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Volumn 19, Issue 9, 2010, Pages 1616-1626

The structure and evolution of the murine inhibitor of carbonic anhydrase: A member of the transferrin superfamily

Author keywords

Inhibitor of carbonic anhydrase; Protein structure; Pseudomerohedral twinned crystal; Selection pressure (dN dS); Transferrin family

Indexed keywords

ARGININE; CARBONATE DEHYDRATASE; INHIBITOR OF CARBONIC ANHYDRASE; IRON; SERINE; TRANSFERRIN; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 77956353021     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.439     Document Type: Article
Times cited : (14)

References (79)
  • 2
    • 74649083370 scopus 로고    scopus 로고
    • Iron transport by transferrin
    • Fuchs H, Ed. Kerala, India: Research Signpost
    • Mason AB, Everse SJ, Iron transport by transferrin. In: Fuchs H, Ed. (2008) Iron metabolism and disease. Kerala, India: Research Signpost, pp 83-123.
    • (2008) Iron Metabolism and Disease , pp. 83-123
    • Mason, A.B.1    Everse, S.J.2
  • 6
    • 0028835226 scopus 로고
    • Crystal structure of diferric hen ovotransferrin at 2.4 Å resolution
    • Kurokawa H, Mikami B, Hirose M (1995) Crystal structure of diferric hen ovotransferrin at 2.4 Å resolution. J Mol Biol 254:196-207.
    • (1995) J Mol Biol , vol.254 , pp. 196-207
    • Kurokawa, H.1    Mikami, B.2    Hirose, M.3
  • 8
    • 0036006760 scopus 로고    scopus 로고
    • The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 Å, respectively
    • Hall DR, Hadden JM, Leonard GA, Bailey S, Neu M, Winn M, Lindley PF (2002) The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 Å, respectively. Acta Crystallogr Sect D 58:70-80.
    • (2002) Acta Crystallogr Sect D , vol.58 , pp. 70-80
    • Hall, D.R.1    Hadden, J.M.2    Leonard, G.A.3    Bailey, S.4    Neu, M.5    Winn, M.6    Lindley, P.F.7
  • 9
    • 0016715330 scopus 로고
    • Difference between the two iron-binding sites of transferrin
    • Princiotto JV, Zapolski EJ (1975) Difference between the two iron-binding sites of transferrin. Nature 255: 87-88.
    • (1975) Nature , vol.255 , pp. 87-88
    • Princiotto, J.V.1    Zapolski, E.J.2
  • 10
    • 0017230087 scopus 로고
    • The effect of pH upon human transferrin: Selective labelling of the two iron-binding sites
    • Lestas AN (1976) The effect of pH upon human transferrin: selective labelling of the two iron-binding sites. Br J Haematol 32:341-350.
    • (1976) Br J Haematol , vol.32 , pp. 341-350
    • Lestas, A.N.1
  • 11
    • 0018264497 scopus 로고
    • Oxalate and spin-labeled oxalate as probes of the anion binding site of human transferrin
    • Najarian RC, Harris DC, Aisen P (1978) Oxalate and spin-labeled oxalate as probes of the anion binding site of human transferrin. J Biol Chem 253:38-42.
    • (1978) J Biol Chem , vol.253 , pp. 38-42
    • Najarian, R.C.1    Harris, D.C.2    Aisen, P.3
  • 12
    • 0019891047 scopus 로고
    • The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferric transferrins
    • Baldwin DA, DeSousa DMR (1981) The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferric transferrins. Biochem Biophys Res Commun 99:1101-1107.
    • (1981) Biochem Biophys Res Commun , vol.99 , pp. 1101-1107
    • Baldwin, D.A.1    DeSousa, D.M.R.2
  • 13
    • 0037426355 scopus 로고    scopus 로고
    • Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: Mutational analysis of the role of a pH sensitive triad
    • Halbrooks PJ, He QY, Briggs SK, Everse SJ, Smith VC, MacGillivray RTA, Mason AB (2003) Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: mutational analysis of the role of a pH sensitive triad. Biochemistry 42: 3701-3707.
