메뉴 건너뛰기




Volumn 100, Issue 1, 2002, Pages 299-305

Intersubunit circular permutation of human hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN;

EID: 0036659929     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V100.1.299     Document Type: Article
Times cited : (11)

References (51)
  • 1
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TP. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J Mol Biol. 1983;165:407-413.
    • (1983) J Mol Biol , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.P.2
  • 2
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a βα barrel enzyme in vivo
    • Luger K, Hommel U, Herold M, Hofsteenge J, Kirschner K. Correct folding of circularly permuted variants of a βα barrel enzyme in vivo. Science. 1989;243:206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 3
    • 0028099766 scopus 로고
    • Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis
    • Hahn M, Piotukh K, Borriss R, Heinemann U. Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis. Proc Natl Acad Sci U S A. 1994;91:10417-10421.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10417-10421
    • Hahn, M.1    Piotukh, K.2    Borriss, R.3    Heinemann, U.4
  • 4
    • 0029757154 scopus 로고    scopus 로고
    • Influence of primary sequence transpositions on the folding pathways of ribonuclease T1
    • Johnson JL, Raushel FM. Influence of primary sequence transpositions on the folding pathways of ribonuclease T1. Biochemistry. 1996;35:10223-10233.
    • (1996) Biochemistry , vol.35 , pp. 10223-10233
    • Johnson, J.L.1    Raushel, F.M.2
  • 5
    • 0028173592 scopus 로고
    • Circularly permuted dihydrofolate reductase of E coli has functional activity and a destabilized tertiary structure
    • Protasova NY, Kireeva ML, MurzLna NV, et al. Circularly permuted dihydrofolate reductase of E coli has functional activity and a destabilized tertiary structure. Prot Eng. 1994;7:1373-1377.
    • (1994) Prot Eng , vol.7 , pp. 1373-1377
    • Protasova, N.Y.1    Kireeva, M.L.2    MurzLna, N.V.3
  • 6
    • 0026516388 scopus 로고
    • A fully active variant of dihydrofolate reductase with a circularly permuted sequence
    • Buchwalder A, Szadkowski H, Kirschner K. A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry. 1992;31:1621-1630.
    • (1992) Biochemistry , vol.31 , pp. 1621-1630
    • Buchwalder, A.1    Szadkowski, H.2    Kirschner, K.3
  • 8
    • 0032005329 scopus 로고    scopus 로고
    • Crystal structures and properties of de novo circularly permuted 1,3-1,4-β-glucanases
    • Ay J, Hahn M, Decanniere K, Piotukh K, Borriss R, Heinemann U. Crystal structures and properties of de novo circularly permuted 1,3-1,4-β-glucanases. Proteins. 1998;30:155-167.
    • (1998) Proteins , vol.30 , pp. 155-167
    • Ay, J.1    Hahn, M.2    Decanniere, K.3    Piotukh, K.4    Borriss, R.5    Heinemann, U.6
  • 9
    • 0028178981 scopus 로고
    • A circularly permuted recombinant interleukin 4 toxin with increased activity
    • Kreitman RJ, Puri RK, Pastan I. A circularly permuted recombinant interleukin 4 toxin with increased activity. Proc Natl Acad Sci U S A. 1994; 91:6889-6893.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6889-6893
    • Kreitman, R.J.1    Puri, R.K.2    Pastan, I.3
  • 10
    • 0029786618 scopus 로고    scopus 로고
    • Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    • Uversky VN, Kutyshenko VP, Protasova NY, Rogov VV, Vassilenko KS, Gudkov AT. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands. Prot Sci. 1996;5:1844-1851.
    • (1996) Prot Sci , vol.5 , pp. 1844-1851
    • Uversky, V.N.1    Kutyshenko, V.P.2    Protasova, N.Y.3    Rogov, V.V.4    Vassilenko, K.S.5    Gudkov, A.T.6
  • 11
    • 0026684334 scopus 로고
    • Permuteins of interleukin 1β: A simplified approach for the construction of permuted proteins having new termini
    • Horlick RA, George HJ, Cooke GM, etal. Permuteins of interleukin 1β: a simplified approach for the construction of permuted proteins having new termini. Prot Eng. 1992;5:427-431.
