메뉴 건너뛰기




Volumn 6, Issue 1, 2002, Pages 73-86

Identification, cloning, and expression of uracil-DNA glycosylase from Atlantic cod (Gadus morhua): Characterization and homology modeling of the cold-active catalytic domain

Author keywords

Cold active; Cold adapted; Gadus morhua; Homology modeling; Recombinant gene expression; Subcellular targeting; UDG; UNG; Uracil DNA glycosylase

Indexed keywords

ESCHERICHIA COLI; GADUS MORHUA; MAMMALIA;

EID: 0036484727     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s007920100225     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 0030924747 scopus 로고    scopus 로고
    • Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta
    • Aittaleb M, Hubner R, Lamotte-Brasseur J, Gerday C (1997) Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta. Protein Eng 10:475-477
    • (1997) Protein Eng , vol.10 , pp. 475-477
    • Aittaleb, M.1    Hubner, R.2    Lamotte-Brasseur, J.3    Gerday, C.4
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann E, Ochs B, Abel KJ (1988) Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • Barrett TE, Sawa R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92:117-129
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Sawa, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 4
    • 0029079249 scopus 로고
    • Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration
    • Bennett SE, Sanderson RJ, Mosbaugh DW (1995) Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration. Biochemistry 34:6109-6119
    • (1995) Biochemistry , vol.34 , pp. 6109-6119
    • Bennett, S.E.1    Sanderson, R.J.2    Mosbaugh, D.W.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK, Petsko GA (1985) Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229:23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50:760-763
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 8
    • 0028604549 scopus 로고
    • Unified catalytic mechanism for DNA glycosylases
    • Dodson ML, Michaels ML, Lloyd RS (1994) Unified catalytic mechanism for DNA glycosylases. J Biol Chem 269:32709-32712
    • (1994) J Biol Chem , vol.269 , pp. 32709-32712
    • Dodson, M.L.1    Michaels, M.L.2    Lloyd, R.S.3
  • 9
    • 0022373294 scopus 로고
    • Purification of nuclear and mitochondrial uracil-DNA glycosylase from rat liver. Identification of two distinct subcellular forms
    • Domena JD, Mosbaugh DW (1985) Purification of nuclear and mitochondrial uracil-DNA glycosylase from rat liver. Identification of two distinct subcellular forms. Biochemistry 24:7320-7328
    • (1985) Biochemistry , vol.24 , pp. 7320-7328
    • Domena, J.D.1    Mosbaugh, D.W.2
  • 10
    • 0021248364 scopus 로고
    • The cloning and overproduction of Escherichia coli uracil-DNA glycosylase
    • Duncan BK, Chambers JA (1984) The cloning and overproduction of Escherichia coli uracil-DNA glycosylase. Gene 28:211-219
    • (1984) Gene , vol.28 , pp. 211-219
    • Duncan, B.K.1    Chambers, J.A.2
  • 11
  • 12
    • 0029958604 scopus 로고    scopus 로고
    • A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
    • U S A
    • Gassner NC, Baase WA, Matthews BW (1996) A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. Proc Natl Acad Sci U S A 93:12155-12158
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 12155-12158
    • Gassner, N.C.1    Baase, W.A.2    Matthews, B.W.3
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 84952490376 scopus 로고
    • A review of proteolytic enzymes from marine organisms and their applications in the food industry
    • Haard NF (1992) A review of proteolytic enzymes from marine organisms and their applications in the food industry. J Aquat Food Prod Technol 1:117-125
    • (1992) J Aquat Food Prod Technol , vol.1 , pp. 117-125
    • Haard, N.F.1
  • 15
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter KA, Todd Stukenberg MW, Kirschner MW, Verdine GL (1999) Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. Curr Biol 9:174-185
    • (1999) Curr Biol , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 16
    • 0027300148 scopus 로고
    • Processivity of uracil DNA glycosylase
    • Higley M, Lloyd RS (1993) Processivity of uracil DNA glycosylase. Mutat Res 294:109-116
    • (1993) Mutat Res , vol.294 , pp. 109-116
    • Higley, M.1    Lloyd, R.S.2
  • 19
