메뉴 건너뛰기




Volumn 79, Issue C, 2010, Pages 127-164

Taking charge of proteins: From neurodegeneration to industrial biotechnology

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78650139590     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1876-1623(10)79004-0     Document Type: Chapter
Times cited : (15)

References (98)
  • 1
    • 0016270016 scopus 로고
    • Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond
    • J.L. Abernethy , H.M. Steinman , and R.L. Hill Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond J. Biol. Chem. 249 1974 7339 7347
    • (1974) J. Biol. Chem. , vol.249 , pp. 7339-7347
    • Abernethy, J.L.1    Steinman, H.M.2    Hill, R.L.3
  • 2
    • 20244386847 scopus 로고    scopus 로고
    • Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant his46arg
    • S. Antonyuk , J.S. Elam , M.A. Hough , R.W. Strange , P.A. Doucette , and J.A. Rodriguez Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant his46arg Protein Sci. 14 2005 1201 1213
    • (2005) Protein Sci. , vol.14 , pp. 1201-1213
    • Antonyuk, S.1    Elam, J.S.2    Hough, M.A.3    Strange, R.W.4    Doucette, P.A.5    Rodriguez, J.A.6
  • 3
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • M.R. Arkin , and J.A. Wells Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Nat. Rev. Drug Discov. 3 2004 301 317
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 4
    • 0038004727 scopus 로고    scopus 로고
    • Superoxide dismutase folding/unfolding pathway: Role of the metal ions in modulating structural and dynamical features
    • M. Assfalg , L. Banci , I. Bertini , P. Turano , and P.R. Vasos Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical features J. Mol. Biol. 330 2003 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
  • 6
    • 0038247520 scopus 로고    scopus 로고
    • Solution structure of apo Cu, Zn superoxide dismutase: Role of metal ions in protein folding
    • L. Banci , I. Bertini , F. Cramaro , R. Del Conte , and M.S. Viezzoli Solution structure of apo Cu, Zn superoxide dismutase: role of metal ions in protein folding Biochemistry 42 2003 9543 9553
    • (2003) Biochemistry , vol.42 , pp. 9543-9553
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 7
    • 27744607600 scopus 로고    scopus 로고
    • Fully metallated S134N cu,zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution
    • L. Banci , I. Bertini , N. D'Amelio , E. Gaggelli , E. Libralesso , and I. Matecko Fully metallated S134N cu,zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution J. Biol. Chem. 280 2005 35815 35821
    • (2005) J. Biol. Chem. , vol.280 , pp. 35815-35821
    • Banci, L.1    Bertini, I.2    D'Amelio, N.3    Gaggelli, E.4    Libralesso, E.5    Matecko, I.6
  • 8
    • 0028912816 scopus 로고
    • Correlation of electrophoretic mobilities of proteins and peptides with their physicochemical properties
    • S.K. Basak , and M.R. Ladisch Correlation of electrophoretic mobilities of proteins and peptides with their physicochemical properties Anal. Biochem. 226 1995 51 58
    • (1995) Anal. Biochem. , vol.226 , pp. 51-58
    • Basak, S.K.1    Ladisch, M.R.2
  • 9
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • T. Berg Modulation of protein-protein interactions with small organic molecules Angew. Chem. Int. Ed. Engl. 42 2003 2462 2481
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 2462-2481
    • Berg, T.1
  • 10
    • 0033549036 scopus 로고    scopus 로고
    • Long-range electrostatic contributions to protein-ligand binding estimated using protein charge ladders, affinity capillary electrophoresis, and continuum electrostatic theory
    • J.A. Caravella , J.D. Carbeck , D.C. Duffy , G.M. Whitesides , and B. Tidor Long-range electrostatic contributions to protein-ligand binding estimated using protein charge ladders, affinity capillary electrophoresis, and continuum electrostatic theory J. Am. Chem. Soc. 121 1999 4340 4347
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4340-4347
    • Caravella, J.A.1    Carbeck, J.D.2    Duffy, D.C.3    Whitesides, G.M.4    Tidor, B.5
  • 11
