메뉴 건너뛰기




Volumn 278, Issue 7, 2011, Pages 1137-1144

Acceleration of disulfide-coupled protein folding using glutathione derivatives

Author keywords

arginine; disulfide; folding; glutathione; uroguanylin

Indexed keywords

ARGINYLCYSTEINYLGLYCINE; GLUTAMIC ACID; GLUTAMYLCYSTEINYLARGININE; GLUTATHIONE; GLUTATHIONE DERIVATIVE; GLUTATHIONE DISULFIDE; LYSOZYME; PROUROGUANYLIN; UNCLASSIFIED DRUG; UROGUANYLIN;

EID: 79952845544     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08039.x     Document Type: Article
Times cited : (48)

References (26)
  • 1
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF, (1990) Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63, 69-172.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 2
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, &, Lodish HF, (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 3
    • 0020482340 scopus 로고
    • Regeneration of ribonuclease A from the reduced protein. Rate-limiting steps
    • Konishi Y, Ooi T, &, Scheraga HA, (1982) Regeneration of ribonuclease A from the reduced protein. Rate-limiting steps. Biochemistry 21, 4734-4740.
    • (1982) Biochemistry , vol.21 , pp. 4734-4740
    • Konishi, Y.1    Ooi, T.2    Scheraga, H.A.3
  • 4
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles MM, &, Gilbert HF, (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 5
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • DOI 10.1016/j.tibs.2006.03.005, PII S096800040600082X
    • Arolas JL, Aviles FX, Chang JY, &, Ventura S, (2006) Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci 31, 292-301. (Pubitemid 43674360)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.5 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.-Y.3    Ventura, S.4
  • 6
    • 0040786272 scopus 로고    scopus 로고
    • Disulfide bonds and protein folding
    • DOI 10.1021/bi992922o
    • Wedemeyer WJ, Welker E, Narayan M, &, Scheraga HA, (2000) Disulfide bonds and protein folding. Biochemistry 39, 4207-4216. (Pubitemid 30212634)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4207-4216
    • Wedemeyer, W.J.1    Welker, E.2    Narayan, M.3    Scheraga, H.A.4
  • 7
    • 0027434035 scopus 로고
    • The disulfide folding pathway of hirudin elucidated by stop/go folding experiments
    • Chatrenet B, &, Chang JY, (1993) The disulfide folding pathway of hirudin elucidated by stop/go folding experiments. J Biol Chem 268, 20988-20996. (Pubitemid 23292280)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.28 , pp. 20988-20996
    • Chatrenet, B.1    Chang, J.-Y.2
  • 8
    • 34248137560 scopus 로고    scopus 로고
    • Selenoglutathione: Efficient oxidative protein folding by a diselenide
    • DOI 10.1021/bi700124p
    • Beld J, Woycechowsky KJ, &, Hilvert D, (2007) Selenoglutathione: efficient protein folding by a diselenide. Biochemistry 46, 5382-5390. (Pubitemid 46717263)
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5382-5390
    • Beld, J.1    Woycechowsky, K.J.2    Hilvert, D.3
  • 10
    • 0036774673 scopus 로고    scopus 로고
    • Biophysical effect of amino acids on the prevention of protein aggregation
    • Shiraki K, Kudou M, Fuziwara S, Imanaka T, &, Takagi M, (2002) Biophysical effect of amino acids on the prevention of protein aggregation. J Biochem 132, 591-595. (Pubitemid 35238913)
    • (2002) Journal of Biochemistry , vol.132 , Issue.4 , pp. 591-595
    • Shiraki, K.1    Kudou, M.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 11
    • 15244343628 scopus 로고    scopus 로고
    • L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
    • DOI 10.1110/ps.041085005
    • Reddy KRC, Lilie H, Rudolph R, &, Lange C, (2005) L-Arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci 14, 929-935. (Pubitemid 40389362)
    • (2005) Protein Science , vol.14 , Issue.4 , pp. 929-935
    • Reddy, K.R.C.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 12
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: Not facilitate refolding, but suppress aggregation
    • DOI 10.1016/S0006-291X(03)00578-3
    • Arakawa T, &, Tsumoto K, (2003) The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem Biophys Res Commun 304, 148-152. (Pubitemid 36434209)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.1 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 13
    • 0013001642 scopus 로고    scopus 로고
    • How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system: Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment
    • DOI 10.1074/jbc.M212247200
    • Umetsu M, Tsumoto K, Hara M, Ashish K, Goto S, Adschiri T, &, Kumagai I, (2003) How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment. J Biol Chem 278, 8979-8987. (Pubitemid 36800375)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 8979-8987
    • Umetsu, M.1    Tsumoto, K.2    Hara, M.3    Ashish, K.4    Goda, S.5    Adschiri, T.6    Kumagai, I.7
  • 14
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - Application to a human single-chain Fv fragment
    • DOI 10.1016/S0022-1759(98)00127-6, PII S0022175998001276
    • Tsumoto K, Shinoki K, Kondo H, Uchikawa M, Juji T, &, Kumagai I, (1998) Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagents-application to a human single-chain Fv fragment. J Immunol Methods 219, 119-129. (Pubitemid 28513157)
