fluorescence intensity measurements
    • Lee, C., Gong, P., Harbers, G.M., Grainger, D.W., Castner, D.G. and Gamble, L.J. (2006) Surface coverage and structure of mixed DNA/alkylthiol monolayers on gold: Characterization by XPS, NEXAFS, and Fluorescence intensity measurements. Anal. Chem., 78, 3316-3325.
    • (2006) Anal. Chem. , vol.78 , pp. 3316-3325
    • Lee, C.1    Gong, P.2    Harbers, G.M.3    Grainger, D.W.4    Castner, D.G.5    Gamble, L.J.6
  • 35
    • 0026056970 scopus 로고
    • Genetic disease detection and DNA amplification using cloned thermostable ligase
    • Barany, F. (1991) Genetic disease detection and DNA amplification using cloned thermostable ligase. Proc. Natl Acad. Sci. USA, 88, 189-193.
    • (1991) Proc. Natl Acad. Sci. USA. , vol.88 , pp. 189-193
    • Barany, F.1
  • 36
    • 0017862920 scopus 로고
    • Effect of ATP analogues on T4 polynucleotide ligase
    • Raae, A.J. and Kleppe, K. (1978) Effect of ATP analogues on T4 polynucleotide ligase. Biochem. Biophys. Res. Commun., 81, 24-27.
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 24-27
    • Raae, A.J.1    Kleppe, K.2
  • 37
    • 0025043782 scopus 로고
    • Use of ATP, dATP and their a-thio derivatives to study DNA ligase adenylation
    • Montecucco, A., Lestingi, M., Pedrali-noy, G., Spadari, S. and Ciarrocchi, G. (1990) Use of ATP, dATP and their a-thio derivatives to study DNA ligase adenylation. Biochem. J., 271, 265-268.
    • (1990) Biochem. J. , vol.271 , pp. 265-268
    • Montecucco, A.1    Lestingi, M.2    Pedrali-noy, G.3    Spadari, S.4    Ciarrocchi, G.5
  • 38
    • 0023651476 scopus 로고
    • Nicks 3' or 5' to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase
    • Goffin, C., Bailly, V. and Verly, W.G. (1987) Nicks 3' or 5' to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase. Nucleic Acids Res., 15, 8755-8771.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8755-8771
    • Goffin, C.1    Bailly, V.2    Verly, W.G.3
  • 39
    • 0031054449 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1
    • Ho, C.K., Van Etten, J.L. and Shuman, S. (1997) Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1. J. Virol., 71, 1931-1937.
    • (1997) J. Virol. , vol.71 , pp. 1931-1937
    • Ho, C.K.1    Van Etten, J.L.2    Shuman, S.3
  • 40
    • 0030738222 scopus 로고    scopus 로고
    • Characterization of an ATP-dependent DNA ligase encoded by haemophilus influenzae
    • Cheng, C. and Shuman, S. (1997) Characterization of an ATP-dependent DNA ligase encoded by haemophilus influenzae. Nucleic Acids Res., 25, 1369-1374.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1369-1374
    • Cheng, C.1    Shuman, S.2
  • 41
    • 0028846525 scopus 로고
    • Vaccinia virus DNA ligase: Specificity, fidelity, and inhibition
    • Shuman, S. (1995) Vaccinia virus DNA ligase: Specificity, fidelity, and inhibition. Biochemistry, 34, 16138-16147.
    • (1995) Biochemistry , vol.34 , pp. 16138-16147
    • Shuman, S.1
  • 42
    • 0030813809 scopus 로고    scopus 로고
    • ' phosphate at the nick and occupancy of the adenylate binding site on the enzyme
    • Sekiguchi, J. and Shuman, S. (1997) Nick sensing by vaccinia virus DNA ligase requires a 5' phosphate at the nick and occupancy of the adenylate binding site on the enzyme. J. Virol., 71, 9679-9684.
    • (1997) J. Virol. , vol.71 , pp. 9679-9684
    • Sekiguchi, J.1    Shuman, S.2
  • 43
    • 0036159475 scopus 로고    scopus 로고
    • Substrate recognition and fidelity of strand joining by an archaeal DNA ligase
    • Nakatani, M., Ezaki, S., Atomi, H. and Imanaka, T. (2002) Substrate recognition and fidelity of strand joining by an archaeal DNA ligase. Eur. J. Biochem., 269, 650-656.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 650-656
    • Nakatani, M.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 44
    • 0034653795 scopus 로고    scopus 로고
    • Ligation reaction specificities of NAD+-dependent DNA ligase from the hyperthermophile Aquifex aeolicus
    • Tong, J., Barany, F. and Cao, W. (2000) Ligation reaction specificities of NAD+-dependent DNA ligase from the hyperthermophile Aquifex aeolicus. Nucleic Acids Res., 28, 1447-1454.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1447-1454
    • Tong, J.1    Barany, F.2    Cao, W.3
  • 45
    • 0029147555 scopus 로고
    • Ligation of nonmatching DNA molecule ends
    • Cimmino, C., Santori, F. and Donini, P. (1995) Ligation of nonmatching DNA molecule ends. Plasmid, 34, 1-10.