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • E. Cattaneo , C. Zuccato , and M. Tartari Normal huntingtin function: an alternative approach to Huntington's disease Nat. Rev. Neurosci. 6 2005 919 930
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 12
    • 0037059069 scopus 로고    scopus 로고
    • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    • F. Chiti , M. Calamai , N. Taddei , M. Stefani , G. Ramponi , and C.M. Dobson Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases Proc. Natl. Acad. Sci. U.S.A. 99 Suppl. 4 2002 16419 16426
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.SUPPL. 4 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5    Dobson, C.M.6
  • 13
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti , and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 14
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • F. Chiti , M. Stefani , N. Taddei , G. Ramponi , and C.M. Dobson Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424 2003 805 808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 16
    • 0026009211 scopus 로고
    • Cumulative site-directed charge-change replacements in bacteriophage-T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability
    • S. Daopin , E. Soderlind , W.A. Baase , J.A. Wozniak , U. Sauer , and B.W. Matthews Cumulative site-directed charge-change replacements in bacteriophage-T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability J. Mol. Biol. 221 1991 873 887
    • (1991) J. Mol. Biol. , vol.221 , pp. 873-887
    • Daopin, S.1    Soderlind, E.2    Baase, W.A.3    Wozniak, J.A.4    Sauer, U.5    Matthews, B.W.6
  • 17
    • 0037900194 scopus 로고    scopus 로고
    • Hyperthermostabilization of Bacillus licheniformis alpha-amylase and modulation of its stability over a 50 degrees C temperature range
    • N. Declerck , M. Machius , P. Joyet , G. Wiegand , R. Huber , and C. Gaillardin Hyperthermostabilization of Bacillus licheniformis alpha-amylase and modulation of its stability over a 50 degrees C temperature range Protein Eng. 16 2003 287 293
    • (2003) Protein Eng. , vol.16 , pp. 287-293
    • Declerck, N.1    MacHius, M.2    Joyet, P.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 18
    • 10044231838 scopus 로고    scopus 로고
    • Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein
    • M. del Alamo , and M.G. Mateu Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein J. Mol. Biol. 345 2005 893 906
    • (2005) J. Mol. Biol. , vol.345 , pp. 893-906
    • Del Alamo, M.1    Mateu, M.G.2
  • 19
    • 0042736853 scopus 로고    scopus 로고
    • ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization
    • M. DiDonato , L. Craig , M.E. Huff , M.M. Thayer , R.M. Cardoso , and C.J. Kassmann ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization J. Mol. Biol. 332 2003 601 615
    • (2003) J. Mol. Biol. , vol.332 , pp. 601-615
    • Didonato, M.1    Craig, L.2    Huff, M.E.3    Thayer, M.M.4    Cardoso, R.M.5    Kassmann, C.J.6
  • 20
    • 0042467574 scopus 로고    scopus 로고
    • A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme
    • M. Dumoulin , A.M. Last , A. Desmyter , K. Decanniere , D. Canet , and G. Larsson A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme Nature 424 2003 783 788
    • (2003) Nature , vol.424 , pp. 783-788
    • Dumoulin, M.1    Last, A.M.2    Desmyter, A.3    Decanniere, K.4    Canet, D.5    Larsson, G.6
  • 21
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson , and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 22
    • 0036783381 scopus 로고    scopus 로고
    • Variability in the pKa of histidine side-chains correlates with burial within proteins
    • S.P. Edgcomb , and K.P. Murphy Variability in the pKa of histidine side-chains correlates with burial within proteins Proteins 49 2002 1 6
    • (2002) Proteins , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 23
    • 0038442784 scopus 로고    scopus 로고
    • Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
    • J.S. Elam , A.B. Taylor , R. Strange , S. Antonyuk , P.A. Doucette , and J.A. Rodriguez Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS Nat. Struct. Biol. 10 2003 461 467
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 461-467