    • (1998) Journal of Immunological Methods , vol.219 , Issue.1-2 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3    Uchikawa, M.4    Juji, T.5    Kumagai, I.6
  • 15
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. l. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena VP, &, Wetlaufer DB, (1970) Formation of three-dimensional structure in proteins. l. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9, 5015-5023.
    • (1970) Biochemistry , vol.9 , pp. 5015-5023
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 16
    • 0018791296 scopus 로고
    • Intermediates in the refolding of reduced ribonuclease A
    • Creighton TE, (1979) Intermediates in the refolding of reduced ribonuclease A. J Mol Biol 129, 411-431.
    • (1979) J Mol Biol , vol.129 , pp. 411-431
    • Creighton, T.E.1
  • 17
    • 0030054978 scopus 로고    scopus 로고
    • Refolding of denatured and denatured/reduced lysozyme at high concentrations
    • DOI 10.1074/jbc.271.29.17067
    • Raman B, Ramakrishna T, &, Rao CM, (1996) Refolding of denatured and denatured/reduced lysozyme at high concentrations. J Biol Chem 271, 17067-17072. (Pubitemid 26244254)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17067-17072
    • Raman, B.1    Ramakrishna, T.2    Rao, Ch.M.3
  • 18
    • 0033199237 scopus 로고    scopus 로고
    • The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase
    • DOI 10.1093/emboj/18.17.4794
    • Van den Berg B, Chung EW, Robinson CV, Mateo PL, &, Dobson CM, (1999) The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J 18, 4794-4803. (Pubitemid 29415532)
    • (1999) EMBO Journal , vol.18 , Issue.17 , pp. 4794-4803
    • Van Den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Mateo, P.L.4    Dobson, C.M.5
  • 19
    • 0034682765 scopus 로고    scopus 로고
    • Dual function of the propeptide of prouroguanylin in the folding of the mature peptide: Disulfide-coupled folding and dimerization
    • Hidaka Y, Shimono C, Ohno M, Okumura N, Knut A, Wolf-Georg F, &, Shimonoshi Y, (2000) Dual function of the propeptide of prouroguanylin in the folding of the mature peptide: disulfide-coupled folding and dimerization. J Biol Chem 275, 25155-25162.
    • (2000) J Biol Chem , vol.275 , pp. 25155-25162
    • Hidaka, Y.1    Shimono, C.2    Ohno, M.3    Okumura, N.4    Knut, A.5    Wolf-Georg, F.6    Shimonoshi, Y.7
  • 20
    • 0030797806 scopus 로고    scopus 로고
    • Protein folding coupled to disulphide bond formation
    • Creighton TE, (1997) Protein folding coupled to disulphide bond formation. Biol Chem 378, 731-744. (Pubitemid 27388932)
    • (1997) Biological Chemistry , vol.378 , Issue.8 , pp. 731-744
    • Creighton, T.E.1
  • 21
    • 0032499632 scopus 로고    scopus 로고
    • In vitro disulfide-coupled folding of guanylyl cyclase-activating peptide and its precursor protein
    • DOI 10.1021/bi9731246
    • Hidaka Y, Ohno M, Hemmasi B, Hill O, Forssmann WG, &, Shimonishi Y, (1998) In vitro disulfide-coupled folding of guanylyl cyclase-activating peptide and its precursor proteins. Biochemistry 37, 8498-8507. (Pubitemid 28275469)
    • (1998) Biochemistry , vol.37 , Issue.23 , pp. 8498-8507
    • Hidaka, Y.1    Ohno, M.2    Hemmasi, B.3    Hill, O.4    Forssmann, W.-G.5    Shimonishi, Y.6
  • 22
    • 0028267293 scopus 로고
    • Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: Evidence for two independent reactions
    • Ybe JA, &, Kahn PC, (1994) Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactions. Protein Sci 3, 638-649. (Pubitemid 24136369)
    • (1994) Protein Science , vol.3 , Issue.4 , pp. 638-649
    • Ybe, J.A.1    Kahn, P.C.2
  • 23
    • 0019877708 scopus 로고
    • Electrostatic influence of local cysteine environments on disulfide exchange kinetics
    • Snyder GH, Cennerazzo MJ, Karalis AJ, &, Field D, (1981) Electrostatic influence of local cysteine environments on disulfide exchange kinetics. Biochemistry 20, 6509-6519.
    • (1981) Biochemistry , vol.20 , pp. 6509-6519
    • Snyder, G.H.1    Cennerazzo, M.J.2    Karalis, A.J.3    Field, D.4
  • 24
    • 35848936302 scopus 로고    scopus 로고
    • L-arginine suppresses aggregation of recombinant growth hormones in refolding process from E. coli inclusion bodies
    • DOI 10.1007/s10930-007-9096-x
    • Bajorunaite E, Sereikaite J, &, Bumelis VA, (2007) l-arginine suppresses aggregation of recombinant hormones in refolding process from E. coli inclusion bodies. Protein J 26, 547-555. (Pubitemid 350060771)
    • (2007) Protein Journal , vol.26 , Issue.8 , pp. 547-555
    • Bajorunaite, E.1    Sereikaite, J.2    Bumelis, V.-A.3
  • 25
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J, &, Rudolph R, (1991) Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology, 9, 157-162.
    • (1991) Biotechnology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 26
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman JS, &, Kim PS, (1991) Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393. (Pubitemid 21917286)
    • (1991) Science , vol.253 , Issue.5026 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.