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Volumn 274, Issue 22, 2007, Pages 5826-5833

Identification of three phases in Onconase refolding

Author keywords

Intermediate; Onconase; Proline isomerization; Protein folding; Reactivation

Indexed keywords

GUANIDINE; PEPTIDYLPROLYL ISOMERASE; RANPIRNASE; RIBONUCLEASE A;

EID: 35748985538     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06106.x     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 0025020007 scopus 로고
    • Striking increase of survival of mice bearing M109 Madison carcinoma treated with a novel protein from amphibian embryos
    • Mikulski SM, Ardelt W, Shogen K, Bernstein EH Menduke H (1990) Striking increase of survival of mice bearing M109 Madison carcinoma treated with a novel protein from amphibian embryos. J Natl Cancer Inst 82, 151 153.
    • (1990) J Natl Cancer Inst , vol.82 , pp. 151-153
    • Mikulski, S.M.1    Ardelt, W.2    Shogen, K.3    Bernstein, E.H.4    Menduke, H.5
  • 2
    • 0028266432 scopus 로고
    • Refined 1.7 a X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity
    • Mosimann SC, Ardelt W James MN (1994) Refined 1.7 A X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity. J Mol Biol 236, 1141 1153.
    • (1994) J Mol Biol , vol.236 , pp. 1141-1153
    • Mosimann, S.C.1    Ardelt, W.2    James, M.N.3
  • 3
    • 0027256672 scopus 로고
    • A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity
    • Wu Y, Mikulski SM, Ardelt W, Rybak SM Youle RJ (1993) A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity. J Biol Chem 268, 10686 10693.
    • (1993) J Biol Chem , vol.268 , pp. 10686-10693
    • Wu, Y.1    Mikulski, S.M.2    Ardelt, W.3    Rybak, S.M.4    Youle, R.J.5
  • 4
    • 0037407561 scopus 로고    scopus 로고
    • ONCONASE and its therapeutic potential
    • Saxena SK, Shogen K Ardelt W (2003) ONCONASE and its therapeutic potential. Lab Med 34, 380 387.
    • (2003) Lab Med , vol.34 , pp. 380-387
    • Saxena, S.K.1    Shogen, K.2    Ardelt, W.3
  • 5
    • 33748536073 scopus 로고    scopus 로고
    • Natural and engineered ribonucleases as potential cancer therapeutics
    • Arnold U Ulbrich-Hofmann R (2006) Natural and engineered ribonucleases as potential cancer therapeutics. Biotechnol Lett 28, 1615 1622.
    • (2006) Biotechnol Lett , vol.28 , pp. 1615-1622
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 6
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease a
    • Raines RT (1998) Ribonuclease A. Chem Rev 98, 1045 1066.
    • (1998) Chem Rev , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 7
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts JF, Halvorson HR Brennan M (1975) Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953 4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 8
    • 0039224962 scopus 로고
    • Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease
    • Schmid FX, Grafl R, Wrba A Beintema JJ (1986) Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease. Proc Natl Acad Sci USA 83, 872 876.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 872-876
    • Schmid, F.X.1    Grafl, R.2    Wrba, A.3    Beintema, J.J.4
  • 9
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • Wedemeyer WJ, Welker E Scheraga HA (2002) Proline cis-trans isomerization and protein folding. Biochemistry 41, 14637 14644.
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 10
    • 33645225294 scopus 로고    scopus 로고
    • Contribution of structural peculiarities of onconase to its high stability and folding kinetics
    • Arnold U, Schulenburg C, Schmidt D Ulbrich-Hofmann R (2006) Contribution of structural peculiarities of onconase to its high stability and folding kinetics. Biochemistry 45, 3580 3587.
    • (2006) Biochemistry , vol.45 , pp. 3580-3587
    • Arnold, U.1    Schulenburg, C.2    Schmidt, D.3    Ulbrich-Hofmann, R.4
  • 11
