메뉴 건너뛰기




Volumn 43, Issue 17, 2004, Pages 4899-4905

An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CHEMICAL BONDS; DISSOCIATION; MUTAGENESIS; NEUROLOGY; PROTEINS;

EID: 2142761528     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030246r     Document Type: Article
Times cited : (105)

References (70)
  • 1
    • 0037068826 scopus 로고    scopus 로고
    • Fas(t) balls and Lou Gehrig disease. A clue to selective vulnerability of motor neurons?
    • Xiong, Z. Q., and McNamara, J. O. (2002) Fas(t) balls and Lou Gehrig disease. A clue to selective vulnerability of motor neurons? Neuron 35, 1011-1013.
    • (2002) Neuron , vol.35 , pp. 1011-1013
    • Xiong, Z.Q.1    McNamara, J.O.2
  • 2
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland, D. W., and Rothstein, J. D. (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS, Nat. Rev. Neurosci. 2, 806-819.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 3
    • 0029584941 scopus 로고
    • Superoxide dismutase in familial amyotrophic lateral sclerosis: Models for gain of function
    • Brown, R. H., Jr. (1995) Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function, Curr. Opin. Neurobiol. 5, 841-846.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 841-846
    • Brown Jr., R.H.1
  • 4
    • 0028105029 scopus 로고
    • A transgenic-mouse model of amyotrophic lateral sclerosis
    • Brown, R. H. (1994) A transgenic-mouse model of amyotrophic lateral sclerosis, N. Engl. J. Med. 331, 1091-1092.
    • (1994) N. Engl. J. Med. , vol.331 , pp. 1091-1092
    • Brown, R.H.1
  • 6
    • 0034961104 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Pathogenesis
    • Brown, R. H., Jr., and Robberecht, W. (2001) Amyotrophic lateral sclerosis: pathogenesis, Semin. Neurol. 21, 131-139.
    • (2001) Semin. Neurol. , vol.21 , pp. 131-139
    • Brown Jr., R.H.1    Robberecht, W.2
  • 8
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling, A. C., Schulz, J. B., Brown, R. H., Jr., and Beal, M. F. (1993) Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis, J. Neurochem. 61, 2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown Jr., R.H.3    Beal, M.F.4
  • 11
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
    • Lindberg, M. J., Tibell, L., and Oliveberg, M. (2002) Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state, Proc. Natl. Acad. Sci. U.S.A. 99, 16607-16612.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 12
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward, L. J., Rodriguez, J. A., Kim, J. W., Tiwari, A., Goto, J. J., Cabelli, D. E., Valentine, J. S., and Brown, R. H., Jr. (2002) Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis, J. Biol. Chem. 277, 15923-15931.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15923-15931
    • Hayward, L.J.1    Rodriguez, J.A.2    Kim, J.W.3    Tiwari, A.4    Goto, J.J.5    Cabelli, D.E.6    Valentine, J.S.7    Brown Jr., R.H.8
  • 13
    • 0030596537 scopus 로고    scopus 로고
    • Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis
    • Nakano, R., Inuzuka, T., Kikugawa, K., Takahashi, H., Sakimura, K., Fujii, J., Taniguchi, N., and Tsuji, S. (1996) Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis, Neurosci. Lett. 211, 129-131.
    • (1996) Neurosci. Lett. , vol.211 , pp. 129-131
    • Nakano, R.1    Inuzuka, T.2    Kikugawa, K.3    Takahashi, H.4    Sakimura, K.5    Fujii, J.6    Taniguchi, N.7    Tsuji, S.8
  • 15
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded
    • Julien, J. P. (2001) Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded, Cell 104, 581-591.
    • (2001) Cell , vol.104 , pp. 581-591
    • Julien, J.P.1
  • 16
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations, Nature 418, 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 17
    • 0038004727 scopus 로고    scopus 로고
    • Superoxide dismutase folding/unfolding pathway: Role of the metal ions in modulating structural and dynamical features
    • Assfalg, M., Banci, L., Bertini, I., Turano, P., and Vasos, P. R. (2003) Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical features, J. Mol. Biol. 330, 145-158.