    • Elam, J.S.1    Taylor, A.B.2    Strange, R.3    Antonyuk, S.4    Doucette, P.A.5    Rodriguez, J.A.6
  • 24
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • H.J. Forman , and I. Fridovich On the stability of bovine superoxide dismutase. The effects of metals J. Biol. Chem. 248 1973 2645 2649
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 25
    • 0031568682 scopus 로고    scopus 로고
    • Using protein charge ladders to estimate the effective charges and molecular weights of proteins in solution
    • J.M. Gao , and G.M. Whitesides Using protein charge ladders to estimate the effective charges and molecular weights of proteins in solution Anal. Chem. 69 1997 575 580
    • (1997) Anal. Chem. , vol.69 , pp. 575-580
    • Gao, J.M.1    Whitesides, G.M.2
  • 27
    • 33745033613 scopus 로고    scopus 로고
    • Why are proteins charged? Networks of charge-charge interactions in proteins measured by charge ladders and capillary electrophoresis
    • I. Gitlin , J.D. Carbeck , and G.M. Whitesides Why are proteins charged? Networks of charge-charge interactions in proteins measured by charge ladders and capillary electrophoresis Angew. Chem. Int. Ed. Engl. 45 2006 3022 3060
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 3022-3060
    • Gitlin, I.1    Carbeck, J.D.2    Whitesides, G.M.3
  • 28
    • 33747177046 scopus 로고    scopus 로고
    • Effects of surface charge on denaturation of bovine carbonic anhydrase
    • I. Gitlin , K.L. Gudiksen , and G.M. Whitesides Effects of surface charge on denaturation of bovine carbonic anhydrase Chembiochem 7 2006 1241 1250
    • (2006) Chembiochem , vol.7 , pp. 1241-1250
    • Gitlin, I.1    Gudiksen, K.L.2    Whitesides, G.M.3
  • 29
    • 33644759714 scopus 로고    scopus 로고
    • Peracetylated bovine carbonic anhydrase (BCA-ac18) is kinetically more stable than native BCA to sodium dodecyl sulfate
    • I. Gitlin , K.L. Gudiksen , and G.M. Whitesides Peracetylated bovine carbonic anhydrase (BCA-ac18) is kinetically more stable than native BCA to sodium dodecyl sulfate J. Phys. Chem. B 110 2006 2372 2377
    • (2006) J. Phys. Chem. B , vol.110 , pp. 2372-2377
    • Gitlin, I.1    Gudiksen, K.L.2    Whitesides, G.M.3
  • 31
    • 33745752989 scopus 로고    scopus 로고
    • Increasing the net charge and decreasing the hydrophobicity of bovine carbonic anhydrase decreases the rate of denaturation with sodium dodecyl sulfate
    • K.L. Gudiksen , I. Gitlin , D.T. Moustakas , and G.M. Whitesides Increasing the net charge and decreasing the hydrophobicity of bovine carbonic anhydrase decreases the rate of denaturation with sodium dodecyl sulfate Biophys. J. 91 2006 298 310
    • (2006) Biophys. J. , vol.91 , pp. 298-310
    • Gudiksen, K.L.1    Gitlin, I.2    Moustakas, D.T.3    Whitesides, G.M.4
  • 32
    • 16844371746 scopus 로고    scopus 로고
    • Eliminating positively charged lysine epsilon-NH3+ groups on the surface of carbonic anhydrase has no significant influence on its folding from sodium dodecyl sulfate
    • K.L. Gudiksen , I. Gitlin , J. Yang , A.R. Urbach , D.T. Moustakas , and G.M. Whitesides Eliminating positively charged lysine epsilon-NH3+ groups on the surface of carbonic anhydrase has no significant influence on its folding from sodium dodecyl sulfate J. Am. Chem. Soc. 127 2005 4707 4714
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4707-4714
    • Gudiksen, K.L.1    Gitlin, I.2    Yang, J.3    Urbach, A.R.4    Moustakas, D.T.5    Whitesides, G.M.6
  • 34
    • 0014799161 scopus 로고
    • Alpha-chymotrypsin: A case study of substituent constants and regression analysis in enzymic structure-activity relationships
    • C. Hansch , and E. Coats Alpha-chymotrypsin: a case study of substituent constants and regression analysis in enzymic structure-activity relationships J. Pharm. Sci. 59 1970 731 743
    • (1970) J. Pharm. Sci. , vol.59 , pp. 731-743
    • Hansch, C.1    Coats, E.2
  • 35
    • 33947490704 scopus 로고
    • The use of substituent constants in the analysis of the structure-activity relationship in penicillin derivatives
    • C. Hansch , and A.R. Steward The use of substituent constants in the analysis of the structure-activity relationship in penicillin derivatives J. Med. Chem. 7 1964 691 694
