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Volumn 31, Issue 2, 2005, Pages 141-150

Protein misfolding, aggregation, and degradation in disease

Author keywords

Conformational disease; Protein aggregation; Protein aggregation diseases; Protein folding; Protein misfolding; Protein quality control

Indexed keywords

CONFORMATIONS; DISEASES; GENES; PATHOLOGY;

EID: 24944456875     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:31:2:141     Document Type: Review
Times cited : (57)

References (68)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R. W. and Lomas, D. A. (1997) Conformational disease. Lancet 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 2
    • 0037011795 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency - A model for conformational diseases
    • Carrell, R. W. and Lomas, D. A. (2002) Alpha1-antitrypsin deficiency - a model for conformational diseases. N. Engl. J. Med. 346, 45-53.
    • (2002) N. Engl. J. Med. , vol.346 , pp. 45-53
    • Carrell, R.W.1    Lomas, D.A.2
  • 3
    • 0036301160 scopus 로고    scopus 로고
    • Familial conformational diseases and dementias
    • Crowther, D. C. (2002) Familial conformational diseases and dementias. Hum. Mutat. 20, 1-14.
    • (2002) Hum. Mutat. , vol.20 , pp. 1-14
    • Crowther, D.C.1
  • 4
    • 0032948791 scopus 로고    scopus 로고
    • Identification of novel and known mutations in the genes for keratin 5 and 14 in Danish patients with epidermolysis bullosa simplex: Correlation between genotype and phenotype
    • Sorensen, C. B., Ladekjaer-Mikkelsen, A. S., Andresen, B. S., et al. (1999) Identification of novel and known mutations in the genes for keratin 5 and 14 in Danish patients with epidermolysis bullosa simplex: correlation between genotype and phenotype. J. Invest Dermatol. 112, 184-190.
    • (1999) J. Invest Dermatol. , vol.112 , pp. 184-190
    • Sorensen, C.B.1    Ladekjaer-Mikkelsen, A.S.2    Andresen, B.S.3
  • 5
    • 0032848187 scopus 로고    scopus 로고
    • Folding of peptide models of collagen and misfolding in disease
    • Baum, J. and Brodsky, B. (1999) Folding of peptide models of collagen and misfolding in disease. Curr. Opin. Struct. Biol. 9, 122-128.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 122-128
    • Baum, J.1    Brodsky, B.2
  • 6
    • 0032837587 scopus 로고    scopus 로고
    • The inheritance of hypertrophic cardiomyopathy
    • Burch, M. and Blair, E. (1999) The inheritance of hypertrophic cardiomyopathy. Pediatr. Cardiol. 20, 313-316.
    • (1999) Pediatr. Cardiol. , vol.20 , pp. 313-316
    • Burch, M.1    Blair, E.2
  • 7
    • 85047695905 scopus 로고    scopus 로고
    • Tumour p53 mutations exhibit promoter selective dominance over wild type p53
    • Monti, P., Campomenosi, P., Ciribilli, Y., et al. (2002) Tumour p53 mutations exhibit promoter selective dominance over wild type p53. Oncogene 21, 1641-1648.
    • (2002) Oncogene , vol.21 , pp. 1641-1648
    • Monti, P.1    Campomenosi, P.2    Ciribilli, Y.3
  • 9
    • 0035000631 scopus 로고    scopus 로고
    • The role of chaperone-assisted folding and quality control in inborn errors of metabolism: Protein folding disorders
    • Gregersen, N., Bross, P., Andresen, B. S., Pedersen, C. B., Corydon, T. J., and Bolund, L. (2001) The role of chaperone-assisted folding and quality control in inborn errors of metabolism: protein folding disorders. J. Inherit. Metab. Dis. 24, 189-212.
    • (2001) J. Inherit. Metab. Dis. , vol.24 , pp. 189-212
    • Gregersen, N.1    Bross, P.2    Andresen, B.S.3    Pedersen, C.B.4    Corydon, T.J.5    Bolund, L.6
  • 10
    • 0034911822 scopus 로고    scopus 로고
    • Degradation of mutant proteins, underlying "loss of function" phenotypes, plays a major role in genetic disease
    • Waters, P. J. (2001) Degradation of mutant proteins, underlying "loss of function" phenotypes, plays a major role in genetic disease. Curr. Issues Mol. Biol. 3, 57-65.