    • (1992) Prot Eng , vol.5 , pp. 427-431
    • Horlick, R.A.1    George, H.J.2    Cooke, G.M.3
  • 12
    • 0027143219 scopus 로고
    • Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains
    • Ying R, Schachman HK. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. Proc Natl Acad Sci U S A. 1993;90:11980-11984.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11980-11984
    • Ying, R.1    Schachman, H.K.2
  • 13
    • 0028943593 scopus 로고
    • Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Vignais ML, Corbier C, Mulliert G. Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Prot Sci. 1995;4:994-1000.
    • (1995) Prot Sci , vol.4 , pp. 994-1000
    • Vignais, M.L.1    Corbier, C.2    Mulliert, G.3
  • 15
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera AR, Blanco FJ, Serrano L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J Mol Biol. 1995;247:670-681.
    • (1995) J Mol Biol , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 16
    • 0027264969 scopus 로고
    • In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains
    • Yang YR, Schachman HK. In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains. Prot Sci. 1993;2:1013-1023.
    • (1993) Prot Sci , vol.2 , pp. 1013-1023
    • Yang, Y.R.1    Schachman, H.K.2
  • 17
    • 0027217427 scopus 로고
    • Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains
    • Powers VM, Yang YR, Fogli MJ, Schachman HK. Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains. Prot Sci. 1993;2:1001-1012.
    • (1993) Prot Sci , vol.2 , pp. 1001-1012
    • Powers, V.M.1    Yang, Y.R.2    Fogli, M.J.3    Schachman, H.K.4
  • 18
    • 0026685018 scopus 로고
    • Stable substructures of eightfold βα-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase
    • Eder J, Kirschner K. Stable substructures of eightfold βα-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase. Biochemistry. 1992;31:3617-3625.
    • (1992) Biochemistry , vol.31 , pp. 3617-3625
    • Eder, J.1    Kirschner, K.2
  • 19
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science. 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 21
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird G, Zacharias D, Tsien R. Circular permutation and receptor insertion within green fluorescent proteins. Proc Natl Acad Sci U S A. 1999;96:11241-11246.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11241-11246
    • Baird, G.1    Zacharias, D.2    Tsien, R.3
  • 22
    • 0026550785 scopus 로고
    • A human recombinant haemoglobin designed for use as a blood substitute
    • Looker D, Abbott-Brown D, Cozart P, et al. A human recombinant haemoglobin designed for use as a blood substitute. Nature. 1992;356:258-260.
    • (1992) Nature , vol.356 , pp. 258-260
    • Looker, D.1    Abbott-Brown, D.2    Cozart, P.3
  • 23
    • 0021027685 scopus 로고
    • Structure of oxyhaemoglobin at 2.1 Å resolution
    • Shaanan B. Structure of oxyhaemoglobin at 2.1 Å resolution. J Mol Biol. 1983;171:31-59.
    • (1983) J Mol Biol , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 24
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
    • Fermi G, Perutz MF, Shaanan B. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J Mol Biol. 1984;175:159-174.
    • (1984) J Mol Biol , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shaanan, B.3
  • 25
    • 0031568811 scopus 로고    scopus 로고
    • Structures of a hemoglobin-based blood substitute: Insights into the function of allosteric proteins
    • Kroeger KS, Kundrot CE. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure. 1997;5:227-237.
    • (1997) Structure , vol.5 , pp. 227-237
    • Kroeger, K.S.1    Kundrot, C.E.2
  • 26
    • 0023494191 scopus 로고
    • Structure and stability of phage T4 lysozyme
    • Alber T, Mathews BW. Structure and stability of phage T4 lysozyme. Meth Enzymol. 1987;154:511-533.
    • (1987) Meth Enzymol , vol.154 , pp. 511-533
    • Alber, T.1    Mathews, B.W.2
  • 28
    • 0028799067 scopus 로고
    • Hemoglobin allostery: Resonance raman spectroscopy of kinetic intermediates
    • Jayaraman V, Rodgers KR, Mukerji I, Spiro TG. Hemoglobin allostery: resonance raman spectroscopy of kinetic intermediates. Science. 1995;269:1843-1848.
