메뉴 건너뛰기




Volumn 10, Issue 6, 2009, Pages 614-625

The role of thiols and disulfides on protein stability

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DITHIODIPYRIDINE; CYSTEINE; EPTIFIBATIDE; GLUTATHIONE; OXYTOCIN; SUBTILISIN; SUPEROXIDE DISMUTASE; THIOL; THIOREDOXIN;

EID: 73549100208     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920309789630534     Document Type: Article
Times cited : (319)

References (84)
  • 1
    • 73549093664 scopus 로고    scopus 로고
    • Bio Approved biotechnology drugs. Guide to Biotechnology, 2007, http://www.bio.org/speeches/pubs/er/.
    • Bio Approved biotechnology drugs. Guide to Biotechnology, 2007, http://www.bio.org/speeches/pubs/er/.
  • 2
    • 73549112270 scopus 로고    scopus 로고
    • The market for bioengineered protein drugs
    • Cyran, R. The market for bioengineered protein drugs. BCC Research Reports and Reviews, 2004, http://www.bccresearch.com.
    • (2004) BCC Research Reports and Reviews
    • Cyran, R.1
  • 3
    • 18044400215 scopus 로고    scopus 로고
    • Comparison of the rates of deamidation, diketopiperazine formation and oxidation in recombinant human vascular endothelial growth factor and model peptides
    • Goolcharran, C.; Cleland, J.L.; Keck, R.; Jones, A.J.; Borchardt, R.T. Comparison of the rates of deamidation, diketopiperazine formation and oxidation in recombinant human vascular endothelial growth factor and model peptides. AAPS PharmSci., 2000, 2, E5.
    • (2000) AAPS PharmSci , vol.2
    • Goolcharran, C.1    Cleland, J.L.2    Keck, R.3    Jones, A.J.4    Borchardt, R.T.5
  • 4
    • 0033817051 scopus 로고    scopus 로고
    • The effects of a histidine residue on the C-terminal side of an asparaginyl residue on the rate of deamidation using model pentapeptides
    • Goolcharran, C.; Stauffer, L.L.; Cleland, J.L.; Borchardt, R.T. The effects of a histidine residue on the C-terminal side of an asparaginyl residue on the rate of deamidation using model pentapeptides. J. Pharm. Sci., 2000, 89, 818-825.
    • (2000) J. Pharm. Sci , vol.89 , pp. 818-825
    • Goolcharran, C.1    Stauffer, L.L.2    Cleland, J.L.3    Borchardt, R.T.4
  • 5
    • 0032881295 scopus 로고    scopus 로고
    • Chemical stability of peptides in polymers. 2. Discriminating between solvent and plasticizing effects of water on peptide deamidation in poly(vinylpyrrolidone)
    • Lai, M.C.; Hageman, M.J.; Schowen, R.L.; Borchardt, R.T.; Laird, B.B.; Topp, E.M. Chemical stability of peptides in polymers. 2. Discriminating between solvent and plasticizing effects of water on peptide deamidation in poly(vinylpyrrolidone). J. Pharm. Sci., 1999, 88, 1081-1089.
    • (1999) J. Pharm. Sci , vol.88 , pp. 1081-1089
    • Lai, M.C.1    Hageman, M.J.2    Schowen, R.L.3    Borchardt, R.T.4    Laird, B.B.5    Topp, E.M.6
  • 6
    • 0029665540 scopus 로고    scopus 로고
    • Effects of polyaminocarboxylate metal chelators on iron-thiolate induced oxidation of methionineand histidine-containing peptides
    • Zhao, F.; Yang, J.; Schoneich, C. Effects of polyaminocarboxylate metal chelators on iron-thiolate induced oxidation of methionineand histidine-containing peptides. Pharm. Res., 1996, 13, 931-938.
    • (1996) Pharm. Res , vol.13 , pp. 931-938
    • Zhao, F.1    Yang, J.2    Schoneich, C.3
  • 7
    • 0029969392 scopus 로고    scopus 로고
    • Oxidative modification of a carboxylterminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase
    • Yao, Y.; Yin, D.; Jas, G.S.; Kuczera, K.; Williams, T.D.; Schoneich, C.; Squier, T.C. Oxidative modification of a carboxylterminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. Biochemistry, 1996, 35, 2767-2787.