    • (2003) J. Mol. Biol. , vol.330 , pp. 145-158
    • Assfalg, M.1    Banci, L.2    Bertini, I.3    Turano, P.4    Vasos, P.R.5
  • 19
    • 0036440686 scopus 로고    scopus 로고
    • Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase
    • Cardoso, R. M., Thayer, M. M., DiDonato, M., Lo, T. P., Bruns, C. K., Getzoff, E. D., and Tainer, J. A. (2002) Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase, J. Mol. Biol. 324, 247-256.
    • (2002) J. Mol. Biol. , vol.324 , pp. 247-256
    • Cardoso, R.M.1    Thayer, M.M.2    DiDonato, M.3    Lo, T.P.4    Bruns, C.K.5    Getzoff, E.D.6    Tainer, J.A.7
  • 20
    • 0031577722 scopus 로고    scopus 로고
    • Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes
    • Ogawa, Y., Kosaka, H., Nakanishi, T., Shimizu, A., Ohoi, N., Shouji, H., Yanagihara, T., and Sakoda, S. (1997) Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes, Biochem. Biophys. Res. Commun. 241, 251-257.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 251-257
    • Ogawa, Y.1    Kosaka, H.2    Nakanishi, T.3    Shimizu, A.4    Ohoi, N.5    Shouji, H.6    Yanagihara, T.7    Sakoda, S.8
  • 21
    • 0031025061 scopus 로고    scopus 로고
    • Instability of expressed Cu/Zn superoxide dismutase with 2 bp deletion found in familial amyotrophic lateral sclerosis
    • Watanabe, Y., Kono, Y., Nanba, E., Ohama, E., and Nakashima, K. (1997) Instability of expressed Cu/Zn superoxide dismutase with 2 bp deletion found in familial amyotrophic lateral sclerosis, FEBS Lett. 400, 108-112.
    • (1997) FEBS Lett. , vol.400 , pp. 108-112
    • Watanabe, Y.1    Kono, Y.2    Nanba, E.3    Ohama, E.4    Nakashima, K.5
  • 22
    • 0025929954 scopus 로고
    • Advances in the understanding of the structure-function relationship in Cu,Zn superoxide dismutase
    • Banci, L., Bertini, I., Cabelli, D. E., Hallewell, R. A., Luchinat, C., and Viezzoli, M. S. (1991) Advances in the understanding of the structure-function relationship in Cu,Zn superoxide dismutase, Free Radical Res. Commun. 12-13 (Part 1), 239-251.
    • (1991) Free Radical Res. Commun. , vol.12-13 , Issue.PART 1 , pp. 239-251
    • Banci, L.1    Bertini, I.2    Cabelli, D.E.3    Hallewell, R.A.4    Luchinat, C.5    Viezzoli, M.S.6
  • 23
    • 0025074777 scopus 로고
    • Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine
    • McRee, D. E., Redford, S. M., Getzoff, E. D., Lepock, J. R., Hallewell, R. A., and Tainer, J. A. (1990) Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine, J. Biol. Chem. 265, 14234-14241.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14234-14241
    • McRee, D.E.1    Redford, S.M.2    Getzoff, E.D.3    Lepock, J.R.4    Hallewell, R.A.5    Tainer, J.A.6
  • 24
    • 0038627546 scopus 로고    scopus 로고
    • The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)
    • Potter, S. Z., and Valentine, J. S. (2003) The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease), J. Biol. Inorg. Chem. 8, 373-380.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 373-380
    • Potter, S.Z.1    Valentine, J.S.2
  • 25
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells
    • Rabizadeh, S., Gralla, E. B., Borchelt, D. R., Gwinn, R., Valentine, J. S., Sisodia, S., Wong, P., Lee, M., Hahn, H., and Bredesen, D. E. (1995) Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells, Proc. Natl. Acad. Sci. U.S.A. 92, 3024-3028.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.R.3    Gwinn, R.4    Valentine, J.S.5    Sisodia, S.6    Wong, P.7    Lee, M.8    Hahn, H.9    Bredesen, D.E.10
  • 26
    • 0028149084 scopus 로고
    • Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis
    • Nishida, C. R., Gralla, E. B., and Valentine, J. S. (1994) Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. U.S.A. 91, 9906-9910.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9906-9910
    • Nishida, C.R.1    Gralla, E.B.2    Valentine, J.S.3
  • 27
    • 0031015422 scopus 로고    scopus 로고
    • Prognosis in familial amyotrophic lateral sclerosis: Progression and survival in patients with glu100gly and ala4val mutations in Cu,Zn superoxide dismutase
    • Juneja, T., Pericak-Vance, M. A., Laing, N. G., Dave, S., and Siddique, T. (1997) Prognosis in familial amyotrophic lateral sclerosis: progression and survival in patients with glu100gly and ala4val mutations in Cu,Zn superoxide dismutase, Neurology 48, 55-57.
