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Volumn 5, Issue 2, 1996, Pages 270-277

Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase

Author keywords

intermolecular disulfides; protein aggregation annulment; size exclusion chromatography; thymidylate synthase

Indexed keywords

THYMIDYLATE SYNTHASE; UREA;

EID: 0030041283     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050211     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennet MJ, Choe S, Eisenberg D. 1994. Domain swapping: Entangling alliances between proteins. Proc Natl Acad Sci USA 91:3127-3131.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3127-3131
    • Bennet, M.J.1    Choe, S.2    Eisenberg, D.3
  • 2
    • 0027166926 scopus 로고
    • Characterization of the covalent chromatography of thymidylate synthase on thiopropyl-sepharose 6B
    • Bradshaw TP, Dunlap BR. 1979. Characterization of the covalent chromatography of thymidylate synthase on thiopropyl-sepharose 6B. Biochim Biophys Acta 1163:165-175.
    • (1979) Biochim Biophys Acta , vol.1163 , pp. 165-175
    • Bradshaw, T.P.1    Dunlap, B.R.2
  • 4
    • 0023039205 scopus 로고
    • Characterization of an associated equilibrium folding intermediate of bovine growth hormone
    • Brems DN, Plaisted SM, Kauffman EW, Havel HA. 1986. Characterization of an associated equilibrium folding intermediate of bovine growth hormone. Biochemistry 25:6539-5643.
    • (1986) Biochemistry , vol.25 , pp. 6539-15643
    • Brems, D.N.1    Plaisted, S.M.2    Kauffman, E.W.3    Havel, H.A.4
  • 5
    • 0028859841 scopus 로고
    • Folding intermediates are involved in genetic diseases?
    • Bychkova VE, Ptitsyn OB. 1995. Folding intermediates are involved in genetic diseases? FEBS Lett 359:3-5.
    • (1995) FEBS Lett , vol.359 , pp. 3-5
    • Bychkova, V.E.1    Ptitsyn, O.B.2
  • 6
    • 0027975260 scopus 로고
    • Predisposition of prion protein homozygotes to Creutzfeldt-Jacob disease can be explained by a nucleation-dependent polymerization mechanism
    • Come JH, Lansbury PT Jr. 1994. Predisposition of prion protein homozygotes to Creutzfeldt-Jacob disease can be explained by a nucleation-dependent polymerization mechanism. J Am Chem Soc 116:4109-4110.
    • (1994) J Am Chem Soc , vol.116 , pp. 4109-4110
    • Come, J.H.1    Lansbury Jr., P.T.2
  • 7
    • 0021759423 scopus 로고
    • Use of high speed size-exclusion chromatography for the study of protein folding and stability
    • Corbett RJT, Roche RS. 1984. Use of high speed size-exclusion chromatography for the study of protein folding and stability Biochemistry 23: 1888-1894.
    • (1984) Biochemistry , vol.23 , pp. 1888-1894
    • Corbett, R.J.T.1    Roche, R.S.2
  • 8
    • 0020647834 scopus 로고
    • An empirical approach to protein conformation stability and flexibility
    • Creighton TE. 1983. An empirical approach to protein conformation stability and flexibility. Biopolymers 22:49-58.
    • (1983) Biopolymers , vol.22 , pp. 49-58
    • Creighton, T.E.1
  • 10
    • 0001236723 scopus 로고
    • On the aggregation of bovine pancreatic ribonuclease
    • Crestfield AM, Stein WH, Moore S. 1962. On the aggregation of bovine pancreatic ribonuclease. Arch Biochem Biophys(Suppl 1):217-233.
    • (1962) Arch Biochem Biophys , Issue.1 SUPPL. , pp. 217-233
    • Crestfield, A.M.1    Stein, W.H.2    Moore, S.3
  • 11
    • 0027273987 scopus 로고
    • Aggregation and denaturation of apomyoglobin in aqueous urea solutions
    • DeYoung LR, Dill KA, Fink AL. 1993a. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry 32:3877-3886.
    • (1993) Biochemistry , vol.32 , pp. 3877-3886
    • DeYoung, L.R.1    Dill, K.A.2    Fink, A.L.3
  • 14
    • 0014690974 scopus 로고
    • The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride
    • Fish WW, Mann KG, Tanford C. 1969. The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride. J Biol Chem 244:4989-4994.
    • (1969) J Biol Chem , vol.244 , pp. 4989-4994
    • Fish, W.W.1    Mann, K.G.2    Tanford, C.3
  • 15
    • 0014940352 scopus 로고
    • Gel chromatography of proteins in denaturing solutions
    • Fish WW, Reynolds JA, Tanford C. 1970. Gel chromatography of proteins in denaturing solutions. J Biol Chem 245:5166-5168.
    • (1970) J Biol Chem , vol.245 , pp. 5166-5168
    • Fish, W.W.1    Reynolds, J.A.2    Tanford, C.3
  • 16
    • 0001848681 scopus 로고
    • Folding of large proteins
    • Creighton TE, ed. W.H. Freeman & Co.
    • Garel JR. 1992. Folding of large proteins. In: Creighton TE, ed. Protein folding. W.H. Freeman & Co. pp 405-454.
    • (1992) Protein Folding , pp. 405-454
    • Garel, J.R.1
  • 18
    • 0028064007 scopus 로고
    • Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface
    • Gokhale RS, Agarwalla S, Francis VS, Santi DV, Balaram P. 1994. Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface. J Mol Biol 235:89-94.
    • (1994) J Mol Biol , vol.235 , pp. 89-94
    • Gokhale, R.S.1    Agarwalla, S.2    Francis, V.S.3    Santi, D.V.4    Balaram, P.5
  • 19
    • 0021416620 scopus 로고
    • Gel electrophoresis in studies of protein conformation and folding