    • (1996) Biochemistry , vol.35 , pp. 2767-2787
    • Yao, Y.1    Yin, D.2    Jas, G.S.3    Kuczera, K.4    Williams, T.D.5    Schoneich, C.6    Squier, T.C.7
  • 8
    • 0029028559 scopus 로고
    • Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation
    • Li, S.; Nguyen, T.H.; Schoneich, C.; Borchardt, R.T. Aggregation and precipitation of human relaxin induced by metal-catalyzed oxidation. Biochemistry, 1995, 34, 5762-5772.
    • (1995) Biochemistry , vol.34 , pp. 5762-5772
    • Li, S.1    Nguyen, T.H.2    Schoneich, C.3    Borchardt, R.T.4
  • 9
  • 12
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar, A.A.; Borchardt, R.T. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J. Pharm. Sci., 2006, 95, 2321-2336.
    • (2006) J. Pharm. Sci , vol.95 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 14
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura, H.; Katzen, F.; Beckwith, J. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem., 2003, 72, 111-135.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 15
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand, A.R.; Cuozzo, J.W.; Kaiser, C.A. Pathways for protein disulphide bond formation. Trends Cell Biol., 2000, 10, 203-210.
    • (2000) Trends Cell Biol , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 16
    • 33745861722 scopus 로고    scopus 로고
    • Conservation and diversity of the cellular disulfide bond formation pathways
    • Sevier, C.S.; Kaiser, C.A. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid. Redox Signal, 2006, 8, 797-811.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 797-811
    • Sevier, C.S.1    Kaiser, C.A.2
  • 17
    • 33644868738 scopus 로고    scopus 로고
    • Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation
    • Kulp, M.S.; Frickel, E.M.; Ellgaard, L.; Weissman, J.S. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J. Biol. Chem., 2006, 281, 876-884.
    • (2006) J. Biol. Chem , vol.281 , pp. 876-884
    • Kulp, M.S.1    Frickel, E.M.2    Ellgaard, L.3    Weissman, J.S.4
  • 18
    • 0041761699 scopus 로고    scopus 로고
    • Genomics perspective on disulfide bond formation
    • Fomenko, D.E.; Gladyshev, V.N. Genomics perspective on disulfide bond formation. Antioxid. Redox Signal., 2003, 5, 397-402.
    • (2003) Antioxid. Redox Signal , vol.5 , pp. 397-402
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 20
    • 0028818785 scopus 로고
    • A kinetic explanation for the rearrangement pathway of BPTI folding
    • Weissman, J.S.; Kim, P.S. A kinetic explanation for the rearrangement pathway of BPTI folding. Nat. Struct. Biol., 1995, 2, 1123-1130.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 1123-1130
    • Weissman, J.S.1    Kim, P.S.2
  • 21
    • 0029098928 scopus 로고
    • A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor
    • Dadlez, M.; Kim, P.S. A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor. Nat. Struct. Biol., 1995, 2, 674-679.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 674-679
    • Dadlez, M.1    Kim, P.S.2
  • 22
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • Arolas, J.L.; Aviles, F.X.; Chang, J.Y.; Ventura, S. Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem. Sci., 2006, 31, 292-301.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.Y.3    Ventura, S.4
  • 23
    • 0041987555 scopus 로고    scopus 로고
    • Conformational analysis of intermediates involved in the in vitro folding pathways of recombinant human macrophage colony stimulating factor beta by sulfhydryl group trapping and hydrogen/ deuterium pulsed labeling
    • Zhang, Y.H.; Yan, X.; Maier, C.S.; Schimerlik, M.I.; Deinzer, M.L. Conformational analysis of intermediates involved in the in vitro folding pathways of recombinant human macrophage colony stimulating factor beta by sulfhydryl group trapping and hydrogen/ deuterium pulsed labeling. Biochemistry, 2002, 41, 15495-15504.
    • (2002) Biochemistry , vol.41 , pp. 15495-15504
    • Zhang, Y.H.1    Yan, X.2    Maier, C.S.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 24
    • 0034819513 scopus 로고    scopus 로고
    • Oxidative folding of murine prion mPrP(23-231)
    • Lu, B.-Y.; Beck, P.J.; Chang, J.-Y. Oxidative folding of murine prion mPrP(23-231). Eur. J. Biochem., 2001, 268, 3767-3773.