    • (1995) Plasmid , vol.34 , pp. 1-10
    • Cimmino, C.1    Santori, F.2    Donini, P.3
  • 46
    • 0023652090 scopus 로고
    • Mismatch and blunt to protruding-end joining by DNA ligases
    • Wiaderkiewicz, R. and Ruiz-Carrillo, A. (1987) Mismatch and blunt to protruding-end joining by DNA ligases. Nucleic Acids Res., 15, 7831-7847.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 7831-7847
    • Wiaderkiewicz, R.1    Ruiz-Carrillo, A.2
  • 47
    • 28544431617 scopus 로고    scopus 로고
    • A colorimetric method for point mutation detection using high-fidelity DNA ligase
    • Li, J., Chu, X., Liu, Y., Jiang, J., He, Z., Zhang, Z., Shen, G. and Yu, R. (2005) A colorimetric method for point mutation detection using high-fidelity DNA ligase. Nucleic Acids Res., 33, e168.
    • (2005) Nucleic Acids Res. , vol.33
    • Li, J.1    Chu, X.2    Liu, Y.3    Jiang, J.4    He, Z.5    Zhang, Z.6    Shen, G.7    Yu, R.8
  • 48
    • 0034121447 scopus 로고    scopus 로고
    • Universal DNA array detection of small insertions and deletions in BRCA1 and BRCA2
    • Favis, R., Day, J.P., Gerry, N.P., Phelan, C., Narod, S. and Barany, F. (2000) Universal DNA array detection of small insertions and deletions in BRCA1 and BRCA2. Nat. Biotechnol., 18, 561-564.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 561-564
    • Favis, R.1    Day, J.P.2    Gerry, N.P.3    Phelan, C.4    Narod, S.5    Barany, F.6
  • 49
    • 0029743388 scopus 로고    scopus 로고
    • Oligonucleotide ligation assay (OLA) for the diagnosis of familial hypercholesterolemia
    • Baron, H., Fung, S., Aydin, A., Bahring, S., Luft, F.C. and Schuster, H. (1996) Oligonucleotide ligation assay (OLA) for the diagnosis of familial hypercholesterolemia. Nat. Biotechnol., 14, 1279-1282.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1279-1282
    • Baron, H.1    Fung, S.2    Aydin, A.3    Bahring, S.4    Luft, F.C.5    Schuster, H.6
  • 50
    • 0026489345 scopus 로고
    • DNA ligase I from Saccharomyces cerevisiae: Physical and Biochemical characterization of the CDC9 gene product
    • Tomkinson, A.E., Tappe, N.J. and Friedberg, E.C. (1992) DNA ligase I from Saccharomyces cerevisiae: Physical and Biochemical characterization of the CDC9 gene product. Biochemistry, 31, 11762-11771.
    • (1992) Biochemistry , vol.31 , pp. 11762-11771
    • Tomkinson, A.E.1    Tappe, N.J.2    Friedberg, E.C.3
  • 51
    • 0025299872 scopus 로고
    • DNA ligases from rat liver. Purification and partial characterization of two molecular forms
    • Elder, R.H. and Rossignol, J. (1990) DNA ligases from rat liver. Purification and partial characterization of two molecular forms. Biochemistry, 29, 6009-6017.
    • (1990) Biochemistry , vol.29 , pp. 6009-6017
    • Elder, R.H.1    Rossignol, J.2
  • 52
    • 0024297824 scopus 로고
    • A ligase-mediated gene detection technique
    • Landegren, U., Kaiser, R., Sanders, J. and Hood, L. (1988) A ligase-mediated gene detection technique. Science, 241, 1077-1080.
    • (1988) Science , vol.241 , pp. 1077-1080
    • Landegren, U.1    Kaiser, R.2    Sanders, J.3    Hood, L.4
  • 53
    • 0020480166 scopus 로고
    • Sealing of gaps in duplex DNA by T4 DNA ligase
    • Nilsson, S.V. and Magnusson, G. (1982) Sealing of gaps in duplex DNA by T4 DNA ligase. Nucleic Acids Res., 10, 1425-1437.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1425-1437
    • Nilsson, S.V.1    Magnusson, G.2


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