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR (1993) Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32:11259-11269
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    Elmasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 20
    • 0034170459 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of the heat-labile uracil-DNA glycosylase from a marine psychrophilic bacterium, strain BMTU3346
    • Jaeger S, Schmuck R, Sobek H (2000) Molecular cloning, sequencing, and expression of the heat-labile uracil-DNA glycosylase from a marine psychrophilic bacterium, strain BMTU3346. Extremophiles 4:115-122.
    • (2000) Extremophiles , vol.4 , pp. 115-122
    • Jaeger, S.1    Schmuck, R.2    Sobek, H.3
  • 21
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 22
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, Slupphaug G (1997) DNA glycosylases in the base excision repair of DNA. Biochem J 325:1-16
    • (1997) Biochem J , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 23
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase beta and the XRCC1 protein
    • Kubota Y, Nash RA, Klungland A, Schar P, Barnes DE, Lindahl T (1996) Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO J 15:6662-6670
    • (1996) EMBO J , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 24
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • U S A
    • Kunkel TA (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci U S A 82:488-492
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0033744003 scopus 로고    scopus 로고
    • Purification and characterization of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua)
    • Lanes O, Guddal PH, Gjellesvik DR, Willassen NP (2000) Purification and characterization of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua). Comp Biochem Physiol B 127:399-410.
    • (2000) Comp Biochem Physiol B , vol.127 , pp. 399-410
    • Lanes, O.1    Guddal, P.H.2    Gjellesvik, D.R.3    Willassen, N.P.4
  • 27
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • Leiros HK, Willassen NP, Smalås AO (1999) Residue determinants and sequence analysis of cold-adapted trypsins. Extremophiles 3:205-219
    • (1999) Extremophiles , vol.3 , pp. 205-219
    • Leiros, H.K.1    Willassen, N.P.2    Smalås, A.O.3
  • 28
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation
    • Leiros HKS, Willassen NP, Smalås AO (2000) Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation. Eur J Biochem 267:1-12
    • (2000) Eur J Biochem , vol.267 , pp. 1-12
    • Leiros, H.K.S.1    Willassen, N.P.2    Smalås, A.O.3
  • 30
    • 0017392934 scopus 로고
    • DNA N-glycosidases: Properties of uracil-DNA glycosidase from Escherichia coli
    • Lindahl T, Ljungquist S, Siegert W, Nyberg B, Sperens B (1977) DNA N-glycosidases: properties of uracil-DNA glycosidase from Escherichia coli. J Biol Chem 252:3286-3294
    • (1977) J Biol Chem , vol.252 , pp. 3286-3294
    • Lindahl, T.1    Ljungquist, S.2    Siegert, W.3    Nyberg, B.4    Sperens, B.5
  • 31
    • 0022573212 scopus 로고
    • Kinetics of protein-nucleic acid interactions: Use of salt effects to probe mechanisms of interaction
    • Lohman TM (1986) Kinetics of protein-nucleic acid interactions: use of salt effects to probe mechanisms of interaction. Crit Rev Biochem 19:191-245
    • (1986) Crit Rev Biochem , vol.19 , pp. 191-245
    • Lohman, T.M.1
  • 32
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmatic transport: The soluble phase
    • Mattaj IW, Englmeier L (1998) Nucleocytoplasmatic transport: the soluble phase. Annu Rev Biochem 67:265-306
    • (1998) Annu Rev Biochem , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 33
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM (1994) Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 34
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA (1995) Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80:869-878
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 36
    • 0026093209 scopus 로고
    • Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase
    • Muller SJ, Caradonna S (1991) Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase. Biochim Biophys Acta 1088:197-207
    • (1991) Biochim Biophys Acta , vol.1088 , pp. 197-207
    • Muller, S.J.1    Caradonna, S.2
  • 37
    • 0030996226 scopus 로고    scopus 로고