    • (2001) Eur. J. Biochem , vol.268 , pp. 3767-3773
    • Lu, B.-Y.1    Beck, P.J.2    Chang, J.-Y.3
  • 25
    • 2542483890 scopus 로고    scopus 로고
    • The role of disulfide bonds in the conformational stability and catalytic activity of phytase
    • Wang, X.-Y.; Meng, F.-G.; Zhou, H.-M. The role of disulfide bonds in the conformational stability and catalytic activity of phytase. Biochem. Cell Biol., 2004, 82, 329-334.
    • (2004) Biochem. Cell Biol , vol.82 , pp. 329-334
    • Wang, X.-Y.1    Meng, F.-G.2    Zhou, H.-M.3
  • 26
    • 0037013987 scopus 로고    scopus 로고
    • Reductive unfolding and oxidative refolding of a Bowman-Birk inhibitor from horsegram seeds (Dolichos biflorus): Evidence for 'hyperreactive' disulfide bonds and rate-limiting nature of disulfide isomerization in folding
    • Singh, R.R.; Appu Rao, A.G. Reductive unfolding and oxidative refolding of a Bowman-Birk inhibitor from horsegram seeds (Dolichos biflorus): evidence for 'hyperreactive' disulfide bonds and rate-limiting nature of disulfide isomerization in folding. Biochim. Biophys. Acta, 2002, 1597, 280-291.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 280-291
    • Singh, R.R.1    Appu Rao, A.G.2
  • 27
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation
    • Voss, R.H.; Ermler, U.; Essen, L.-O.; Wenzl, G.; Kim, Y.-M.; Flecker, P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. Eur. J. Biochem., 1996, 242, 122-131.
    • (1996) Eur. J. Biochem , vol.242 , pp. 122-131
    • Voss, R.H.1    Ermler, U.2    Essen, L.-O.3    Wenzl, G.4    Kim, Y.-M.5    Flecker, P.6
  • 28
    • 0025232324 scopus 로고
    • Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease
    • Takagi, H.; Takahashi, T.; Momose, H.; Inouye, M.; Maeda, Y.; Matsuzawa, H.; Ohta, T. Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease. J. Biol. Chem., 1990, 265, 6874-6878.
    • (1990) J. Biol. Chem , vol.265 , pp. 6874-6878
    • Takagi, H.1    Takahashi, T.2    Momose, H.3    Inouye, M.4    Maeda, Y.5    Matsuzawa, H.6    Ohta, T.7
  • 31
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
    • Pace, C.N.; Grimsley, G.R.; Thomson, J.A.; Barnett, B.J. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem., 1988, 263, 11820-11825.
    • (1988) J. Biol. Chem , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Barnett, B.J.4
  • 32
    • 34347355574 scopus 로고    scopus 로고
    • Thermodynamic effects of disulfide bond on thermal unfolding of the starch-binding domain of Aspergillus niger glucoamylase
    • Sugimoto, H.; Nakaura, M.; Kosuge, Y.; Imai, K.; Miyake, H.; Karita, S.; Tanaka, A. Thermodynamic effects of disulfide bond on thermal unfolding of the starch-binding domain of Aspergillus niger glucoamylase. Biosci. Biotechnol. Biochem., 2007, 71, 1535-1541.
    • (2007) Biosci. Biotechnol. Biochem , vol.71 , pp. 1535-1541
    • Sugimoto, H.1    Nakaura, M.2    Kosuge, Y.3    Imai, K.4    Miyake, H.5    Karita, S.6    Tanaka, A.7
  • 33
    • 33846330197 scopus 로고    scopus 로고
    • Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds
    • Davoodi, J.; Wakarchuk, W.W.; Carey, P.R.; Surewicz, W.K. Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds. Biophys. Chem., 2007, 125, 453-461.
    • (2007) Biophys. Chem , vol.125 , pp. 453-461
    • Davoodi, J.1    Wakarchuk, W.W.2    Carey, P.R.3    Surewicz, W.K.4
  • 35
    • 34249882805 scopus 로고    scopus 로고
    • Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase
    • Asgeirsson, B.; Adalbjornsson, B.V.; Gylfason, G.A. Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase. Biochim. Biophys. Acta, 2007, 1774, 679-687.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 679-687
    • Asgeirsson, B.1    Adalbjornsson, B.V.2    Gylfason, G.A.3
  • 37
    • 0035122978 scopus 로고    scopus 로고
    • Comparative specificity of platelet alpha(IIb)beta(3) integrin antagonists
    • Thibault, G.; Tardif, P.; Lapalme, G. Comparative specificity of platelet alpha(IIb)beta(3) integrin antagonists. J. Pharmacol. Exp. Ther., 2001, 296, 690-696.