    • Goldenberg DP, Creighton TE. 1984. Gel electrophoresis in studies of protein conformation and folding. Anal Biochem 138:1-18.
    • (1984) Anal Biochem , vol.138 , pp. 1-18
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 21
    • 0022976484 scopus 로고
    • Reversible self-association of bovine growth hormone during equilibrium unfolding
    • Havel HA, Kauffman EW, Plaisted SM, Brems DN. 1986. Reversible self-association of bovine growth hormone during equilibrium unfolding. Biochemistry 25:6533-6538.
    • (1986) Biochemistry , vol.25 , pp. 6533-6538
    • Havel, H.A.1    Kauffman, E.W.2    Plaisted, S.M.3    Brems, D.N.4
  • 22
    • 0027446868 scopus 로고
    • Interactive intermediates are formed during the urea unfolding of rhodanase
    • Horowitz PM, Butler M. 1993. interactive intermediates are formed during the urea unfolding of rhodanase. J Biol Chem 268:2500-2504.
    • (1993) J Biol Chem , vol.268 , pp. 2500-2504
    • Horowitz, P.M.1    Butler, M.2
  • 23
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke R. 1987. Folding and association of proteins. Prog Biophys Mol Biol 49:117-237.
    • (1987) Prog Biophys Mol Biol , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • Lammeli UK. 1970. Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Lammeli, U.K.1
  • 26
    • 0025887736 scopus 로고
    • Site-directed mutagenesis to probe protein folding: Evidence that the formation and aggregation of a bovine growth hormone folding intermediate are dissociable processes
    • Lehrman RS, Tuls JL, Havel HA, Haskell RJ, Putnam SD, Tomich CSC. 1991. Site-directed mutagenesis to probe protein folding: Evidence that the formation and aggregation of a bovine growth hormone folding intermediate are dissociable processes. Biochemistry 30:5777-5784.
    • (1991) Biochemistry , vol.30 , pp. 5777-5784
    • Lehrman, R.S.1    Tuls, J.L.2    Havel, H.A.3    Haskell, R.J.4    Putnam, S.D.5    Tomich, C.S.C.6
  • 27
    • 0016206102 scopus 로고
    • Renaturation of E. coli tryptophanase after exposure to 8 M urea. Evidence for the existence of multinucleation centeres
    • London J, Skrzynia C, Goldberg ME. 1974. Renaturation of E. coli tryptophanase after exposure to 8 M urea. Evidence for the existence of multinucleation centeres. Eur J Biochem 47:409-415.
    • (1974) Eur J Biochem , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.E.3
  • 28
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride, a calorimetric study
    • Makhatadze GI, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride, a calorimetric study. J Mol Biol 226:491-505.
    • (1992) J Mol Biol , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 29
    • 0027043310 scopus 로고
    • Reversible dissociation and unfolding of the dimeric protein thymidylate synthase
    • Perry KM, Pookanjanatavip M, Zhao J, Santi DV, Stroud RM. 1992. Reversible dissociation and unfolding of the dimeric protein thymidylate synthase. Protein Sci 1:796-800.
    • (1992) Protein Sci , vol.1 , pp. 796-800
    • Perry, K.M.1    Pookanjanatavip, M.2    Zhao, J.3    Santi, D.V.4    Stroud, R.M.5
  • 30
    • 0027978909 scopus 로고
    • Reversible dissociation and unfolding of pyruvate decarboxylase from Zymomonas mobilis
    • Pohl M, Grotzinger J, Wollmer A, Kula M. 1994. Reversible dissociation and unfolding of pyruvate decarboxylase from Zymomonas mobilis. Eur J Biochem 224:651-661.
    • (1994) Eur J Biochem , vol.224 , pp. 651-661
    • Pohl, M.1    Grotzinger, J.2    Wollmer, A.3    Kula, M.4
  • 32
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. 1991. Molecular biology of prion diseases. Science 252:1515-1518.
    • (1991) Science , vol.252 , pp. 1515-1518
    • Prusiner, S.B.1
  • 33
    • 0018772480 scopus 로고
    • Denaturation of thymidylate synthase from amethopterin-resistant Lactobacillus casei
    • Reinsch JW, Smith LL, Dunlap RB. 1979. Denaturation of thymidylate synthase from amethopterin-resistant Lactobacillus casei. Cancer Biochem Biophys 3:57-64.
    • (1979) Cancer Biochem Biophys , vol.3 , pp. 57-64
    • Reinsch, J.W.1    Smith, L.L.2    Dunlap, R.B.3
  • 34
    • 0024429732 scopus 로고
    • Production of soluble recombinant protein in bacteria
    • Schein CH. 1989. Production of soluble recombinant protein in bacteria. Biotechnology 7:1141.
    • (1989) Biotechnology , vol.7 , pp. 1141
    • Schein, C.H.1
  • 35
    • 0024818499 scopus 로고
    • Stereochemical modelling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini R, Srinivasan N, Shoichet B, Santi DV, Ramakrishnan C, Balaram P. 1989. Stereochemical modelling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 3:95-103.
    • (1989) Protein Eng , vol.3 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 37
    • 0016218601 scopus 로고
    • Molecular characterization of proteins in detergent solutions
    • Tanford C, Nozaki Y, Reynolds JA, Makino S. 1974. Molecular characterization of proteins in detergent solutions. Biochemistry 13:2369-2376.
    • (1974) Biochemistry , vol.13 , pp. 2369-2376
    • Tanford, C.1    Nozaki, Y.2    Reynolds, J.A.3    Makino, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.