    • (1997) Neurology , vol.48 , pp. 55-57
    • Juneja, T.1    Pericak-Vance, M.A.2    Laing, N.G.3    Dave, S.4    Siddique, T.5
  • 28
    • 0035892642 scopus 로고    scopus 로고
    • Assay of superoxide dismutase: Cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide
    • Okado-Matsumoto, A., and Fridovich, I. (2001) Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide, Anal. Biochem. 298, 337-342.
    • (2001) Anal. Biochem. , vol.298 , pp. 337-342
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 30
    • 0030900245 scopus 로고    scopus 로고
    • A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value
    • Yim, H. S., Kang, J. H., Chock, P. B., Stadtman, E. R., and Yim, M. B. (1997) A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value, J. Biol. Chem. 272, 8861-8863.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8861-8863
    • Yim, H.S.1    Kang, J.H.2    Chock, P.B.3    Stadtman, E.R.4    Yim, M.B.5
  • 31
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel, H. A., Petre, B. M., Wall, J., Simon, M., Nowak, R. J., Walz, T., and Lansbury, P. T., Jr. (2002) Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils, J. Mol. Biol. 322, 1089-1102.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 33
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini, R., Srinivasan, N., Shoichet, B., Santi, D. V., Ramakrishnan, C., and Balaram, P. (1989) Stereochemical modeling 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
  • 34
    • 0027489388 scopus 로고
    • Modelling multiple disulphide loop containing polypeptides by random conformation generation. The test cases of alpha-conotoxin GI and endothelin I
    • Sowdhamini, R., Ramakrishnan, C., and Balaram, P. (1993) Modelling multiple disulphide loop containing polypeptides byrandom conformation generation. The test cases of alpha-conotoxin GI and endothelin I, Protein Eng. 6, 873-882.
    • (1993) Protein Eng. , vol.6 , pp. 873-882
    • Sowdhamini, R.1    Ramakrishnan, C.2    Balaram, P.3
  • 37
    • 0037742610 scopus 로고    scopus 로고
    • An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: Rates enhanced via proposed enzyme-associated peroxycarbonate intermediate
    • Elam, J. S., Malek, K., Rodriguez, J. A., Doucette, P. A., Taylor, A. B., Hayward, L. J., Cabelli, D. E., Valentine, J. S., and Hart, P. J. (2003) An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate, J. Biol. Chem. 278, 21032-21039.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21032-21039
    • Elam, J.S.1    Malek, K.2    Rodriguez, J.A.3    Doucette, P.A.4    Taylor, A.B.5    Hayward, L.J.6    Cabelli, D.E.7    Valentine, J.S.8    Hart, P.J.9
  • 39
    • 0037088793 scopus 로고    scopus 로고
    • Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS
    • Higgins, C. M., Jung, C., Ding, H., and Xu, Z. (2002) Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS, J. Neurosci. 22, No. RC215.