    • 33748286745 scopus 로고    scopus 로고
    • Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family
    • Pradeep L, Shin HC Scheraga HA (2006) Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family. FEBS Lett 580, 5029 5032.
    • (2006) FEBS Lett , vol.580 , pp. 5029-5032
    • Pradeep, L.1    Shin, H.C.2    Scheraga, H.A.3
  • 13
    • 0035822616 scopus 로고    scopus 로고
    • Contribution of chain termini to the conformational stability and biological activity of onconase
    • Notomista E, Catanzano F, Graziano G, Di Gaetano S, Barone G Di Donato A (2001) Contribution of chain termini to the conformational stability and biological activity of onconase. Biochemistry 40, 9097 9103.
    • (2001) Biochemistry , vol.40 , pp. 9097-9103
    • Notomista, E.1    Catanzano, F.2    Graziano, G.3    Di Gaetano, S.4    Barone, G.5    Di Donato, A.6
  • 15
    • 33646095781 scopus 로고    scopus 로고
    • Tandemization endows bovine pancreatic ribonuclease with cytotoxic activity
    • Leich F, Köditz J, Ulbrich-Hofman R Arnold U (2006) Tandemization endows bovine pancreatic ribonuclease with cytotoxic activity. J Mol Biol 358, 1305 1313.
    • (2006) J Mol Biol , vol.358 , pp. 1305-1313
    • Leich, F.1    Köditz, J.2    Ulbrich-Hofman, R.3    Arnold, U.4
  • 16
    • 0027049568 scopus 로고
    • Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation
    • Schultz DA, Schmid FX Baldwin RL (1992) Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci 1, 917 924.
    • (1992) Protein Sci , vol.1 , pp. 917-924
    • Schultz, D.A.1    Schmid, F.X.2    Baldwin, R.L.3
  • 17
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson SE Fersht AR (1991) Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428 10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 18
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • Parker MJ Marqusee S (1999) The cooperativity of burst phase reactions explored. J Mol Biol 293, 1195 1210.
    • (1999) J Mol Biol , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 19
    • 0002203625 scopus 로고    scopus 로고
    • Kinetic models in protein folding
    • In. Pain, R.H., ed.), pp. Oxford University Press, Oxford.
    • Bieri O Kiefhaber T (2000) Kinetic models in protein folding. In Mechanisms of Protein Folding (Pain RH, ed.), pp. 34 64. Oxford University Press, Oxford.
    • (2000) Mechanisms of Protein Folding , pp. 34-64
    • Bieri, O.1    Kiefhaber, T.2
  • 21
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki LS, Evans PA, Dobson CM Radford SE (1994) Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 33, 5212 5220.
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 23
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G (1990) WHAT IF: a molecular modeling and drug design program. J Mol Graph 8, 52 56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 24
    • 0032847748 scopus 로고    scopus 로고
    • Elementary steps in protein folding
    • Bieri O Kiefhaber T (1999) Elementary steps in protein folding. Biol Chem 380, 923 929.
    • (1999) Biol Chem , vol.380 , pp. 923-929
    • Bieri, O.1    Kiefhaber, T.2
  • 25
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim PS Baldwin RL (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Bochem 51, 459 489.
    • (1982) Annu Rev Bochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 26
    • 0028387381 scopus 로고
    • Finding intermediates in protein folding
    • Baldwin RL (1994) Finding intermediates in protein folding. Bioessays 16, 207 210.
    • (1994) Bioessays , vol.16 , pp. 207-210
    • Baldwin, R.L.1
  • 27
    • 0015715985 scopus 로고
    • Both the fast and slow refolding reactions of ribonuclease a yield native enzyme
    • Garel JR Baldwin RL (1973) Both the fast and slow refolding reactions of ribonuclease A yield native enzyme. Proc Natl Acad Sci USA 70, 3347 3351.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 3347-3351