    • (2001) J. Pharmacol. Exp. Ther , vol.296 , pp. 690-696
    • Thibault, G.1    Tardif, P.2    Lapalme, G.3
  • 38
    • 4344629332 scopus 로고    scopus 로고
    • Inhibitors of platelets glycoprotein IIb/IIIa (GP IIb/IIIa) receptor: Rationale for their use in clinical cardiology
    • Rossi, M.L.; Zavalloni, D. Inhibitors of platelets glycoprotein IIb/IIIa (GP IIb/IIIa) receptor: rationale for their use in clinical cardiology. Mini Rev. Med. Chem., 2004, 4, 703-709.
    • (2004) Mini Rev. Med. Chem , vol.4 , pp. 703-709
    • Rossi, M.L.1    Zavalloni, D.2
  • 40
    • 0033030771 scopus 로고    scopus 로고
    • The effect of conformation on the solution stability of linear vs. cyclic RGD peptides
    • Bogdanowich-Knipp, S.J.; Jois, D.S.; Siahaan, T.J. The effect of conformation on the solution stability of linear vs. cyclic RGD peptides. J. Pept. Res., 1999, 53, 523-529.
    • (1999) J. Pept. Res , vol.53 , pp. 523-529
    • Bogdanowich-Knipp, S.J.1    Jois, D.S.2    Siahaan, T.J.3
  • 41
    • 0032865716 scopus 로고    scopus 로고
    • Effect of conformation on the conversion of cyclo-(1,7)-Gly-Arg-Gly-Asp-Ser-Pro-Asp-Gly-OH to its cyclic imide degradation product
    • Bogdanowich-Knipp, S.J.; Jois, S.D.; Siahaan, T.J. Effect of conformation on the conversion of cyclo-(1,7)-Gly-Arg-Gly-Asp-Ser-Pro-Asp-Gly-OH to its cyclic imide degradation product. J. Pept. Res., 1999, 54, 43-53.
    • (1999) J. Pept. Res , vol.54 , pp. 43-53
    • Bogdanowich-Knipp, S.J.1    Jois, S.D.2    Siahaan, T.J.3
  • 44
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G.L. Tissue sulfhydryl groups. Arc. Biochem. Biophys., 1959, 82, 70-77.
    • (1959) Arc. Biochem. Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 45
    • 0015150661 scopus 로고
    • Reaction of protein disulfide groups with Ellman's reagent: A case study of the number of sulfhydryl and disulfide groups in Aspergillus oryzae -amylase, papain, and lysozyme
    • Robyt, J.F.; Ackerman, R.J.; Chittenden, C.G. Reaction of protein disulfide groups with Ellman's reagent: a case study of the number of sulfhydryl and disulfide groups in Aspergillus oryzae -amylase, papain, and lysozyme. Arch. Biochem. Biophys., 1971, 147, 262-269.
    • (1971) Arch. Biochem. Biophys , vol.147 , pp. 262-269
    • Robyt, J.F.1    Ackerman, R.J.2    Chittenden, C.G.3
  • 46
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak, J.; Lindsay, R.H. Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem., 1968, 25, 192-205.
    • (1968) Anal. Biochem , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 47
    • 0036318194 scopus 로고    scopus 로고
    • Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine
    • Riener, C.K.; Kada, G.; Gruber, H.J. Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine. Anal. Bioanal. Chem., 2002, 373, 266-276.
    • (2002) Anal. Bioanal. Chem , vol.373 , pp. 266-276
    • Riener, C.K.1    Kada, G.2    Gruber, H.J.3
  • 48
    • 0032401864 scopus 로고    scopus 로고
    • Evaluation of methods for the quantitation of cysteines in proteins
    • Wright, S.K.; Viola, R.E. Evaluation of methods for the quantitation of cysteines in proteins. Anal. Biochem., 1998, 265, 8-14.