    • (2003) Biochemistry , vol.42 , pp. 3701-3707
    • Halbrooks, P.J.1    He, Q.Y.2    Briggs, S.K.3    Everse, S.J.4    Smith, V.C.5    MacGillivray, R.T.A.6    Mason, A.B.7
  • 14
    • 0030008682 scopus 로고    scopus 로고
    • Anion binding by transferrins: Importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin
    • Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN (1996) Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin. Biochemistry 35:9007-9013.
    • (1996) Biochemistry , vol.35 , pp. 9007-9013
    • Baker, H.M.1    Anderson, B.F.2    Brodie, A.M.3    Shongwe, M.S.4    Smith, C.A.5    Baker, E.N.6
  • 15
    • 0001231645 scopus 로고    scopus 로고
    • Transferrin as a metal ion mediator
    • Sun H, Li H, Sadler PJ (1999) Transferrin as a metal ion mediator. Chem Rev 99:2817-2842.
    • (1999) Chem Rev , vol.99 , pp. 2817-2842
    • Sun, H.1    Li, H.2    Sadler, P.J.3
  • 16
    • 11144261515 scopus 로고    scopus 로고
    • Evolution of the duplications in the transferrin family of proteins
    • Lambert LA, Perri H, Meehan TJ (2005) Evolution of the duplications in the transferrin family of proteins. Comp Biochem Physiol B 140:11-25.
    • (2005) Comp Biochem Physiol B , vol.140 , pp. 11-25
    • Lambert, L.A.1    Perri, H.2    Meehan, T.J.3
  • 17
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of the transferrin family: Conservation of residues associated with iron and anion binding
    • Lambert LA, Perri H, Halbrooks PJ, Mason AB (2005) Evolution of the transferrin family: conservation of residues associated with iron and anion binding. Comp Biochem Physiol B 142:129-141.
    • (2005) Comp Biochem Physiol B , vol.142 , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3    Mason, A.B.4
  • 19
    • 0034568949 scopus 로고    scopus 로고
    • The catalytic mechanism of mammalian carbonic anhydrases
    • Lindskog S, Silverman DN (2000) The catalytic mechanism of mammalian carbonic anhydrases. EXS 90: 175-195.
    • (2000) EXS , vol.90 , pp. 175-195
    • Lindskog, S.1    Silverman, D.N.2
  • 21
    • 0026619849 scopus 로고
    • Genetics of the mammalian carbonic anhydrases
    • Tashian RE (1992) Genetics of the mammalian carbonic anhydrases. Adv Genet 30:321-356.
    • (1992) Adv Genet , vol.30 , pp. 321-356
    • Tashian, R.E.1
  • 22
    • 0034569944 scopus 로고    scopus 로고
    • An overview of the distribution and function of carbonic anhydrase in mammals
    • Chegwidden WR, Edwards Y, Carter N, Eds. Basel: Birkhäuser Verlag
    • Parkkila S, An overview of the distribution and function of carbonic anhydrase in mammals. In: Chegwidden WR, Edwards Y, Carter N, Eds. (2000) The carbonic anhydrases-new horizons. Basel: Birkhäuser Verlag, pp 79-93.
    • (2000) The Carbonic Anhydrases-new Horizons , pp. 79-93
    • Parkkila, S.1
  • 23
    • 0034100924 scopus 로고    scopus 로고
    • Carbon dioxide transport and carbonic anhydrase in blood and muscle
    • Geers C, Gros G (2000) Carbon dioxide transport and carbonic anhydrase in blood and muscle. Physiol Rev 80:681-715. (Pubitemid 30164947)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 681-715
    • Geers, C.1    Gros, G.2
  • 25
    • 0030981906 scopus 로고    scopus 로고
    • Cloning, sequencing, and recombinant expression of the porcine inhibitor of carbonic anhydrase: A novel member of the transferrin family
    • Wuebbens MW, Roush ED, Decastro CM, Fierke CA (1997) Cloning, sequencing, and recombinant expression of the porcine inhibitor of carbonic anhydrase: a novel member of the transferrin family. Biochemistry 36:4327-4336.