    • Garel, J.R.1    Baldwin, R.L.2
  • 28
    • 0019406826 scopus 로고
    • A native-like intermediate on the ribonuclease a folding pathway. 2. Comparison of its properties to native ribonuclease a
    • Schmid FX Blaschek H (1981) A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. Eur J Biochem 114, 111 117.
    • (1981) Eur J Biochem , vol.114 , pp. 111-117
    • Schmid, F.X.1    Blaschek, H.2
  • 29
    • 0018556595 scopus 로고
    • Role of proline isomerization in folding of ribonuclease a at low temperatures
    • Cook KH, Schmid FX Baldwin RL (1979) Role of proline isomerization in folding of ribonuclease A at low temperatures. Proc Natl Acad Sci USA 76, 6157 6161.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6157-6161
    • Cook, K.H.1    Schmid, F.X.2    Baldwin, R.L.3
  • 30
    • 0022547669 scopus 로고
    • Proline isomerization during refolding of ribonuclease a is accelerated by the presence of folding intermediates
    • Schmid FX (1986) Proline isomerization during refolding of ribonuclease A is accelerated by the presence of folding intermediates. FEBS Lett 198, 217 220.
    • (1986) FEBS Lett , vol.198 , pp. 217-220
    • Schmid, F.X.1
  • 31
    • 0029864379 scopus 로고    scopus 로고
    • Collapse and cooperativity in protein folding
    • Miranker AD Dobson CM (1996) Collapse and cooperativity in protein folding. Curr Opin Struct Biol 6, 31 42.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 31-42
    • Miranker, A.D.1    Dobson, C.M.2
  • 32
    • 0032515910 scopus 로고    scopus 로고
    • Single amino acid substitutions at the N-terminus of a recombinant cytotoxic ribonuclease markedly influence biochemical and biological properties
    • Newton DL, Boque L, Wlodawer A, Huang CY Rybak SM (1998) Single amino acid substitutions at the N-terminus of a recombinant cytotoxic ribonuclease markedly influence biochemical and biological properties. Biochemistry 37, 5173 5183.
    • (1998) Biochemistry , vol.37 , pp. 5173-5183
    • Newton, D.L.1    Boque, L.2    Wlodawer, A.3    Huang, C.Y.4    Rybak, S.M.5
  • 33
    • 0141483327 scopus 로고    scopus 로고
    • Contribution of active-site residues to the function of onconase, a ribonuclease with antitumoral activity
    • Lee JE Raines RT (2003) Contribution of active-site residues to the function of onconase, a ribonuclease with antitumoral activity. Biochemistry 42, 11443 11450.
    • (2003) Biochemistry , vol.42 , pp. 11443-11450
    • Lee, J.E.1    Raines, R.T.2
  • 34
    • 0022430422 scopus 로고
    • The refolding of urea-denatured ribonuclease a is catalyzed by peptidyl-prolyl cis-trans isomerase
    • Fischer G Bang H (1985) The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase. Biochim Biophys Acta 828, 39 42.
    • (1985) Biochim Biophys Acta , vol.828 , pp. 39-42
    • Fischer, G.1    Bang, H.2
  • 35
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T Schmid FX (1989) Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476 478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 37
    • 0025005004 scopus 로고
    • Mechanistic studies of peptidyl prolyl cis-trans isomerase: Evidence for catalysis by distortion
    • Harrison RK Stein RL (1990) Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion. Biochemistry 29, 1684 1689.
    • (1990) Biochemistry , vol.29 , pp. 1684-1689
    • Harrison, R.K.1    Stein, R.L.2
  • 38
    • 0023655832 scopus 로고
    • The analysis of enzyme progress curves by numerical differentiation, including competitive product inhibition and enzyme reactivation
    • Koerber SC Fink AL (1987) The analysis of enzyme progress curves by numerical differentiation, including competitive product inhibition and enzyme reactivation. Anal Biochem 165, 75 87.
    • (1987) Anal Biochem , vol.165 , pp. 75-87
    • Koerber, S.C.1    Fink, A.L.2


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