메뉴 건너뛰기




Volumn 32, Issue 7, 2000, Pages 725-736

Structural characterization of acid-induced intermediates of human glutathione transferase P1-1

Author keywords

Acid unfolding; Human glutathione transferase P1 1; Molten globule

Indexed keywords

GLUTATHIONE TRANSFERASE;

EID: 0034237678     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(00)00018-2     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfisen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfisen, C.B.1
  • 2
    • 0021114569 scopus 로고
    • 'Molten-globule state': A compact form of globular proteins with mobile side-chains
    • Ohgushi M., Wada A. 'Molten-globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett. 164:1983;21-24.
    • (1983) FEBS Lett. , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 3
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins. 6:1989;87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 4
    • 0025982146 scopus 로고
    • Molten globule intermediates and protein folding
    • Christensen H., Pain R.H. Molten globule intermediates and protein folding. Eur. J. Biophys. 19:1991;221-230.
    • (1991) Eur. J. Biophys. , vol.19 , pp. 221-230
    • Christensen, H.1    Pain, R.H.2
  • 6
    • 0032498239 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin from Aplysia limacina: The effect of salt and pH on the cooperativity of folding
    • Staniforth R.A., Bigotti M.G., Cutruzzolá F., Travaglini C., Brunori M. Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and pH on the cooperativity of folding. J. Mol. Biol. 275:1998;133-148.
    • (1998) J. Mol. Biol. , vol.275 , pp. 133-148
    • Staniforth, R.A.1    Bigotti, M.G.2    Cutruzzolá, F.3    Travaglini, C.4    Brunori, M.5
  • 7
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink A.L., Calciano L.J., Goto Y., Kurotsu T., Palleros D.R. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry. 33:1994;12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 10
    • 0027432676 scopus 로고
    • Secondary structure of globular proteins at the early and the final stages in protein folding
    • Kuwajima K., Semisotnov G.V., Finkelstein A.V., Sugai S., Ptitsyn O.B. Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS Lett. 334:1993;265-268.
    • (1993) FEBS Lett. , vol.334 , pp. 265-268
    • Kuwajima, K.1    Semisotnov, G.V.2    Finkelstein, A.V.3    Sugai, S.4    Ptitsyn, O.B.5
  • 11
    • 0024269217 scopus 로고
    • Glutathione transferases. Structure and catalytic activity
    • Mannervik B., Danielson U.H. Glutathione transferases. Structure and catalytic activity. Crit. Rev. Biochem. 23:1988;283-337.
    • (1988) Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 13
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30:1995;445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 14
    • 0025816448 scopus 로고
    • The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer P., Dirr H.W., Ladenstein R., Schaffer J., Gallay O., Huber R. The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005.
    • (1991) EMBO J. , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schaffer, J.4    Gallay, O.5    Huber, R.6
  • 16
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton T.E. Protein folding. Biochem. J. 270:1990;1-16.
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 17
    • 0029310535 scopus 로고
    • High level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA
    • Kolm R.H., Stenberg G., Widersten M., Mannervik B. High level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA. Protein Expression Purif. 6:1995;265-271.
    • (1995) Protein Expression Purif. , vol.6 , pp. 265-271
    • Kolm, R.H.1    Stenberg, G.2    Widersten, M.3    Mannervik, B.4
  • 18
    • 0025649469 scopus 로고
    • Differential activity of human, rat and bacteria glutathione transferase isoenzymes toward 4-nitroquinoline 1-oxide
    • Aceto A., Di Ilio C., Lo Bello M., Bucciarelli T., Angelucci S., Federici G. Differential activity of human, rat and bacteria glutathione transferase isoenzymes toward 4-nitroquinoline 1-oxide. Carcinogenesis. 11:1990;2267-2269.
    • (1990) Carcinogenesis , vol.11 , pp. 2267-2269
    • Aceto, A.1    Di Ilio, C.2    Lo, B.M.3    Bucciarelli, T.4    Angelucci, S.5    Federici, G.6
  • 19
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the beta-turns
    • Chang C.T., Wu C.S.C., Yang J.T. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal. Biochem. 91:1978;13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.C.2    Yang, J.T.3
  • 20
    • 0025911762 scopus 로고
    • How does protein synthesis give rise to the 3D-structure?
    • Ptitsyn O.B. How does protein synthesis give rise to the 3D-structure? FEBS Lett. 285:1991;176-181.
    • (1991) FEBS Lett. , vol.285 , pp. 176-181
    • Ptitsyn, O.B.1
  • 22
    • 0028100451 scopus 로고
    • Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase
    • Artigues A., Iriarte A., Martinez-Carrion M. Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase. J. Biol. Chem. 269:1994;21990-21999.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21990-21999
    • Artigues, A.1    Iriarte, A.2    Martinez-Carrion, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.