    • (1997) Biochemistry , vol.36 , pp. 4327-4336
    • Wuebbens, M.W.1    Roush, E.D.2    Decastro, C.M.3    Fierke, C.A.4
  • 26
    • 0026969367 scopus 로고
    • Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma
    • Roush ED, Fierke CA (1992) Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma. Biochemistry 31:12536-12542.
    • (1992) Biochemistry , vol.31 , pp. 12536-12542
    • Roush, E.D.1    Fierke, C.A.2
  • 27
    • 0001067375 scopus 로고
    • The carbonic anhydrase inhibitor in serum
    • Booth VH (1938) The carbonic anhydrase inhibitor in serum. J Physiol 91:474-489.
    • (1938) J Physiol , vol.91 , pp. 474-489
    • Booth, V.H.1
  • 28
    • 0022530866 scopus 로고
    • Inhibition of carbonic anhydrase by plasma of dogs and rabbits
    • Hill EP (1986) Inhibition of carbonic anhydrase by plasma of dogs and rabbits. J Appl Physiol 60:191-197. (Pubitemid 16024032)
    • (1986) Journal of Applied Physiology , vol.60 , Issue.1 , pp. 191-197
    • Hill, E.P.1
  • 29
    • 0023201332 scopus 로고
    • Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene
    • Schaeffer E, Lucero MA, Jeltsch JM, Py MC, Levin MJ, Chambon P, Cohen GN, Zakin MM (1987) Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene. Gene 56:109-116.
    • (1987) Gene , vol.56 , pp. 109-116
    • Schaeffer, E.1    Lucero, M.A.2    Jeltsch, J.M.3    Py, M.C.4    Levin, M.J.5    Chambon, P.6    Cohen, G.N.7    Zakin, M.M.8
  • 30
    • 0008144817 scopus 로고
    • Primary structure of the human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence
    • Rose TM, Plowman GD, Teplow DP, Dreyer WJ, Hellström KE, Brown TP (1986) Primary structure of the human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence. Proc Natl Acad Sci USA 83:1261-1265.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1261-1265
    • Rose, T.M.1    Plowman, G.D.2    Teplow, D.P.3    Dreyer, W.J.4    Hellström, K.E.5    Brown, T.P.6
  • 32
    • 0034644835 scopus 로고    scopus 로고
    • The membrane-bound transferrin homologue melanotransferrin: Roles other than iron transport?
    • Sekyere E, Richardson DR (2000) The membrane-bound transferrin homologue melanotransferrin: roles other than iron transport?FEBS Lett 483:11-16.
    • (2000) FEBS Lett , vol.483 , pp. 11-16
    • Sekyere, E.1    Richardson, D.R.2
  • 33
    • 14544273227 scopus 로고    scopus 로고
    • Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human
    • Sekyere EO, Dunn LL, Richardson DR (2005) Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human. Biochim Biophys Acta 1722:131-142.
    • (2005) Biochim Biophys Acta , vol.1722 , pp. 131-142
    • Sekyere, E.O.1    Dunn, L.L.2    Richardson, D.R.3
  • 34
    • 33645528381 scopus 로고    scopus 로고
    • Role of melanotransferrin in iron metabolism: Studies using targeted gene disruption in vivo
    • Sekyere EO, Dunn LL, Rahmanto YS, Richardson DR (2006) Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo. Blood 107:2599-2601.
    • (2006) Blood , vol.107 , pp. 2599-2601
    • Sekyere, E.O.1    Dunn, L.L.2    Rahmanto, Y.S.3    Richardson, D.R.4
  • 35
    • 33747641642 scopus 로고    scopus 로고
    • The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding
    • DOI 10.1074/jbc.M604592200
    • Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK (2006) The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding. J Biol Chem 281:24934-24944. (Pubitemid 44274264)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24934-24944
    • Wally, J.1    Halbrooks, P.J.2    Vonrhein, C.3    Rould, M.A.4    Everse, S.J.5    Mason, A.B.6    Buchanan, S.K.7
  • 36
    • 0346432066 scopus 로고    scopus 로고
    • Acetobacter turbidans alpha-amino acid ester hydrolase: Merohedral twinning in P21 obscured by pseudo-translational NCS
    • Barends TR, Dijkstra BW (2003) Acetobacter turbidans alpha-amino acid ester hydrolase: merohedral twinning in P21 obscured by pseudo-translational NCS. Acta Crystallogr Sect D 59:2237-2241.