    • (2001) Curr. Issues Mol. Biol. , vol.3 , pp. 57-65
    • Waters, P.J.1
  • 11
    • 0033361889 scopus 로고    scopus 로고
    • Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein
    • Riordan, J. R. (1999) Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein. Am. J. Hum. Genet. 64, 1499-1504.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1499-1504
    • Riordan, J.R.1
  • 12
    • 0034110962 scopus 로고    scopus 로고
    • Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype
    • Waters, P. J., Parniak, M. A., Akerman, B. R., and Scriver, C. R. (2000) Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype. Mol. Genet. Metab. 69, 101-110.
    • (2000) Mol. Genet. Metab. , vol.69 , pp. 101-110
    • Waters, P.J.1    Parniak, M.A.2    Akerman, B.R.3    Scriver, C.R.4
  • 13
    • 0037240146 scopus 로고    scopus 로고
    • How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: Insights from in vitro expression
    • Waters, P. J. (2003) How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: insights from in vitro expression. Hum. Mutat. 21, 357-369.
    • (2003) Hum. Mutat. , vol.21 , pp. 357-369
    • Waters, P.J.1
  • 14
    • 0033049537 scopus 로고    scopus 로고
    • Misfolded proteins in the endoplasmic reticulum
    • Perlmutter, D. H. (1999) Misfolded proteins in the endoplasmic reticulum. Lab. Invest. 79, 623-638.
    • (1999) Lab. Invest. , vol.79 , pp. 623-638
    • Perlmutter, D.H.1
  • 15
    • 0034866130 scopus 로고    scopus 로고
    • Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship
    • Gregersen, N., Andresen, B. S., Corydon, M. J., et al. (2001) Mutation analysis in mitochondrial fatty acid oxidation defects: exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. Hum. Mutat. 18, 169-189.
    • (2001) Hum. Mutat. , vol.18 , pp. 169-189
    • Gregersen, N.1    Andresen, B.S.2    Corydon, M.J.3
  • 16
    • 0842330592 scopus 로고    scopus 로고
    • Genetic defects in fatty acid beta-oxidation and acyl-CoA dehydrogenases
    • Gregersen, N., Bross, P., and Andresen, B. S. (2004) Genetic defects in fatty acid beta-oxidation and acyl-CoA dehydrogenases. Eur. J. Biochem. 271, 470-482.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 470-482
    • Gregersen, N.1    Bross, P.2    Andresen, B.S.3
  • 18
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 20
    • 33745099303 scopus 로고    scopus 로고
    • Chapter 13.1: Protein folding and misfolding: The role of cellular protein quality control systems in inherited disorders
    • (Scriver, C. R., Beaudet, A. L., Valle, D., Sly, W. S., Vogelstein, B., Childs, B., and Kinzler, K. W., eds.), McGraw-Hill, New York
    • Gregersen, N., Bross, P., and Jørgensen, M. M. Chapter 13.1: Protein folding and misfolding: The role of cellular protein quality control systems in inherited disorders. In: MMBID - ONLINE (Scriver, C. R., Beaudet, A. L., Valle, D., Sly, W. S., Vogelstein, B., Childs, B., and Kinzler, K. W., eds.), McGraw-Hill, New York, URL: http://genetics.accessmedicine.com.
    • MMBID - ONLINE
    • Gregersen, N.1    Bross, P.2    Jørgensen, M.M.3
  • 22
    • 0033987778 scopus 로고    scopus 로고
    • Human gene mutation database - A biomedical information and research resource
    • Krawczak, M., Ball, E. V., Fenton, I., et al. (2000) Human gene mutation database - a biomedical information and research resource. Hum. Mutat. 15, 45-51.
    • (2000) Hum. Mutat. , vol.15 , pp. 45-51
    • Krawczak, M.1    Ball, E.V.2    Fenton, I.3
  • 23
    • 0036207384 scopus 로고    scopus 로고
    • Listening to silence and understanding nonsense: Exonic mutations that affect splicing
    • Cartegni, L., Chew, S. L., and Krainer, A. R. (2002) Listening to silence and understanding nonsense: exonic mutations that affect splicing. Nut. Rev. Genet. 3, 285-298.