    • A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A
    • Nagelhus TA, Haug T, Singh KK, Keshav KF, Skorpen F, Otterlei M, Bharati S, Lindmo T, Benichou S, Benarous R, Krokan HE (1997) A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A. J Biol Chem 272:6561-6566
    • (1997) J Biol Chem , vol.272 , pp. 6561-6566
    • Nagelhus, T.A.1    Haug, T.2    Singh, K.K.3    Keshav, K.F.4    Skorpen, F.5    Otterlei, M.6    Bharati, S.7    Lindmo, T.8    Benichou, S.9    Benarous, R.10    Krokan, H.E.11
  • 38
    • 0030939690 scopus 로고    scopus 로고
    • Reconstitution of human base excision repair with purified proteins
    • Nicholl ID, Nealon K, Kenny MK (1997) Reconstitution of human base excision repair with purified proteins. Biochemistry 36:7557-7566
    • (1997) Biochemistry , vol.36 , pp. 7557-7566
    • Nicholl, I.D.1    Nealon, K.2    Kenny, M.K.3
  • 39
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 40
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • Nilsen H, Otterlei M, Haug T, Solum K, Nagelhus TA, Skorpen F, Krokan HE (1997) Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res 25:750-755
    • (1997) Nucleic Acids Res , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 41
    • 0034659762 scopus 로고    scopus 로고
    • Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues
    • Nilsen H, Steinsbekk KS, Otterlei M, Slupphaug G, Aas PA, Krokan HE (2000) Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues. Nucleic Acids Res 28:2277-2285.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2277-2285
    • Nilsen, H.1    Steinsbekk, K.S.2    Otterlei, M.3    Slupphaug, G.4    Aas, P.A.5    Krokan, H.E.6
  • 42
    • 0032531934 scopus 로고    scopus 로고
    • Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively
    • Otterlei M, Haug T, Nagelhus TA, Slupphaug G, Lindmo T, Krokan HE (1998) Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively. Nucleic Acids Res 26:4611-4617
    • (1998) Nucleic Acids Res , vol.26 , pp. 4611-4617
    • Otterlei, M.1    Haug, T.2    Nagelhus, T.A.3    Slupphaug, G.4    Lindmo, T.5    Krokan, H.E.6
  • 44
    • 0029851195 scopus 로고    scopus 로고
    • Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin
    • Outzen H, Berglund GI, Smalås AO, Willassen NP (1996) Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp Biochem Physiol B 115:33-45
    • (1996) Comp Biochem Physiol B , vol.115 , pp. 33-45
    • Outzen, H.1    Berglund, G.I.2    Smalås, A.O.3    Willassen, N.P.4
  • 45
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace CN, Scholtz JM (1998) A helix propensity scale based on experimental studies of peptides and proteins. Biophys J 75:422-427
    • (1998) Biophys J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 46
    • 0031574192 scopus 로고    scopus 로고
    • Base excision repair enzyme family portrait: Integrating the structure and chemistry of an entire DNA repair pathway
    • Parikh SS, Mol CD, Tainer JA (1997) Base excision repair enzyme family portrait: integrating the structure and chemistry of an entire DNA repair pathway. Structure 5:1543-1550
    • (1997) Structure , vol.5 , pp. 1543-1550
    • Parikh, S.S.1    Mol, C.D.2    Tainer, J.A.3
  • 47
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA (1998) Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J 17:5214-5226
    • (1998) EMBO J , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 48
    • 0034734380 scopus 로고    scopus 로고
    • Lessons learned from structural results on uracil-DNA glycosylase
    • Parikh SS, Putnam CD, Tainer JA (2000) Lessons learned from structural results on uracil-DNA glycosylase. Mutat Res 460:183-199.
    • (2000) Mutat Res , vol.460 , pp. 183-199
    • Parikh, S.S.1    Putnam, C.D.2    Tainer, J.A.3
  • 49
    • 0027963399 scopus 로고
    • Uracil DNA N-glycosylase distributively interacts with duplex polynucleotides containing repeating units of either TGGCCAAGCU or TGGCCAAGCTTGGCCAAGCU
    • Purmal AA, Lampman GW, Pourmal EI, Melamede RJ, Wallace SS, Kow YW (1994) Uracil DNA N-glycosylase distributively interacts with duplex polynucleotides containing repeating units of either TGGCCAAGCU or TGGCCAAGCTTGGCCAAGCU. J Biol Chem 269:22046-22053
    • (1994) J Biol Chem , vol.269 , pp. 22046-22053
    • Purmal, A.A.1    Lampman, G.W.2    Pourmal, E.I.3    Melamede, R.J.4    Wallace, S.S.5    Kow, Y.W.6