    • (1995) Science , vol.269 , pp. 1843-1848
    • Jayaraman, V.1    Rodgers, K.R.2    Mukerji, I.3    Spiro, T.G.4
  • 30
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side length of the penultimate amino acid
    • Hirel PH, Schmitter JM, Dessen P, Fayat G, Blanquet S. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side length of the penultimate amino acid. Proc Natl Acad Sci U S A. 1989;86:8247-8251.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, J.M.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 31
    • 0003540294 scopus 로고
    • Cambridge, United Kingdom: Cambridge University Press
    • Imai K. Allosteric Effects in Hemoglobin. Cambridge, United Kingdom: Cambridge University Press; 1982.
    • (1982) Allosteric Effects in Hemoglobin
    • Imai, K.1
  • 32
    • 0019755378 scopus 로고
    • Analysis of ligand binding equilibria
    • lmai K. Analysis of ligand binding equilibria. Meth Enzymol. 1981;76:470-486.
    • (1981) Meth Enzymol , vol.76 , pp. 470-486
    • Imai, K.1
  • 33
    • 0031586213 scopus 로고    scopus 로고
    • Conformation-invariant structures of the alpha (1) beta (1) human hemoglobin dimer
    • Nichols WL, Zimm BH, TenEyck LF. Conformation-invariant structures of the alpha (1) beta (1) human hemoglobin dimer. J Mol Biol. 1998;270:598-615.
    • (1998) J Mol Biol , vol.270 , pp. 598-615
    • Nichols, W.L.1    Zimm, B.H.2    TenEyck, L.F.3
  • 34
    • 0016243691 scopus 로고
    • Calorimetric studies of hemoglobin function, the binding of 2,3-diphosphoglycerate and inositol hexaphosphate to human hemoglobin
    • Nelson DP, Miller WD, Kiesow LA. Calorimetric studies of hemoglobin function, the binding of 2,3-diphosphoglycerate and inositol hexaphosphate to human hemoglobin. J Biol Chem. 1974;249:4770-4775.
    • (1974) J Biol Chem , vol.249 , pp. 4770-4775
    • Nelson, D.P.1    Miller, W.D.2    Kiesow, L.A.3
  • 35
    • 0016345571 scopus 로고
    • Structure of inositol hexaphosphate-human deoxy hemoglobin complex
    • Arnone A, Perutz MF. Structure of inositol hexaphosphate-human deoxy hemoglobin complex. Nature. 1974;249:34-36.
    • (1974) Nature , vol.249 , pp. 34-36
    • Arnone, A.1    Perutz, M.F.2
  • 36
    • 0017638317 scopus 로고
    • Reciprocal interaction of hemoglobin with oxygen and protons: The influence of allosteric polyanions
    • Bensch RE, Edalji R, Bensch R. Reciprocal interaction of hemoglobin with oxygen and protons: the influence of allosteric polyanions. Biochemistry. 1977;16:2594-2597.
    • (1977) Biochemistry , vol.16 , pp. 2594-2597
    • Bensch, R.E.1    Edalji, R.2    Bensch, R.3
  • 37
    • 0018720275 scopus 로고
    • The binding of chloride ions to the ligated and unligated human hemoglobin and its influence on the bohr effect
    • Beek GGMV. Zuiderweg ERR, deBruin SH. The binding of chloride ions to the ligated and unligated human hemoglobin and its influence on the bohr effect. Eur J Biochem. 1979;99:379-388.
    • (1979) Eur J Biochem , vol.99 , pp. 379-388
    • Beek, G.G.M.V.1    Zuiderweg, E.R.R.2    DeBruin, S.H.3
  • 39
    • 0018868084 scopus 로고
    • Role of the β146 histidyl residue in the alkaline Bohr effect of hemoglobin
    • Russu IM, Ho TN, Ho C. Role of the β146 histidyl residue in the alkaline Bohr effect of hemoglobin. Biochemistry. 1980;19:1043-1047.