    • (2002) J. Neurosci. , vol.22 , Issue.RC215
    • Higgins, C.M.1    Jung, C.2    Ding, H.3    Xu, Z.4
  • 40
    • 27244462026 scopus 로고    scopus 로고
    • Dynamic features of the subunit interface of Cu,Zn superoxide dismutase as probed by tryptophan phosphorescence
    • Cioni, P., Stroppolo, M. E., Desideri, A., and Strambini, G. B. (2001) Dynamic features of the subunit interface of Cu,Zn superoxide dismutase as probed by tryptophan phosphorescence, Arch. Biochem. Biophys. 391, 111-118.
    • (2001) Arch. Biochem. Biophys. , vol.391 , pp. 111-118
    • Cioni, P.1    Stroppolo, M.E.2    Desideri, A.3    Strambini, G.B.4
  • 41
    • 0034720474 scopus 로고    scopus 로고
    • Single mutation induces a metal-dependent subunit association in dimeric Cu,Zn superoxide dismutase
    • D'Orazio, M., Battistoni, A., Stroppolo, M. E., and Desideri, A. (2000) Single mutation induces a metal-dependent subunit association in dimeric Cu,Zn superoxide dismutase, Biochem. Biophys. Res. Commun. 272, 81-83.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 81-83
    • D'Orazio, M.1    Battistoni, A.2    Stroppolo, M.E.3    Desideri, A.4
  • 43
    • 0034657260 scopus 로고    scopus 로고
    • Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases
    • Stroppolo, M. E., Malvezzi-Campeggi, F., Mei, G., Rosato, N., and Desideri, A. (2000) Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases, Arch. Biochem. Biophys. 377, 215-218.
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 215-218
    • Stroppolo, M.E.1    Malvezzi-Campeggi, F.2    Mei, G.3    Rosato, N.4    Desideri, A.5
  • 44
    • 0017034938 scopus 로고
    • Aggregation of deoxyhemoglobin subunits
    • McGovern, P., Reisberg, P., and Olson, J. S. (1976) Aggregation of deoxyhemoglobin subunits, J. Biol. Chem. 251, 7871-7879.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7871-7879
    • McGovern, P.1    Reisberg, P.2    Olson, J.S.3
  • 45
    • 0022628340 scopus 로고
    • Shy-Drager syndrome and amyotrophic lateral sclerosis. Cytoarchitectonic and morphometric studies of sacral autonomic neurons
    • Konno, H., Yamamoto, T., Iwasaki, Y., and Iizuka, H. (1986) Shy-Drager syndrome and amyotrophic lateral sclerosis. Cytoarchitectonic and morphometric studies of sacral autonomic neurons, J. Neurol. Sci. 73, 193-204.
    • (1986) J. Neurol. Sci. , vol.73 , pp. 193-204
    • Konno, H.1    Yamamoto, T.2    Iwasaki, Y.3    Iizuka, H.4
  • 46
    • 0030814099 scopus 로고    scopus 로고
    • Quaternary structure regulates hemin dissociation from human hemoglobin
    • Hargrove, M. S., Whitaker, T., Olson, J. S., Vali, R. J., and Mathews, A. J. (1997) Quaternary structure regulates hemin dissociation from human hemoglobin, J. Biol. Chem. 272, 17385-17389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17385-17389
    • Hargrove, M.S.1    Whitaker, T.2    Olson, J.S.3    Vali, R.J.4    Mathews, A.J.5
  • 47
    • 0024432915 scopus 로고
    • Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli
    • Bras, G. L., Teschner, W., Deville-Bonne, D., and Garel, J. R. (1989) Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli, Biochemistry 28, 6836-6841.
    • (1989) Biochemistry , vol.28 , pp. 6836-6841
    • Bras, G.L.1    Teschner, W.2    Deville-Bonne, D.3    Garel, J.R.4
  • 48
    • 0033580635 scopus 로고    scopus 로고
    • Thermodynamic analysis of unfolding and dissociation in lactose repressor protein
    • Barry, J. K., and Matthews, K. S. (1999) Thermodynamic analysis of unfolding and dissociation in lactose repressor protein, Biochemistry 38, 6520-6528.