    • (1998) Anal. Biochem , vol.265 , pp. 8-14
    • Wright, S.K.1    Viola, R.E.2
  • 49
    • 0000964662 scopus 로고
    • Bimane fluorescent labels: Labeling of normal human red cells under physiological conditions
    • Kosower, N.S.; Kosower, E.M.; Newton, G.L.; Ranney, H.M. Bimane fluorescent labels: labeling of normal human red cells under physiological conditions. Proc. Natl. Acad. Sci. USA, 1979, 76, 3382-3386.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3382-3386
    • Kosower, N.S.1    Kosower, E.M.2    Newton, G.L.3    Ranney, H.M.4
  • 50
    • 0018893590 scopus 로고
    • Bimane fluorescent labels: Characterization of the bimane labeling of human hemoglobin
    • Kosower, N.S.; Newton, G.L.; Kosower, E.M.; Ranney, H.M. Bimane fluorescent labels: characterization of the bimane labeling of human hemoglobin. Biochim. Biophys. Acta, 1980, 622, 201-209.
    • (1980) Biochim. Biophys. Acta , vol.622 , pp. 201-209
    • Kosower, N.S.1    Newton, G.L.2    Kosower, E.M.3    Ranney, H.M.4
  • 51
    • 0023051821 scopus 로고
    • Site-directed labeling of a monoclonal antibody: Targeting to a disulfide bond
    • Packard, B.; Edidin, M.; Komoriya, A. Site-directed labeling of a monoclonal antibody: targeting to a disulfide bond. Biochemistry, 1986, 25, 3548-3552.
    • (1986) Biochemistry , vol.25 , pp. 3548-3552
    • Packard, B.1    Edidin, M.2    Komoriya, A.3
  • 52
    • 0027533704 scopus 로고
    • Determination and derivatization of protein thiols by n-octyldithionitrobenzoic acid
    • Faulstich, H.; Tews, P.; Heintz, D. Determination and derivatization of protein thiols by n-octyldithionitrobenzoic acid. Anal. Biochem., 1993, 208, 357-362.
    • (1993) Anal. Biochem , vol.208 , pp. 357-362
    • Faulstich, H.1    Tews, P.2    Heintz, D.3
  • 53
    • 0022873550 scopus 로고
    • Determination of thiol proteins using monobromobimane labeling and high-performance liquid chromatographic analysis: Application to Escherichia coli thioredoxin
    • Chinn, P.C.; Pigiet, V.; Fahey, R.C. Determination of thiol proteins using monobromobimane labeling and high-performance liquid chromatographic analysis: application to Escherichia coli thioredoxin. Anal. Biochem., 1986, 159, 143-149.
    • (1986) Anal. Biochem , vol.159 , pp. 143-149
    • Chinn, P.C.1    Pigiet, V.2    Fahey, R.C.3
  • 54
    • 0000962563 scopus 로고
    • Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
    • Holmgren, A.; Soderberg, B.O.; Eklund, H.; Branden, C.I. Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Proc. Natl. Acad. Sci. USA, 1975, 72, 2305-2309.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2305-2309
    • Holmgren, A.1    Soderberg, B.O.2    Eklund, H.3    Branden, C.I.4
  • 55
    • 0025909444 scopus 로고
    • High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution
    • Forman-Kay, J.D.; Clore, G.M.; Wingfield, P.T.; Gronenborn, A.M. High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry, 1991, 30, 2685-2698.
    • (1991) Biochemistry , vol.30 , pp. 2685-2698
    • Forman-Kay, J.D.1    Clore, G.M.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 58
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • Sharma, D.; Rajarathnam, K. 13C NMR chemical shifts can predict disulfide bond formation. J. Biomol. NMR, 2000, 18, 165-171.
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 59
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D.S.; Sykes, B.D.; Richards, F.M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry, 1992, 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 60
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S.; Sykes, B.D.; Richards, F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol., 1991, 222, 311-333.
    • (1991) J. Mol. Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 61
    • 0028393784 scopus 로고
    • 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR, 1994, 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 62
    • 34548719269 scopus 로고    scopus 로고
    • Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy
    • Piotukh, K.; Kosslick, D.; Zimmermann, J.; Krause, E.; Freund, C. Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy. Free Radic. Biol. Med., 2007, 43, 1263-1270.
    • (2007) Free Radic. Biol. Med , vol.43 , pp. 1263-1270
    • Piotukh, K.1    Kosslick, D.2    Zimmermann, J.3    Krause, E.4    Freund, C.5
  • 63
    • 33749996172 scopus 로고    scopus 로고
    • Synthesis and chemical stability of a disulfide bond in a model cyclic pentapeptide: Cyclo(1,4)-Cys-Gly-Phe-Cys-Gly-OH
    • He, H.T.; Gürsoy, R.N.; Kupczyk-Subotkowska, L.; Tian, J.; Williams, T.; Siahaan, T.J. Synthesis and chemical stability of a disulfide bond in a model cyclic pentapeptide: Cyclo(1,4)-Cys-Gly-Phe-Cys-Gly-OH. J. Pharm. Sci., 2006, 95, 2222-2234.