    • (1964) J. Med. Chem. , vol.7 , pp. 691-694
    • Hansch, C.1    Steward, A.R.2
  • 36
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • P. Harjes , and E.E. Wanker The hunt for huntingtin function: interaction partners tell many different stories Trends Biochem. Sci. 28 2003 425 433
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 37
    • 0031911637 scopus 로고    scopus 로고
    • Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis
    • P.J. Hart , H. Liu , M. Pellegrini , A.M. Nersissian , E.B. Gralla , and J.S. Valentine Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis Protein Sci. 7 1998 545 555
    • (1998) Protein Sci. , vol.7 , pp. 545-555
    • Hart, P.J.1    Liu, H.2    Pellegrini, M.3    Nersissian, A.M.4    Gralla, E.B.5    Valentine, J.S.6
  • 38
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • L.J. Hayward , J.A. Rodriguez , J.W. Kim , A. Tiwari , J.J. Goto , and D.E. Cabelli Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis J. Biol. Chem. 277 2002 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
  • 39
    • 11144357460 scopus 로고    scopus 로고
    • Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants
    • M.A. Hough , J.G. Grossmann , S.V. Antonyuk , R.W. Strange , P.A. Doucette , and J.A. Rodriguez Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants Proc. Natl. Acad. Sci. U.S.A. 101 2004 5976 5981
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 5976-5981
    • Hough, M.A.1    Grossmann, J.G.2    Antonyuk, S.V.3    Strange, R.W.4    Doucette, P.A.5    Rodriguez, J.A.6
  • 40
    • 0031591073 scopus 로고    scopus 로고
    • Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution
    • K.Y. Hwang , H.K. Song , C. Chang , J. Lee , S.Y. Lee , and K.K. Kim Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution Mol. Cells 7 1997 251 258
    • (1997) Mol. Cells , vol.7 , pp. 251-258
    • Hwang, K.Y.1    Song, H.K.2    Chang, C.3    Lee, J.4    Lee, S.Y.5    Kim, K.K.6
  • 41
    • 0037084116 scopus 로고    scopus 로고
    • Designing protein denaturants: Synthetic agents induce cytochrome c unfolding at low concentrations and stoichiometries
    • R. Jain , and A.D. Hamilton Designing protein denaturants: synthetic agents induce cytochrome c unfolding at low concentrations and stoichiometries Angew. Chem. Int. Ed. Engl. 41 2002 641 643
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 641-643
    • Jain, R.1    Hamilton, A.D.2
  • 42
    • 38349124133 scopus 로고    scopus 로고
    • Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors
    • S.M. Johnson , S. Connelly , I.A. Wilson , and J.W. Kelly Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors J. Med. Chem. 51 2008 260 270
    • (2008) J. Med. Chem. , vol.51 , pp. 260-270
    • Johnson, S.M.1    Connelly, S.2    Wilson, I.A.3    Kelly, J.W.4
  • 43
    • 54549114463 scopus 로고    scopus 로고
    • Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies
    • S.M. Johnson , S. Connelly , I.A. Wilson , and J.W. Kelly Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies J. Med. Chem. 51 2008 6348 6358
    • (2008) J. Med. Chem. , vol.51 , pp. 6348-6358
    • Johnson, S.M.1    Connelly, S.2    Wilson, I.A.3    Kelly, J.W.4
  • 44
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • S.M. Johnson , R.L. Wiseman , Y. Sekijima , N.S. Green , S.L. Adamski-Werner , and J.W. Kelly Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses Acc. Chem. Res. 38 2005 911 921
    • (2005) Acc. Chem. Res. , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5    Kelly, J.W.6
  • 45
    • 0015217710 scopus 로고
    • Further characterization of bovine superoxide dismutase and its isolation from bovine heart
    • B.B.J. Keele , J.M. McCord , and I. Fridovich Further characterization of bovine superoxide dismutase and its isolation from bovine heart J. Biol. Chem. 246 1971 2875 2880
    • (1971) J. Biol. Chem. , vol.246 , pp. 2875-2880
    • Keele, B.B.J.1    McCord, J.M.2    Fridovich, I.3
  • 47
    • 78650123745 scopus 로고    scopus 로고
    • Amyloid beta-protein and amyloid precursor protein: How "seminal" are they in Alzheimer's disease?