    • (2003) Acta Crystallogr Sect D , vol.59 , pp. 2237-2241
    • Barends, T.R.1    Dijkstra, B.W.2
  • 38
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • Baker EN, Baker HM (2009) A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 91:3-10.
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.N.1    Baker, H.M.2
  • 39
    • 0025690309 scopus 로고
    • Situations of gamma-turns in proteins. Their relation to alpha-helices, beta-sheets and ligand binding sites
    • Milner-White EJ (1990) Situations of gamma-turns in proteins. Their relation to alpha-helices, beta-sheets and ligand binding sites. J Mol Biol 216:386-397.
    • (1990) J Mol Biol , vol.216 , pp. 386-397
    • Milner-White, E.J.1
  • 40
    • 70349916052 scopus 로고    scopus 로고
    • A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping
    • Mason AB, Byrne SL, Everse SJ, Roberts SE, Chasteen ND, Smith VC, MacGillivray RT, Kandemir B, Bou-Abdallah F (2009) A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping. J Mol Recognit 22: 521-529.
    • (2009) J Mol Recognit , vol.22 , pp. 521-529
    • Mason, A.B.1    Byrne, S.L.2    Everse, S.J.3    Roberts, S.E.4    Chasteen, N.D.5    Smith, V.C.6    MacGillivray, R.T.7    Kandemir, B.8    Bou-Abdallah, F.9
  • 43
    • 0032213139 scopus 로고    scopus 로고
    • Structure of human apolactoferrin at 2.0 a resolution. Refinement and analysis of ligand-induced conformational change
    • Jameson GB, Anderson BF, Norris GE, Thomas DH, Baker EN (1998) Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallogr Sect D 54:1319-1335.
    • (1998) Acta Crystallogr Sect D , vol.54 , pp. 1319-1335
    • Jameson, G.B.1    Anderson, B.F.2    Norris, G.E.3    Thomas, D.H.4    Baker, E.N.5
  • 44
    • 0027438949 scopus 로고
    • Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces
    • DOI 10.1006/jmbi.1993.1592
    • Gerstein M, Anderson BF, Norris GE, Baker EN, Lesk AM, Chothia C (1993) Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces. J Mol Biol 234:357-372. (Pubitemid 23361207)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.2 , pp. 357-372
    • Gerstein, M.1    Anderson, B.F.2    Norris, G.E.3    Baker, E.N.4    Lesk, A.M.5    Chothia, C.6
  • 45
    • 0032486130 scopus 로고    scopus 로고
    • The nature of ligand-induced conformational change in transferrin in solution. An investigation using X-ray scattering, XAFS and site-directed mutants
    • Grossmann JG, Crawley JB, Strange RW, Patel KJ, Murphy LM, Neu M, Evans RW, Hasnain SS (1998) The nature of ligand-induced conformational change in transferrin in solution. An investigation using X-ray scattering, XAFS and site-directed mutants. J Mol Biol 279:461-472.