    • (1999) Biochemistry , vol.38 , pp. 6520-6528
    • Barry, J.K.1    Matthews, K.S.2
  • 49
    • 0030041283 scopus 로고    scopus 로고
    • Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase
    • Agarwalla, S., Gokhale, R. S., Santi, D. V., and Balaram, P. (1996) Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase, Protein Sci. 5, 270-277.
    • (1996) Protein Sci. , vol.5 , pp. 270-277
    • Agarwalla, S.1    Gokhale, R.S.2    Santi, D.V.3    Balaram, P.4
  • 50
    • 0029982719 scopus 로고    scopus 로고
    • Covalent reinforcement of a fragile region in the dimeric enzyme thymidylate synthase stabilizes the protein against chaotrope-induced unfolding
    • Gokhale, R. S., Agarwalla, S., Santi, D. V., and Balaram, P. (1996) Covalent reinforcement of a fragile region in the dimeric enzyme thymidylate synthase stabilizes the protein against chaotrope-induced unfolding, Biochemistry 35, 7150-7158.
    • (1996) Biochemistry , vol.35 , pp. 7150-7158
    • Gokhale, R.S.1    Agarwalla, S.2    Santi, D.V.3    Balaram, P.4
  • 51
    • 0036785613 scopus 로고    scopus 로고
    • Structure and dynamics of copper-free SOD: The protein before binding copper
    • Banci, L., Bertini, I., Cantini, F., D'Onofrio, M., and Viezzoli, M. S. (2002) Structure and dynamics of copper-free SOD: The protein before binding copper, Protein Sci. 11, 2479-2492.
    • (2002) Protein Sci. , vol.11 , pp. 2479-2492
    • Banci, L.1    Bertini, I.2    Cantini, F.3    D'Onofrio, M.4    Viezzoli, M.S.5
  • 52
    • 0036231449 scopus 로고    scopus 로고
    • The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization
    • Banci, L., Bertini, I., Cramaro, F., Del Conte, R., and Viezzoli, M. S. (2002) The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization, Eur. J. Biochem. 269, 1905-1915.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1905-1915
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 53
    • 0034687667 scopus 로고    scopus 로고
    • Commitment to folded and aggregated states occurs late in interleukin-1 beta folding
    • Finke, J. M., Gross, L. A., Ho, H. M., Sept, D., Zimm, B. H., and Jennings, P. A. (2000) Commitment to folded and aggregated states occurs late in interleukin-1 beta folding, Biochemistry 39, 15633-15642.
    • (2000) Biochemistry , vol.39 , pp. 15633-15642
    • Finke, J.M.1    Gross, L.A.2    Ho, H.M.3    Sept, D.4    Zimm, B.H.5    Jennings, P.A.6
  • 54
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly, J. W. (1997) Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases, Structure 5, 595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 56
    • 0034919395 scopus 로고    scopus 로고
    • Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins
    • Schneider, F., Hammarstrom, P., and Kelly, J. W. (2001) Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins, Protein Sci. 10, 1606-1613.
    • (2001) Protein Sci. , vol.10 , pp. 1606-1613
    • Schneider, F.1    Hammarstrom, P.2    Kelly, J.W.3
  • 57
    • 0031684499 scopus 로고    scopus 로고
    • Discovering transthyretin amyloid fibril inhibitors by limited screening
    • Baures, P. W., Peterson, S. A., and Kelly, J. W. (1998) Discovering transthyretin amyloid fibril inhibitors by limited screening, Bioorg. Med. Chem. 6, 1389-1401.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1389-1401
    • Baures, P.W.1    Peterson, S.A.2    Kelly, J.W.3
  • 59
    • 0035949632 scopus 로고    scopus 로고
    • Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: Insight into the chaotrope unfolding dichotomy
    • Hammarstrom, P., Jiang, X., Deechongkit, S., and Kelly, J. W. (2001) Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy, Biochemistry 40, 11453-11459.
    • (2001) Biochemistry , vol.40 , pp. 11453-11459
    • Hammarstrom, P.1    Jiang, X.2    Deechongkit, S.3    Kelly, J.W.4
  • 60
    • 0035964955 scopus 로고    scopus 로고
    • Transsuppression of misfolding in an amyloid disease
    • Hammarstrom, P., Schneider, F., and Kelly, J. W. (2001) Transsuppression of misfolding in an amyloid disease, Science 293, 2459-2462.