    • E. Koo Amyloid beta-protein and amyloid precursor protein: how "seminal" are they in Alzheimer's disease? J. Neurochem. 98 2006 12 12
    • (2006) J. Neurochem. , vol.98 , pp. 12
    • Koo, E.1
  • 48
    • 42149143745 scopus 로고    scopus 로고
    • Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding
    • V.M. Krishnamurthy , G.K. Kaufman , A.R. Urbach , I. Gitlin , K.L. Gudiksen , and D.B. Weibel Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding Chem. Rev. 108 2008 946 1051
    • (2008) Chem. Rev. , vol.108 , pp. 946-1051
    • Krishnamurthy, V.M.1    Kaufman, G.K.2    Urbach, A.R.3    Gitlin, I.4    Gudiksen, K.L.5    Weibel, D.B.6
  • 49
    • 17644370014 scopus 로고    scopus 로고
    • Polymer-surfactant and protein-surfactant interactions
    • C. La Mesa Polymer-surfactant and protein-surfactant interactions J. Colloid Interface Sci. 286 2005 148 157
    • (2005) J. Colloid Interface Sci. , vol.286 , pp. 148-157
    • La Mesa, C.1
  • 50
    • 34548174652 scopus 로고    scopus 로고
    • Supercharging proteins can impart unusual resilience
    • M.S. Lawrence , K.J. Phillips , and D.R. Liu Supercharging proteins can impart unusual resilience J. Am. Chem. Soc. 129 2007 10110 10112
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10110-10112
    • Lawrence, M.S.1    Phillips, K.J.2    Liu, D.R.3
  • 51
    • 0030855080 scopus 로고    scopus 로고
    • Stabilization of protein structures
    • B. Lee , and G. Vasmatzis Stabilization of protein structures Curr. Opin. Biotechnol. 8 1997 423 428
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 423-428
    • Lee, B.1    Vasmatzis, G.2
  • 52
    • 22244489417 scopus 로고    scopus 로고
    • Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
    • M.J. Lindberg , R. Bystrom , N. Boknas , P.M. Andersen , and M. Oliveberg Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants Proc. Natl. Acad. Sci. U.S.A. 102 2005 9754 9759
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 9754-9759
    • Lindberg, M.J.1    Bystrom, R.2    Boknas, N.3    Andersen, P.M.4    Oliveberg, M.5
  • 53
    • 8644290067 scopus 로고    scopus 로고
    • Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers
    • M.J. Lindberg , J. Normark , A. Holmgren , and M. Oliveberg Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers Proc. Natl. Acad. Sci. U.S.A. 101 2004 15893 15898
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15893-15898
    • Lindberg, M.J.1    Normark, J.2    Holmgren, A.3    Oliveberg, M.4
  • 54
    • 34948886235 scopus 로고    scopus 로고
    • Interaction between casein and the oppositely charged surfactant
    • Y. Liu , and R. Guo Interaction between casein and the oppositely charged surfactant Biomacromolecules. 8 2007 2902 2908
    • (2007) Biomacromolecules. , vol.8 , pp. 2902-2908
    • Liu, Y.1    Guo, R.2
  • 56
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis alpha-amylase through a disorder-&Very Thin Space; order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • M. Machius , N. Declerck , R. Huber , and G. Wiegand Activation of Bacillus licheniformis alpha-amylase through a disorder-&Very Thin Space order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad Structure 6 1998 281 292
    • (1998) Structure , vol.6 , pp. 281-292
    • MacHius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 57
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
    • M. Machius , N. Declerck , R. Huber , and G. Wiegand Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface J. Biol. Chem. 278 2003 11546 11553
    • (2003) J. Biol. Chem. , vol.278 , pp. 11546-11553
    • MacHius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 58
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution
    • M. Machius , G. Wiegand , and R. Huber Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution J. Mol. Biol. 246 1995 545 559
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • MacHius, M.1    Wiegand, G.2    Huber, R.3
  • 59
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • B.W. Matthews Structural and genetic analysis of protein stability Annu. Rev. Biochem. 62 1993 139 160
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 60
    • 0036728536 scopus 로고    scopus 로고