    • (1980) Biochemistry , vol.19 , pp. 1043-1047
    • Russu, I.M.1    Ho, T.N.2    Ho, C.3
  • 40
    • 0014693848 scopus 로고
    • 2 combination and reduction of the Bohr effect in hemoglobin chemically modified at the α-amino group
    • 2 combination and reduction of the Bohr effect in hemoglobin chemically modified at the α-amino group. Nature. 1969;222:1243-1246.
    • (1969) Nature , vol.222 , pp. 1243-1246
    • Kilmartin, J.V.1    Rossi-Bernardi, L.2
  • 41
    • 0015606667 scopus 로고
    • Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin
    • Kilmartin JV, Breen JJ, Roberts GCK, Ho C. Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin. Proc Natl Acad Sci U S A. 1973;70:1246-1249.
    • (1973) Proc Natl Acad Sci U S A , vol.70 , pp. 1246-1249
    • Kilmartin, J.V.1    Breen, J.J.2    Roberts, G.C.K.3    Ho, C.4
  • 43
    • 0030979555 scopus 로고    scopus 로고
    • Circular permutations of natural protein sequences: Structural evidence
    • Lindqvist Y, Schneider G. Circular permutations of natural protein sequences: structural evidence. Curr Opin Struct Biol. 1997;7:422-427.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 422-427
    • Lindqvist, Y.1    Schneider, G.2
  • 45
    • 0026737980 scopus 로고
    • Human hemoglobin expression in Escherichia coli: Importance of optimal codon usage
    • Hernan RA, Hui HL,Andracki ME, et al. Human hemoglobin expression in Escherichia coli: importance of optimal codon usage. Biochemistry. 1992;31:8619-8628.
    • (1992) Biochemistry , vol.31 , pp. 8619-8628
    • Hernan, R.A.1    Hui, H.L.2    Andracki, M.E.3
  • 46
    • 0026745130 scopus 로고
    • Functional properties of human hemoglobin synthesized from recombinant β-globin
    • Doyle ML, Lew G, Young AD, et al. Functional properties of human hemoglobin synthesized from recombinant β-globin. Biochemistry. 1992;31:8629-8639.
    • (1992) Biochemistry , vol.31 , pp. 8629-8639
    • Doyle, M.L.1    Lew, G.2    Young, A.D.3
  • 47
    • 0030746342 scopus 로고    scopus 로고
    • Role of the hemA gene product and 8-aminolevuliinic acid in regulation of Escherichia coli heme synthesis
    • Verderber E, Lucast LJ, VanDehy JA, Cozart P, Etter JB, Best EA. Role of the hemA gene product and 8-aminolevuliinic acid in regulation of Escherichia coli heme synthesis. J Bacteriol. 1997;179:4583-4590.
    • (1997) J Bacteriol , vol.179 , pp. 4583-4590
    • Verderber, E.1    Lucast, L.J.2    VanDehy, J.A.3    Cozart, P.4    Etter, J.B.5    Best, E.A.6
  • 48
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman P, Begg G. A protein sequenator. Eur J Biochem. 1967;1:80-91.
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 49
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (pyridine hemochromogen)
    • Paul K, Theorell H, Akeson A. The molar light absorption of pyridine ferroprotoporphyrin (pyridine hemochromogen). Acta Chem Scand. 1953;7:1284-1287.
    • (1953) Acta Chem Scand , vol.7 , pp. 1284-1287
    • Paul, K.1    Theorell, H.2    Akeson, A.3
  • 50
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of the protein conformation
    • Greenfield N, Fasman GD. Computed circular dichroism spectra for the evaluation of the protein conformation. Biochemistry. 1969;8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 51
    • 0015790339 scopus 로고
    • An enzymatic reduction system for metmyoglobin and methemoglobin and its application to functional studies of oxygen carriers
    • Hayashi A, Suzuki T, Masateru T. An enzymatic reduction system for metmyoglobin and methemoglobin and its application to functional studies of oxygen carriers. Biochem Biophys Acta. 1973;310:309-316.
    • (1973) Biochem Biophys Acta , vol.310 , pp. 309-316
    • Hayashi, A.1    Suzuki, T.2    Masateru, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.