    • (2006) J. Pharm. Sci , vol.95 , pp. 2222-2234
    • He, H.T.1    Gürsoy, R.N.2    Kupczyk-Subotkowska, L.3    Tian, J.4    Williams, T.5    Siahaan, T.J.6
  • 64
    • 0019063552 scopus 로고
    • Degradation of protein disulphide bonds in dilute alkali
    • Florence, M.T. Degradation of protein disulphide bonds in dilute alkali. Biochem. J., 1980, 189, 507-520.
    • (1980) Biochem. J , vol.189 , pp. 507-520
    • Florence, M.T.1
  • 66
    • 0027666050 scopus 로고
    • Disulfide-linked aggregation of thyroglobulin normally occurs during nascent protein folding
    • Kim, P.S.; Kim, K.R.; Arvan, P. Disulfide-linked aggregation of thyroglobulin normally occurs during nascent protein folding. Am. J. Physiol., 1993, 265, C704-711.
    • (1993) Am. J. Physiol , vol.265
    • Kim, P.S.1    Kim, K.R.2    Arvan, P.3
  • 67
    • 0022360237 scopus 로고
    • Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies
    • Bucala, R.; Manabe, S.; Urban, R.C.; Cerami, A. Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies. Exp. Eye Res., 1985, 41, 353-363.
    • (1985) Exp. Eye Res , vol.41 , pp. 353-363
    • Bucala, R.1    Manabe, S.2    Urban, R.C.3    Cerami, A.4
  • 68
    • 0021690560 scopus 로고
    • Nonenzymatic addition of glucocorticoids to lens proteins in steroid-induced cataracts
    • Manabe, S.; Bucala, R.; Cerami, A. Nonenzymatic addition of glucocorticoids to lens proteins in steroid-induced cataracts. J. Clin. Invest., 1984, 74, 1803-1810.
    • (1984) J. Clin. Invest , vol.74 , pp. 1803-1810
    • Manabe, S.1    Bucala, R.2    Cerami, A.3
  • 69
    • 0036044886 scopus 로고    scopus 로고
    • The effect of modification of alphacrystallin by prednisolone-21-hemisuccinate and fructose 6-phosphate on chaperone activity
    • Hook, D.W.A.; Harding, J.J. The effect of modification of alphacrystallin by prednisolone-21-hemisuccinate and fructose 6-phosphate on chaperone activity. Dev. Ophthalmol., 2002, 35, 150-160.
    • (2002) Dev. Ophthalmol , vol.35 , pp. 150-160
    • Hook, D.W.A.1    Harding, J.J.2
  • 70
    • 0028485953 scopus 로고
    • Effects of intermolecular thiol-disulfide interchange reactions on BSA fouling during microfiltration
    • Kelly, S.T.; Zydney, A.L. Effects of intermolecular thiol-disulfide interchange reactions on BSA fouling during microfiltration. Biotechnol. Bioeng., 1994, 44, 972-982.
    • (1994) Biotechnol. Bioeng , vol.44 , pp. 972-982
    • Kelly, S.T.1    Zydney, A.L.2
  • 71
    • 0017680987 scopus 로고
    • Alkylation of Cysteine Thiols with 1,3-Propane Sultone
    • Hirs, C.H.W, Timasheff, S.N, Eds, Elsevier Inc, USA
    • Ruegg, U.; Rudinger, J. Alkylation of Cysteine Thiols with 1,3-Propane Sultone. In Hirs, C.H.W.; Timasheff, S.N.; Eds.; Methods in Enzymology. Volume 47: Elsevier Inc, USA, 1977, p. 116-122.
    • (1977) Methods in Enzymology , vol.47 , pp. 116-122
    • Ruegg, U.1    Rudinger, J.2
  • 72
    • 0016638276 scopus 로고
    • Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes
    • Smith, D.J.; Miggio, E.T.; Kenyon, G.L. Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes. Biochem., 1975, 14, 766-771.