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 61
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe, M., Dykes-Hoberg, M., Culotta, V. C., Price, D. L., Wong, P. C., and Rothstein, J. D. (2001) Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues, Neurobiol. Dis. 8, 933-941.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 63
    • 0033524469 scopus 로고    scopus 로고
    • Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: Evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant
    • Gokhale, R. S., Ray, S. S., Balaram, H., and Balaram, P. (1999) Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant, Biochemistry 38, 423-431.
    • (1999) Biochemistry , vol.38 , pp. 423-431
    • Gokhale, R.S.1    Ray, S.S.2    Balaram, H.3    Balaram, P.4
  • 64
    • 0033524490 scopus 로고    scopus 로고
    • Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: Restoration of stability by disulfide cross-linking of subunits
    • Gopal, B., Ray, S. S., Gokhale, R. S., Balaram, H., Murthy, M. R., and Balaram, P. (1999) Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: restoration of stability by disulfide cross-linking of subunits, Biochemistry 38, 478-486.
    • (1999) Biochemistry , vol.38 , pp. 478-486
    • Gopal, B.1    Ray, S.S.2    Gokhale, R.S.3    Balaram, H.4    Murthy, M.R.5    Balaram, P.6
  • 65
    • 0032891249 scopus 로고    scopus 로고
    • Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase: Crystal structure of the T155C/E188C/C244T mutant
    • Velanker, S. S., Gokhale, R. S., Ray, S. S., Gopal, B., Parthasarathy, S., Santi, D. V., Balaram, P., and Murthy, M. R. (1999) Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase: crystal structure of the T155C/E188C/C244T mutant, Protein Sci. 8, 930-933.
    • (1999) Protein Sci. , vol.8 , pp. 930-933
    • Velanker, S.S.1    Gokhale, R.S.2    Ray, S.S.3    Gopal, B.4    Parthasarathy, S.5    Santi, D.V.6    Balaram, P.7    Murthy, M.R.8
  • 66
    • 0028064007 scopus 로고
    • Thermal stabilization of thymidylate synthase by engineering two disulfide bridges across the dimer interface
    • Gokhale, R. S., Agarwalla, S., Francis, V. S., Santi, D. V., and 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
  • 67
    • 0027052444 scopus 로고
    • Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme
    • Jacobson, R. H., Matsumura, M., Faber, H. R., and Matthews, B. W. (1992) Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme, Protein Sci. 1, 46-57.
    • (1992) Protein Sci. , vol.1 , pp. 46-57
    • Jacobson, R.H.1    Matsumura, M.2    Faber, H.R.3    Matthews, B.W.4
  • 68
    • 0025319751 scopus 로고
    • Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein
    • Pjura, P. E., Matsumura, M., Wozniak, J. A., and Matthews, B. W. (1990) Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein, Biochemistry 29, 2592-2598.
    • (1990) Biochemistry , vol.29 , pp. 2592-2598
    • Pjura, P.E.1    Matsumura, M.2    Wozniak, J.A.3    Matthews, B.W.4
  • 69
    • 0026319603 scopus 로고
    • Stabilization of functional proteins by introduction of multiple disulfide bonds
    • Matsumura, M., and Matthews, B. W. (1991) Stabilization of functional proteins by introduction of multiple disulfide bonds, Methods Enzymol. 202, 336-356.
    • (1991) Methods Enzymol. , vol.202 , pp. 336-356
    • Matsumura, M.1    Matthews, B.W.2
  • 70
    • 0031012304 scopus 로고    scopus 로고
    • Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions
    • Kunst, C. B., Mezey, E., Brownstein, M. J., and Patterson, D. (1997) Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions, Nat. Genet. 15, 91-94.
    • (1997) Nat. Genet. , vol.15 , pp. 91-94
    • Kunst, C.B.1    Mezey, E.2    Brownstein, M.J.3    Patterson, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.