    • (2002) Nut. Rev. Genet. , vol.3 , pp. 285-298
    • Cartegni, L.1    Chew, S.L.2    Krainer, A.R.3
  • 24
    • 0037072890 scopus 로고    scopus 로고
    • Aggregation of misfolded proteins can be a selective process dependent upon peptide composition
    • Milewski, M. I., Mickle, J. E., Forrest, J. K., Stanton, B. A., and Cutting, G. R. (2002) Aggregation of misfolded proteins can be a selective process dependent upon peptide composition. J. Biol. Chem. 277, 34462-34470.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34462-34470
    • Milewski, M.I.1    Mickle, J.E.2    Forrest, J.K.3    Stanton, B.A.4    Cutting, G.R.5
  • 25
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A., Ward, C. L., and Kopito, R. R. (1998) Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 26
    • 0347481388 scopus 로고    scopus 로고
    • Misfolding, Degradation, and aggregation of variant proteins: The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency
    • Pedersen, C. B., Bross, P., Winter, V. S., et al. (2003) Misfolding, Degradation, and aggregation of variant proteins: the molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency. J. Biol. Chem. 278, 47449-47458.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47449-47458
    • Pedersen, C.B.1    Bross, P.2    Winter, V.S.3
  • 27
    • 0032812042 scopus 로고    scopus 로고
    • Biochemical and molecular correlations in carnitine palmitoyltransferase II deficiency
    • Vladutiu, G. D. (1999) Biochemical and molecular correlations in carnitine palmitoyltransferase II deficiency. Muscle Nerve 22, 949-951.
    • (1999) Muscle Nerve , vol.22 , pp. 949-951
    • Vladutiu, G.D.1
  • 28
    • 0032948791 scopus 로고    scopus 로고
    • Identification of novel and known mutations in the genes for keratin 5 and 14 in Danish patients with epidermolysis bullosa simplex: Correlation between genotype and phenotype
    • Sorensen, C. B., Ladekjaer-Mikkelsen, A. S., Andresen, B. S., et al. (1999) Identification of novel and known mutations in the genes for keratin 5 and 14 in Danish patients with epidermolysis bullosa simplex: correlation between genotype and phenotype. J. Invest Dermatol. 112, 184-190.
    • (1999) J. Invest Dermatol. , vol.112 , pp. 184-190
    • Sorensen, C.B.1    Ladekjaer-Mikkelsen, A.S.2    Andresen, B.S.3
  • 29
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. (2001) The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond B Biol. Sci. 356, 133-145.
    • (2001) Philos. Trans. R. Soc. Lond B Biol. Sci. , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 30
    • 0028593988 scopus 로고
    • A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency
    • Wu, Y., Whitman, I., Molmenti, E., Moore, K., Hippenmeyer, P., and Perlmutter, D. H. (1994) A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. Proc. Natl. Acad. Sci. USA 91, 9014-9018.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9014-9018
    • Wu, Y.1    Whitman, I.2    Molmenti, E.3    Moore, K.4    Hippenmeyer, P.5    Perlmutter, D.H.6
  • 31
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T., and Carrell, R. W. (1992) The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 357, 605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 32
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz, M. F. (1999) Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24, 58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 33
    • 0036304650 scopus 로고    scopus 로고
    • Modification of brain aging and neurodegenerative disorders by genes, diet, and behavior
    • Mattson, M. P., Chan, S. L., and Duan, W. (2002) Modification of brain aging and neurodegenerative disorders by genes, diet, and behavior. Physiol. Rev. 82, 637-672.
    • (2002) Physiol. Rev. , vol.82 , pp. 637-672
    • Mattson, M.P.1    Chan, S.L.2    Duan, W.3
  • 34
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., Hardy, J., and Fischbeck, K. H. (2002) Toxic proteins in neurodegenerative disease. Science 296, 1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 35
    • 0036720019 scopus 로고    scopus 로고
    • Mouse and fly models of neurodegeneration
    • Zoghbi, H. Y. and Botas, J. (2002) Mouse and fly models of neurodegeneration. Trends Genet. 18, 463-471.