    • (1975) Biochem , vol.14 , pp. 766-771
    • Smith, D.J.1    Miggio, E.T.2    Kenyon, G.L.3
  • 73
    • 0023646709 scopus 로고
    • Sulfhydryl modification and activation of phenylalanine hydroxylase by dinitrophenyl alkyl disulfide
    • Koizumi, S.; Suzuki, T.; Takahashi, S.; Satake, K.; Takeuchi, T.; Umezawa, H.; Nagatsu, T. Sulfhydryl modification and activation of phenylalanine hydroxylase by dinitrophenyl alkyl disulfide. Biochem., 1987, 26, 6461-6465.
    • (1987) Biochem , vol.26 , pp. 6461-6465
    • Koizumi, S.1    Suzuki, T.2    Takahashi, S.3    Satake, K.4    Takeuchi, T.5    Umezawa, H.6    Nagatsu, T.7
  • 76
    • 0029793539 scopus 로고    scopus 로고
    • Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase
    • Marchand, P.; Volkmann, M.; Bond, J.S. Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase. J. Biol. Chem., 1996, 271, 24236-24241.
    • (1996) J. Biol. Chem , vol.271 , pp. 24236-24241
    • Marchand, P.1    Volkmann, M.2    Bond, J.S.3
  • 77
    • 34547776752 scopus 로고    scopus 로고
    • Site specific protein PEGylation: Application to cysteine analogs of recombinant human granulocyte colony-stimulating factor
    • Rosendahl, M.S.; Doherty, D.H.; Smith, D.J.; Bendale, A.M.; Cox, G.N. Site specific protein PEGylation: Application to cysteine analogs of recombinant human granulocyte colony-stimulating factor. Bioprocess Intern., 2005, 3, 52-62.
    • (2005) Bioprocess Intern , vol.3 , pp. 52-62
    • Rosendahl, M.S.1    Doherty, D.H.2    Smith, D.J.3    Bendale, A.M.4    Cox, G.N.5
  • 78
  • 79
    • 0034682480 scopus 로고    scopus 로고
    • Site-specific chemical modification with polyethylene glycol of recombinant immunotoxin anti-Tac(Fv)-PE38 (LMB-2) improves antitumor activity and reduces animal toxicity and immunogenicity
    • Tsutsumi, Y.; Onda, M.; Nagata, S.; Lee, B.; Kreitman, R.J.; Pastan, I. Site-specific chemical modification with polyethylene glycol of recombinant immunotoxin anti-Tac(Fv)-PE38 (LMB-2) improves antitumor activity and reduces animal toxicity and immunogenicity. Proc. Natl. Acad. Sci. USA, 2000, 97, 8548-8553.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8548-8553
    • Tsutsumi, Y.1    Onda, M.2    Nagata, S.3    Lee, B.4    Kreitman, R.J.5    Pastan, I.6
  • 83
    • 85123225068 scopus 로고    scopus 로고
    • Basu, A.; Yang, K.; Wang, M.; Liu, S.; Chintala, R.; Palm, T.; Zhao, H.; Peng, P.; Wu, D.; Zhang, Z.; Hua, J.; Hsieh, M.C.; Zhou, J.; Petti, G.; Li, X.; Janjua, A.; Mendez, M.; Liu, J.; Longley, C.; Zhang, Z.; Mehlig, M.; Borowski, V.; Viswanathan, M.; Filpula, D. Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation. Bioconjug. Chem., 2006, 17, 618-630.
    • Basu, A.; Yang, K.; Wang, M.; Liu, S.; Chintala, R.; Palm, T.; Zhao, H.; Peng, P.; Wu, D.; Zhang, Z.; Hua, J.; Hsieh, M.C.; Zhou, J.; Petti, G.; Li, X.; Janjua, A.; Mendez, M.; Liu, J.; Longley, C.; Zhang, Z.; Mehlig, M.; Borowski, V.; Viswanathan, M.; Filpula, D. Structure-function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation. Bioconjug. Chem., 2006, 17, 618-630.
  • 84
    • 33748918574 scopus 로고    scopus 로고
    • Nanomedicine: Clinical applications of polyethylene glycol conjugated proteins and drugs
    • Parveen, S.; Sahoo, S.K. Nanomedicine: clinical applications of polyethylene glycol conjugated proteins and drugs. Clin. Pharmacokinet., 2006, 45, 965-988.
    • (2006) Clin. Pharmacokinet , vol.45 , pp. 965-988
    • Parveen, S.1    Sahoo, S.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.