    • (1998) J Mol Biol , vol.279 , pp. 461-472
    • Grossmann, J.G.1    Crawley, J.B.2    Strange, R.W.3    Patel, K.J.4    Murphy, L.M.5    Neu, M.6    Evans, R.W.7    Hasnain, S.S.8
  • 46
    • 0031214161 scopus 로고    scopus 로고
    • Tertiary structural changes and iron release from human serum transferrin
    • DOI 10.1006/jmbi.1997.1126
    • Mecklenburg SL, Donohoe RJ, Olah GA (1997) Tertiary structural changes and iron release from human serum transferrin. J Mol Biol 270:739-750. (Pubitemid 27332063)
    • (1997) Journal of Molecular Biology , vol.270 , Issue.5 , pp. 739-750
    • Mecklenburg, S.L.1    Donohoe, R.J.2    Olah, G.A.3
  • 47
    • 0035876277 scopus 로고    scopus 로고
    • Domain closure mechanism in transferrins: New viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe
    • DOI 10.1006/jmbi.2001.4719
    • Mizutani K, Mikami B, Hirose M (2001) Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe. J Mol Biol 309:937-947. (Pubitemid 32575086)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.4 , pp. 937-947
    • Mizutani, K.1    Mikami, B.2    Hirose, M.3
  • 48
    • 0344119509 scopus 로고    scopus 로고
    • A Computational Study of the Open and Closed Forms of the N-Lobe Human Serum Transferrin Apoprotein
    • Rinaldo D, Field MJ (2003) A computational study of the open and closed forms of the N-lobe human serum transferrin apoprotein. Biophys J 85:3485-3501. (Pubitemid 37490265)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3485-3501
    • Rinaldo, D.1    Field, M.J.2
  • 49
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • DOI 10.1038/nature06232, PII NATURE06232
    • Tang C, Schwieters CD, Clore GM (2007) Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 449: 1078-1082. (Pubitemid 350014601)
    • (2007) Nature , vol.449 , Issue.7165 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 50
    • 77749286394 scopus 로고    scopus 로고
    • Ligand-free open-closed transitions of periplasmic binding proteins: The case of glutamine-binding protein
    • Bermejo GA, Strub MP, Ho C, Tjandra N (2010) Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein. Biochemistry 49:1893-1902.
    • (2010) Biochemistry , vol.49 , pp. 1893-1902
    • Bermejo, G.A.1    Strub, M.P.2    Ho, C.3    Tjandra, N.4
  • 51
    • 0141591721 scopus 로고    scopus 로고
    • Kinetics of metal ion exchange between citric acid and serum transferrin
    • Harris WR, Wang Z, Brook C, Yang B, Islam A (2003) Kinetics of metal ion exchange between citric acid and serum transferrin. Inorg Chem 42:5880-5889.
    • (2003) Inorg Chem , vol.42 , pp. 5880-5889
    • Harris, W.R.1    Wang, Z.2    Brook, C.3    Yang, B.4    Islam, A.5
  • 52
    • 22444436454 scopus 로고    scopus 로고
    • The limit of accuracy of protein modeling: Influence of crystal packing on protein structure
    • DOI 10.1016/j.jmb.2005.05.066, PII S0022283605006339
    • Eyal E, Gerzon S, Potapov V, Edelman M, Sobolev V (2005) The limit of accuracy of protein modeling: influence of crystal packing on protein structure. J Mol Biol 351:431-442. (Pubitemid 41007760)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.2 , pp. 431-442
    • Eyal, E.1    Gerzon, S.2    Potapov, V.3    Edelman, M.4    Sobolev, V.5
  • 53
    • 0027360843 scopus 로고
    • Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron release
    • DOI 10.1021/bi00096a004
    • Dewan JC, Mikami B, Hirose M, Sacchettini JC (1993) Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release. Biochemistry 32:11963-11968. (Pubitemid 23353632)
    • (1993) Biochemistry , vol.32 , Issue.45 , pp. 11963-11968
    • Dewan, J.C.1    Mikami, B.2    Hirose, M.3    Sacchettini, J.C.4
  • 54
    • 0033609501 scopus 로고    scopus 로고
    • Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: Iron-release trigger and anion-binding site
    • He QY, Mason AB, Tam BM, MacGillivray RTA, Wood-worth RC (1999) Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron-release trigger and anion-binding site. Biochemistry 38:9704-9711.
    • (1999) Biochemistry , vol.38 , pp. 9704-9711
    • He, Q.Y.1    Mason, A.B.2    Tam, B.M.3    MacGillivray, R.T.A.4    Wood-Worth, R.C.5
  • 55
    • 28244493040 scopus 로고    scopus 로고
    • Composition of pH sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release
    • Halbrooks PJ, Giannetti AM, Klein JS, Bjorkman PJ, Larouche JR, Smith VC, MacGillivray RTA, Everse SJ, Mason AB (2005) Composition of pH sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release. Biochemistry 44:15451-15460.