    • Measurement of alpha-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the Ceralpha assay: Collaborative study
    • B.V. McCleary , M. McNally , D. Monaghan , and D.C. Mugford Measurement of alpha-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the Ceralpha assay: collaborative study J. AOAC Int. 85 2002 1096 1102
    • (2002) J. AOAC Int. , vol.85 , pp. 1096-1102
    • McCleary, B.V.1    McNally, M.2    Monaghan, D.3    Mugford, D.C.4
  • 61
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord , and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 62
    • 0034669239 scopus 로고    scopus 로고
    • Determination of effective protein charge by capillary electrophoresis: Effects of charge regulation in the analysis of charge ladders
    • M.K. Menon , and A.L. Zydney Determination of effective protein charge by capillary electrophoresis: effects of charge regulation in the analysis of charge ladders Anal. Chem. 72 2000 5714 5717
    • (2000) Anal. Chem. , vol.72 , pp. 5714-5717
    • Menon, M.K.1    Zydney, A.L.2
  • 63
  • 64
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • S. Miller , A.M. Lesk , J. Janin , and C. Chothia The accessible surface area and stability of oligomeric proteins Nature 328 1987 834 836
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 65
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • G.L. Millhauser Copper and the prion protein: methods, structures, function, and disease Annu. Rev. Phys. Chem. 58 2007 299 320
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 66
    • 0027616709 scopus 로고
    • How my interest in proteins developed
    • L. Pauling How my interest in proteins developed Protein Sci. 2 1993 1060 1063
    • (1993) Protein Sci. , vol.2 , pp. 1060-1063
    • Pauling, L.1
  • 67
    • 34247505040 scopus 로고    scopus 로고
    • Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein
    • S.Z. Potter , H. Zhu , B.F. Shaw , J.A. Rodriguez , P.A. Doucette , and S.H. Sohn Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein J. Am. Chem. Soc. 129 2007 4575 4583
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4575-4583
    • Potter, S.Z.1    Zhu, H.2    Shaw, B.F.3    Rodriguez, J.A.4    Doucette, P.A.5    Sohn, S.H.6
  • 68
    • 1942501776 scopus 로고    scopus 로고
    • A possible therapeutic target for Lou Gehrig's disease
    • S.S. Ray , and P.T. Lansbury Jr. A possible therapeutic target for Lou Gehrig's disease Proc. Natl. Acad. Sci. U.S.A. 101 2004 5701 5702
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 5701-5702
    • Ray, S.S.1    Lansbury, Jr.P.T.2
  • 69
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • S.S. Ray , R.J. Nowak , R.H. Brown Jr. , and P.T. Lansbury Jr. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation Proc. Natl. Acad. Sci. U.S.A. 102 2005 3639 3644
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3639-3644
    • Ray, S.S.1    Nowak, R.J.2    Brown, Jr.R.H.3    Lansbury, Jr.P.T.4
  • 70
    • 0001495297 scopus 로고
    • Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: Chain tracing and metal ligands
    • J. Richardson , K.A. Thomas , B.H. Rubin , and D.C. Richardson Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands Proc. Natl. Acad. Sci. U.S.A. 72 1975 1349 1353
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 1349-1353
    • Richardson, J.1    Thomas, K.A.2    Rubin, B.H.3    Richardson, D.C.4
  • 71
    • 0025772266 scopus 로고
    • Correlation of electrophoretic mobilities from capillary electrophoresis with physicochemical properties of proteins and peptides
    • E.C. Rickard , M.M. Strohl , and R.G. Nielsen Correlation of electrophoretic mobilities from capillary electrophoresis with physicochemical properties of proteins and peptides Anal. Biochem. 197 1991 197 207
    • (1991) Anal. Biochem. , vol.197 , pp. 197-207
    • Rickard, E.C.1    Strohl, M.M.2    Nielsen, R.G.3
  • 72
    • 34848900432 scopus 로고    scopus 로고
    • Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS
    • B.R. Roberts , J.A. Tainer , E.D. Getzoff , D.A. Malencik , S.R. Anderson , and V.C. Bomben Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS J. Mol. Biol. 373 2007 877 890
    • (2007) J. Mol. Biol. , vol.373 , pp. 877-890