  • 50
    • 3643055084 scopus 로고    scopus 로고
    • X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG
    • Ravishankar R, Bidya Sagar M, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M (1998) X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG. Nucleic Acids Res 26:4880-4887
    • (1998) Nucleic Acids Res , vol.26 , pp. 4880-4887
    • Ravishankar, R.1    Bidya Sagar, M.2    Roy, S.3    Purnapatre, K.4    Handa, P.5    Varshney, U.6    Vijayan, M.7
  • 51
    • 0033587149 scopus 로고    scopus 로고
    • Thermostable uracil-DNA glycosylase from Thermotoga maritima a member of a novel class of DNA repair enzymes
    • Sandigursky M, Franklin WA (1999) Thermostable uracil-DNA glycosylase from Thermotoga maritima a member of a novel class of DNA repair enzymes. Curr Biol 9:531-534
    • (1999) Curr Biol , vol.9 , pp. 531-534
    • Sandigursky, M.1    Franklin, W.A.2
  • 52
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva R, McAuley Hecht K, Brown T, Pearl L (1995) The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373:487-493
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley Hecht, K.2    Brown, T.3    Pearl, L.4
  • 53
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B (1996) Common principles of protein translocation across membranes. Science 271:1519-1526
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 54
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles
    • Serrano L, Bycroft M, Fersht AR (1991) Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. J Mol Biol 218:465-475
    • (1991) J Mol Biol , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 55
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • Slupphaug G, Eftedal I, Kavli B, Bharati S, Helle NM, Haug T, Levine DW, Krokan HE (1995) Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase. Biochemistry 34:128-138
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, N.M.5    Haug, T.6    Levine, D.W.7    Krokan, H.E.8
  • 56
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA (1996) A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature 384:87-92
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 57
    • 0028033122 scopus 로고
    • Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins
    • Smalås AO, Heimstad ES, Hordvik A, Willassen NP, Male R (1994) Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20:149-166
    • (1994) Proteins , vol.20 , pp. 149-166
    • Smalås, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 59
    • 0033579953 scopus 로고    scopus 로고
    • Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase
    • Stivers JT, Pankiewicz KW, Watanabe KA (1999) Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase. Biochemistry 38:952-963
    • (1999) Biochemistry , vol.38 , pp. 952-963
    • Stivers, J.T.1    Pankiewicz, K.W.2    Watanabe, K.A.3
  • 60
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 19244385448 scopus 로고
    • Characterization of the ung1 mutation of Escherichia coli
    • Varshney U, van de Sande JH (1989) Characterization of the ung1 mutation of Escherichia coli. Nucleic Acids Res 17:813
    • (1989) Nucleic Acids Res , vol.17 , pp. 813
    • Varshney, U.1    Van De Sande, J.H.2
  • 62
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel PH, Berg OG (1989) Facilitated target location in biological systems. J Biol Chem 264:675-678
    • (1989) J Biol Chem , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 63
    • 0009618275 scopus 로고    scopus 로고
    • Conservation of genome and gene structure from fishes to mammals
    • Walter RB, Morizot DC (1996) Conservation of genome and gene structure from fishes to mammals. Adv Struct Biol 4:1-24
    • (1996) Adv Struct Biol , vol.4 , pp. 1-24
    • Walter, R.B.1    Morizot, D.C.2
  • 64
    • 0022296158 scopus 로고
    • Uracil-DNA glycosylase in HeLa S3 cells: Interconvertibility of 50 and 20 kDa forms and similarity of the nuclear and mitochondrial form of the enzyme
    • Wittwer CU, Krokan H (1985) Uracil-DNA glycosylase in HeLa S3 cells: interconvertibility of 50 and 20 kDa forms and similarity of the nuclear and mitochondrial form of the enzyme. Biochim Biophys Acta 832:308-318
    • (1985) Biochim Biophys Acta , vol.832 , pp. 308-318
    • Wittwer, C.U.1    Krokan, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.