    • (2002) Trends Genet. , vol.18 , pp. 463-471
    • Zoghbi, H.Y.1    Botas, J.2
  • 36
    • 0036166319 scopus 로고    scopus 로고
    • Kinetic partitioning of protein folding and aggregation
    • Chiti, F., Taddei, N., Baroni, F., et al. (2002) Kinetic partitioning of protein folding and aggregation. Nat. Struct. Biol. 9, 137-143.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 137-143
    • Chiti, F.1    Taddei, N.2    Baroni, F.3
  • 37
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto, C. (2001) Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498, 204-207.
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 38
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., Giannoni, E., Chiti, F., et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3
  • 39
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 40
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 41
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman, J. H. and Perlmutter, D. H. (2000) Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am. J. Physiol Gastrointest. Liver Physiol. 279, G961-G974.
    • (2000) Am. J. Physiol Gastrointest. Liver Physiol. , vol.279
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 42
    • 0023123336 scopus 로고
    • A putative protein-sequestration site involving intermediate filaments for protein degradation by autophagy. Studies with transplanted Sendai-viral envelope proteins in HTC cells
    • Earl, R. T., Mangiapane, E. H., Billett, E. E., and Mayer, R. J. (1987) A putative protein-sequestration site involving intermediate filaments for protein degradation by autophagy. Studies with transplanted Sendai-viral envelope proteins in HTC cells. Biochem. J. 241, 809-815.
    • (1987) Biochem. J. , vol.241 , pp. 809-815
    • Earl, R.T.1    Mangiapane, E.H.2    Billett, E.E.3    Mayer, R.J.4
  • 43
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K., and Martoglio, B. (2002) Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296, 2215-2218.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 44
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion
    • Yang, Y., Turner, R. S., and Gaut, J. R. (1998) The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. J. Biol. Chem. 273, 25552-25555.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 45
    • 0034816052 scopus 로고    scopus 로고
    • Activation of NF-kappaB in airway epithelial cells is dependent on CFTR trafficking and Cl- Channel function
    • Weber, A. J., Soong, G., Bryan, R., Saba, S., and Prince, A. (2001) Activation of NF-kappaB in airway epithelial cells is dependent on CFTR trafficking and Cl- channel function. Am. J. Physiol Lung Cell Mol. Physiol. 281, L71-L78.
    • (2001) Am. J. Physiol Lung Cell Mol. Physiol. , vol.281
    • Weber, A.J.1    Soong, G.2    Bryan, R.3    Saba, S.4    Prince, A.5
  • 47
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky, V. N., Lee, H. J., Li, J., Fink, A. L., and Lee, S. J. (2001) Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations. J. Biol. Chem. 276, 43495-43498.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 48
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal, M. F. (2000) Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 23, 298-304.
    • (2000) Trends Neurosci. , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 49
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield, D. A. and Kanski, J. (2001) Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech. Ageing Dev. 122, 945-962.
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 50
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M., and Kopito, R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 51
    • 0035978485 scopus 로고    scopus 로고
    • The unfolded protein response and Alzheimer's disease
    • Imaizumi, K., Miyoshi, K., Katayama, T., et al. (2001) The unfolded protein response and Alzheimer's disease. Biochim. Biophys. Acta 1536, 85-96.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 85-96
    • Imaizumi, K.1    Miyoshi, K.2    Katayama, T.3
  • 52
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: Signaling for suicide and survival
    • Martindale, J. L. and Holbrook, N. J. (2002) Cellular response to oxidative stress: signaling for suicide and survival. J. Cell Physiol. 192, 1-15.
    • (2002) J. Cell Physiol. , vol.192 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 53
    • 0037133290 scopus 로고    scopus 로고
    • Polyglutamine disease: Acetyltransferases awry
    • Hughes, R. E. (2002) Polyglutamine disease: acetyltransferases awry. Curr. Biol. 12, R141-R143.
    • (2002) Curr. Biol. , vol.12
    • Hughes, R.E.1
  • 54
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation
    • Schaffar, G., Breuer, P., Boteva, R., et al. (2004) Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol. Cell 15, 95-105.
    • (2004) Mol. Cell , vol.15 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3
  • 56
    • 0034703065 scopus 로고    scopus 로고
    • Expression analysis of phenylketonuria mutations. Effect on folding and stability of the phenylalanine hydroxylase protein
    • Gamez, A., Perez, B., Ugarte, M., and Desviat, L. R. (2000) Expression analysis of phenylketonuria mutations. Effect on folding and stability of the phenylalanine hydroxylase protein. J. Biol. Chem. 275, 29,737-29,742.