    • (2005) Biochemistry , vol.44 , pp. 15451-15460
    • Halbrooks, P.J.1    Giannetti, A.M.2    Klein, J.S.3    Bjorkman, P.J.4    Larouche, J.R.5    Smith, V.C.6    MacGillivray, R.T.A.7    Everse, S.J.8    Mason, A.B.9
  • 59
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 60
    • 44649182119 scopus 로고    scopus 로고
    • Protocol to determine accurate absorption coefficients for iron containing transferrins
    • James NG, Mason AB (2008) Protocol to determine accurate absorption coefficients for iron containing transferrins. Anal Biochem 378:202-207.
    • (2008) Anal Biochem , vol.378 , pp. 202-207
    • James, N.G.1    Mason, A.B.2
  • 61
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter CW, Sweet RM, editors. San Diego: Academic Press
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter CW, Sweet RM, editors. Methods in enzymology, part A. San Diego: Academic Press, pp 307-326.
    • Methods in Enzymology, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 62
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudocentering and utility for detecting twinning
    • Padilla JE, Yeates TO (2003) A statistic for local intensity differences: robustness to anisotropy and pseudocentering and utility for detecting twinning. Acta Crystallogr Sect D 59:1124-1130.
    • (2003) Acta Crystallogr Sect D , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 63
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D 50:760-763.
    • (1994) Acta Crystallogr Sect D , vol.50 , pp. 760-763
  • 65
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • Stein N (2008) CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J Appl Crystallogr 41:641-643.
    • (2008) J Appl Crystallogr , vol.41 , pp. 641-643
    • Stein, N.1
  • 68
    • 23844432031 scopus 로고    scopus 로고
    • Structure of a pseudomerohedrally twinned monoclinic crystal form of a pyridoxal phosphate-dependent catalytic antibody
    • Golinelli-Pimpaneau B (2005) Structure of a pseudomerohedrally twinned monoclinic crystal form of a pyridoxal phosphate-dependent catalytic antibody. Acta Crystallogr Sect D 61:472-476.
    • (2005) Acta Crystallogr Sect D , vol.61 , pp. 472-476
    • Golinelli-Pimpaneau, B.1
  • 69
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr Sect D 57:122-133.
    • (2001) Acta Crystallogr Sect D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 70
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr Sect D 60: 2126-2132.
    • (2004) Acta Crystallogr Sect D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 72
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of prgressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matriz choice
    • Thompson J, Higgins D, Gibson T (1994) CLUSTAL W: improving the sensitivity of prgressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matriz choice. Nucleic Acids Res 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 74
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Int J Neural Syst 8: 581-599.
    • (1997) Int J Neural Syst , vol.8 , pp. 581-599
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 75
    • 33747847779 scopus 로고    scopus 로고
    • PAL2NAL: Robust conversion of protein sequence alignments into the corresponding codon alignments
    • Suyama M, Torrents D, Bork P (2006) PAL2NAL: robust conversion of protein sequence alignments into the corresponding codon alignments. Nucleic Acids Res 34:W609-W612.
    • (2006) Nucleic Acids Res , vol.34
    • Suyama, M.1    Torrents, D.2    Bork, P.3
  • 76
    • 34547567977 scopus 로고    scopus 로고
    • Selecton 2007: Advanced models for detecting positive and purifying selection using a Bayesian inference approach
    • Stern A, Doron-Faigenboim A, Erez E, Martz E, Bacharach E, Pupko T (2007) Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach. Nucleic Acids Res 35:W506-W511.
    • (2007) Nucleic Acids Res , vol.35
    • Stern, A.1    Doron-Faigenboim, A.2    Erez, E.3    Martz, E.4    Bacharach, E.5    Pupko, T.6
  • 77
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • DOI 10.1093/bioinformatics/bti263
    • Abascal F, Zardoya R, Posada D (2005) ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21:2104-2105. (Pubitemid 40668057)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 78
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 79
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8:275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3


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