    • Roberts, B.R.1    Tainer, J.A.2    Getzoff, E.D.3    Malencik, D.A.4    Anderson, S.R.5    Bomben, V.C.6
  • 73
    • 40549110221 scopus 로고    scopus 로고
    • Effects of long-range electrostatic forces on simulated protein folding kinetics
    • A. Robertson , E. Luttmann , and V.S. Pande Effects of long-range electrostatic forces on simulated protein folding kinetics J. Comput. Chem. 29 2008 694 700
    • (2008) J. Comput. Chem. , vol.29 , pp. 694-700
    • Robertson, A.1    Luttmann, E.2    Pande, V.S.3
  • 75
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
    • J.A. Rodriguez , J.S. Valentine , D.K. Eggers , J.A. Roe , A. Tiwari , and R.H. Brown Jr. Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase J. Biol. Chem. 277 2002 15932 15937
    • (2002) J. Biol. Chem. , vol.277 , pp. 15932-15937
    • Rodriguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwari, A.5    Brown, Jr.R.H.6
  • 76
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • D.R. Rosen , T. Siddique , D. Patterson , D.A. Figlewicz , P. Sapp , and A. Hentati Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis Nature 362 1993 59 62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5    Hentati, A.6
  • 77
    • 57749208693 scopus 로고    scopus 로고
    • Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases
    • J.A. Rumfeldt , J.R. Lepock , and E.M. Meiering Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases J. Mol. Biol. 385 2009 278 298
    • (2009) J. Mol. Biol. , vol.385 , pp. 278-298
    • Rumfeldt, J.A.1    Lepock, J.R.2    Meiering, E.M.3
  • 78
    • 34447280364 scopus 로고    scopus 로고
    • Detergent alkaline proteases: Enzymatic properties, genes, and crystal structures
    • K. Saeki , K. Ozaki , T. Kobayashi , and S. Ito Detergent alkaline proteases: enzymatic properties, genes, and crystal structures J. Biosci. Bioeng. 103 2007 501 508
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 501-508
    • Saeki, K.1    Ozaki, K.2    Kobayashi, T.3    Ito, S.4
  • 79
    • 34547120448 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
    • E. Sandelin , A. Nordlund , P.M. Andersen , S.S. Marklund , and M. Oliveberg Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins J. Biol. Chem. 282 2007 21230 21236
    • (2007) J. Biol. Chem. , vol.282 , pp. 21230-21236
    • Sandelin, E.1    Nordlund, A.2    Andersen, P.M.3    Marklund, S.S.4    Oliveberg, M.5
  • 80
    • 33745813117 scopus 로고    scopus 로고
    • Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry
    • B.F. Shaw , A. Durazo , A.M. Nersissian , J.P. Whitelegge , K.F. Faull , and J.S. Valentine Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry J. Biol. Chem. 281 2006 18167 18176
    • (2006) J. Biol. Chem. , vol.281 , pp. 18167-18176
    • Shaw, B.F.1    Durazo, A.2    Nersissian, A.M.3    Whitelegge, J.P.4    Faull, K.F.5    Valentine, J.S.6
  • 81
    • 48249157846 scopus 로고    scopus 로고
    • Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation
    • B.F. Shaw , G.F. Schneider , B. Bilgicer , G.K. Kaufman , J.M. Neveu , and W.S. Lane Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation Protein Sci. 17 2008 1446 1455
    • (2008) Protein Sci. , vol.17 , pp. 1446-1455
    • Shaw, B.F.1    Schneider, G.F.2    Bilgicer, B.3    Kaufman, G.K.4    Neveu, J.M.5    Lane, W.S.6
  • 82
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • B.F. Shaw , and J.S. Valentine How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem. Sci. 32 2007 78 85
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 83
    • 0344839082 scopus 로고    scopus 로고
    • Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: Implications for the pathology of familial amyotrophic lateral sclerosis
    • E.L. Shipp , F. Cantini , I. Bertini , J.S. Valentine , and L. Banci Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis Biochemistry 42 2003 1890 1899
    • (2003) Biochemistry , vol.42 , pp. 1890-1899
    • Shipp, E.L.1    Cantini, F.2    Bertini, I.3    Valentine, J.S.4    Banci, L.5
  • 84
    • 33744903388 scopus 로고    scopus 로고
    • Plant genetic engineering to improve biomass characteristics for biofuels
    • M. Sticklen Plant genetic engineering to improve biomass characteristics for biofuels Curr. Opin. Biotechnol. 17 2006 315 319