    • (2000) J. Biol. Chem. , vol.275
    • Gamez, A.1    Perez, B.2    Ugarte, M.3    Desviat, L.R.4
  • 57
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (P88, Ip90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind, S., Riordan, J. R., and Williams, D. B. (1994) Participation of the endoplasmic reticulum chaperone calnexin (P88, Ip90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 269, 12784-12788.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 58
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, alpha(1)- antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu, D. F., Teckman, J. H., Omura, S., and Perlmutter, D. H. (1996) Degradation of a mutant secretory protein, alpha(1)- antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271, 22791-22795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.F.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 59
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • Soti, C. and Csermely, P. (2000) Molecular chaperones and the aging process. Biogerontology 1, 225-233.
    • (2000) Biogerontology , vol.1 , pp. 225-233
    • Soti, C.1    Csermely, P.2
  • 60
    • 0036549108 scopus 로고    scopus 로고
    • Sick chaperones and ageing: A perspective
    • Macario, A. J. and Conway de, M. E. (2002) Sick chaperones and ageing: a perspective. Ageing Res. Rev. 1, 295-311.
    • (2002) Ageing Res. Rev. , vol.1 , pp. 295-311
    • Macario, A.J.1    Conway De, M.E.2
  • 61
    • 0035451646 scopus 로고    scopus 로고
    • Unfolding the role of chaperones and chaperonins in human disease
    • Slavotinek, A. M. and Biesecker, L. G. (2001) Unfolding the role of chaperones and chaperonins in human disease. Trends Genet. 17, 528-535.
    • (2001) Trends Genet. , vol.17 , pp. 528-535
    • Slavotinek, A.M.1    Biesecker, L.G.2
  • 62
    • 2642575701 scopus 로고    scopus 로고
    • Shocking degeneration
    • Benndorf, R. and Welsh, M. J. (2004) Shocking degeneration. Nat. Genet. 36, 547-548.
    • (2004) Nat. Genet. , vol.36 , pp. 547-548
    • Benndorf, R.1    Welsh, M.J.2
  • 63
    • 0032511186 scopus 로고    scopus 로고
    • Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease
    • Casari, G., De Fusco, M., Ciarmatori, S., et al. (1998) Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93, 973-983.
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1    De Fusco, M.2    Ciarmatori, S.3
  • 64
    • 0032721512 scopus 로고    scopus 로고
    • Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia
    • Hazan, J., Fonknechten, N., Mavel, D., et al. (1999) Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia. Nat. Genet. 23, 296-303.
    • (1999) Nat. Genet. , vol.23 , pp. 296-303
    • Hazan, J.1    Fonknechten, N.2    Mavel, D.3
  • 65
    • 0036241765 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60
    • Hansen, J. J., Dürr, A., Cournu-Rebeix, I., et al. (2002) Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am. J. Hum. Genet. 70, 1328-1332.
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1328-1332
    • Hansen, J.J.1    Dürr, A.2    Cournu-Rebeix, I.3
  • 66
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino, L., Silvestri, L., Koppen, M., et al. (2003) Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J. Cell Biol. 163, 777-787.
    • (2003) J. Cell Biol. , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3
  • 67
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant mutation of congenital cataract associated with a missense mutation in the alpha-crystallin gene CRYAA
    • Litt, M., Kramer, P., LaMorticella, D. M., Murphey, W., Lovrien, E. W., and Weleber, R. G. (1998) Autosomal dominant mutation of congenital cataract associated with a missense mutation in the alpha-crystallin gene CRYAA. Hum. Mol. Genet. 7, 471-474.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    Lamorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 68
    • 4243336240 scopus 로고    scopus 로고
    • Superoxide dismutase - Applications and relevance to human diseases
    • Noor, R., Mittal, S., and Iqbal, J. (2002) Superoxide dismutase - applications and relevance to human diseases. Med. Sci. Monit. 8, RA210-RA215.
    • (2002) Med. Sci. Monit. , vol.8
    • Noor, R.1    Mittal, S.2    Iqbal, J.3


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