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 315-319
    • Sticklen, M.1
  • 85
    • 0037427449 scopus 로고    scopus 로고
    • The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
    • R.W. Strange , S. Antonyuk , M.A. Hough , P.A. Doucette , J.A. Rodriguez , and P.J. Hart The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis J. Mol. Biol. 328 2003 877 891
    • (2003) J. Mol. Biol. , vol.328 , pp. 877-891
    • Strange, R.W.1    Antonyuk, S.2    Hough, M.A.3    Doucette, P.A.4    Rodriguez, J.A.5    Hart, P.J.6
  • 86
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • K. Sugase , H.J. Dyson , and P.E. Wright Mechanism of coupled folding and binding of an intrinsically disordered protein Nature 447 2007 1021 1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 88
    • 0034018237 scopus 로고    scopus 로고
    • Influence of emission from rice straw burning on bronchial asthma in children
    • K. Torigoe , S. Hasegawa , O. Numata , S. Yazaki , M. Matsunaga , and N. Boku Influence of emission from rice straw burning on bronchial asthma in children Pediatr. Int. 42 2000 143 150
    • (2000) Pediatr. Int. , vol.42 , pp. 143-150
    • Torigoe, K.1    Hasegawa, S.2    Numata, O.3    Yazaki, S.4    Matsunaga, M.5    Boku, N.6
  • 89
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • J.S. Valentine , P.A. Doucette , and S. Zittin Potter Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis Annu. Rev. Biochem. 74 2005 563 593
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 91
    • 34948823398 scopus 로고    scopus 로고
    • Chemical biology: More charges against aggregation
    • M. Vendruscolo , and C.M. Dobson Chemical biology: more charges against aggregation Nature 449 2007 555
    • (2007) Nature , vol.449 , pp. 555
    • Vendruscolo, M.1    Dobson, C.M.2
  • 92
    • 17144471008 scopus 로고    scopus 로고
    • Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal
    • R. Walser , P.H. Hunenberger , and W.F. van Gunsteren Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal Proteins: Struct. Funct. Bioinf. 43 2001 509 519
    • (2001) Proteins: Struct. Funct. Bioinf. , vol.43 , pp. 509-519
    • Walser, R.1    Hunenberger, P.H.2    Van Gunsteren, W.F.3
  • 93
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • Y.C. Wang , and Y. Ha The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain Mol. Cell 15 2004 343 353
    • (2004) Mol. Cell , vol.15 , pp. 343-353
    • Wang, Y.C.1    Ha, Y.2
  • 94
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: Age-dependent and tissue-specific accumulation
    • J. Wang , G. Xu , and D.R. Borchelt High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation Neurobiol. Dis. 9 2002 139 148
    • (2002) Neurobiol. Dis. , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 95
    • 0023054659 scopus 로고
    • Continuum dielectric modeling of the protein solvent system, and calculation of the long-range electrostatic-field of the enzyme phosphoglycerate mutase
    • J. Warwicker Continuum dielectric modeling of the protein solvent system, and calculation of the long-range electrostatic-field of the enzyme phosphoglycerate mutase J. Theor. Biol. 121 1986 199 210
    • (1986) J. Theor. Biol. , vol.121 , pp. 199-210
    • Warwicker, J.1
  • 97
    • 0032508498 scopus 로고    scopus 로고
    • Long-range electrostatic trapping of single-protein molecules at a liquid-solid interface
    • X.H.N. Xu , and E.S. Yeung Long-range electrostatic trapping of single-protein molecules at a liquid-solid interface Science 281 1998 1650 1653
    • (1998) Science , vol.281 , pp. 1650-1653
    • Xu, X.H.N.1    Yeung, E.S.2
  • 98
    • 22044452188 scopus 로고    scopus 로고
    • The function of the neuronal proteins shc and huntingtin in stem cells and neurons - pharmacologic exploitation for human brain diseases
    • C. Zuccato , L. Conti , E. Reitano , M. Tartari , and E. Cattaneo The function of the neuronal proteins shc and huntingtin in stem cells and neurons - pharmacologic exploitation for human brain diseases Stem Cell Biol. Dev. Plast. 1049 2005 39 50
    • (2005) Stem Cell Biol. Dev. Plast. , vol.1049 , pp. 39-50
    • Zuccato, C.1    Conti, L.2    Reitano, E.3    Tartari, M.4    Cattaneo, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.