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Volumn 61, Issue , 2004, Pages 241-283

Influence of Huntington's disease on the human and mouse proteome

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME;

EID: 16544369609     PISSN: 00747742     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7742(04)61010-5     Document Type: Article
Times cited : (19)

References (96)
  • 1
    • 0035957603 scopus 로고    scopus 로고
    • Cardiovascular proteomics: Evolution and potential
    • Arrell, D. K., Neverova, I., and Van Eyk, J. E. (2001). Cardiovascular proteomics: Evolution and potential. Circ. Res. 88, 763-773.
    • (2001) Circ. Res. , vol.88 , pp. 763-773
    • Arrell, D.K.1    Neverova, I.2    Van Eyk, J.E.3
  • 2
    • 0026556059 scopus 로고
    • Pheromone binding proteins of the mouse, Mus musculus
    • Bacchini, A., Gaetani, E., and Cavaggioni, A. (1992). Pheromone binding proteins of the mouse, Mus musculus. Experientia 48, 419-421.
    • (1992) Experientia , vol.48 , pp. 419-421
    • Bacchini, A.1    Gaetani, E.2    Cavaggioni, A.3
  • 3
    • 0036094817 scopus 로고    scopus 로고
    • Functional diversification during evolution of the murine alpha(1)-proteinase inhibitor family: Role of the hypervariable reactive center loop
    • Barbour, K. W., Goodwin, R. L., Guillonneau, F., Wang, Y., Baumann, H., and Berger, F. G. (2002). Functional diversification during evolution of the murine alpha(1)-proteinase inhibitor family: Role of the hypervariable reactive center loop. Mol. Biol. Evol. 19, 718-727.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 718-727
    • Barbour, K.W.1    Goodwin, R.L.2    Guillonneau, F.3    Wang, Y.4    Baumann, H.5    Berger, F.G.6
  • 4
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates, G. (2003). Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361, 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 5
    • 0035909321 scopus 로고    scopus 로고
    • Huntington's disease. Exploiting expression
    • Bates, G. P. (2001). Huntington's disease. Exploiting expression. Nature 413, 691, 693-694.
    • (2001) Nature , vol.413 , Issue.691 , pp. 693-694
    • Bates, G.P.1
  • 6
    • 0028095919 scopus 로고
    • The acute phase response
    • Baumann, H., and Gauldie, J. (1994). The acute phase response. Immunol. Today 15, 74-80.
    • (1994) Immunol. Today , vol.15 , pp. 74-80
    • Baumann, H.1    Gauldie, J.2
  • 7
    • 0037329161 scopus 로고    scopus 로고
    • Multiple roles of major urinary proteins in the house mouse, Mus domesticus
    • Beynon, R. J., and Hurst, J. L. (2003). Multiple roles of major urinary proteins in the house mouse, Mus domesticus. Biochem. Soc. Trans. 31, 142-146.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 142-146
    • Beynon, R.J.1    Hurst, J.L.2
  • 8
    • 0026325675 scopus 로고
    • Alpha B-crystallin exists as an independent protein in the heart and in the lens
    • Bhat, S. P., Horwitz, J., Srinivasan, A., and Ding, L. (1991). Alpha B-crystallin exists as an independent protein in the heart and in the lens. Eur. J. Biochem. 202, 775-781.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 775-781
    • Bhat, S.P.1    Horwitz, J.2    Srinivasan, A.3    Ding, L.4
  • 9
    • 0024578954 scopus 로고
    • alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • Bhat, S. P., and Nagineni, C. N. (1989). alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun. 158, 319-325.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 11
    • 0035040947 scopus 로고    scopus 로고
    • The vomeronasal system
    • Brennan, P. A. (2001). The vomeronasal system. Cell Mol. Life Sci. 58, 546-555.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 546-555
    • Brennan, P.A.1
  • 12
    • 0033560924 scopus 로고    scopus 로고
    • Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation
    • Carter, R. J., Lione, L. A., Humby, T., Mangiarini, L., Mahal, A., et al. (1999). Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation. J. Neurosci. 19, 3248-3257.
    • (1999) J. Neurosci. , vol.19 , pp. 3248-3257
    • Carter, R.J.1    Lione, L.A.2    Humby, T.3    Mangiarini, L.4    Mahal, A.5
  • 13
    • 0034684271 scopus 로고    scopus 로고
    • Major urinary proteins, alpha(2U)-globulins and aphrodisin
    • Cavaggioni, A., and Mucignat-Caretta, C. (2000). Major urinary proteins, alpha(2U)-globulins and aphrodisin. Biochim. Biophys. Acta 1482, 218-228.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 218-228
    • Cavaggioni, A.1    Mucignat-Caretta, C.2
  • 14
    • 0037101838 scopus 로고    scopus 로고
    • Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease
    • Chan, E. Y., Luthi-Carter, R., Strand, A., Solano, S. M., Hanson, S. A., et al. (2002). Increased huntingtin protein length reduces the number of polyglutamine-induced gene expression changes in mouse models of Huntington's disease. Hum. Mol. Genet. 11, 1939-1951.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1939-1951
    • Chan, E.Y.1    Luthi-Carter, R.2    Strand, A.3    Solano, S.M.4    Hanson, S.A.5
  • 15
    • 0020469678 scopus 로고
    • Variation in mouse major urinary protein (MUP) genes and the MUP gene products within and between inbred lines
    • Clissold, P. M., and Bishop, J. O. (1982). Variation in mouse major urinary protein (MUP) genes and the MUP gene products within and between inbred lines. Gene 18, 211-220.
    • (1982) Gene , vol.18 , pp. 211-220
    • Clissold, P.M.1    Bishop, J.O.2
  • 16
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., et al. (1997). Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    DiFiglia, M.4    Sharp, A.H.5
  • 17
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat-shock protein family
    • de Jong, W. W., Leunissen, J. A., and Voorter, C. E. (1993). Evolution of the alpha-crystallin/small heat-shock protein family. Mol. Biol. Ecol. 10, 103-126.
    • (1993) Mol. Biol. Ecol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 18
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., et al. (1997). Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5
  • 19
    • 0037934549 scopus 로고    scopus 로고
    • Subcellular proteomics
    • Dreger, M. (2003). Subcellular proteomics. Mass Spectrom. Rev. 22, 27-56.
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 27-56
    • Dreger, M.1
  • 20
    • 0024580908 scopus 로고
    • Expression of the murine alpha B-crystallin gene is not restricted to the lens
    • Dubin, R. A., Wawrousek, E. F., and Piatigorsky, J. (1989). Expression of the murine alpha B-crystallin gene is not restricted to the lens. Mol. Cell Biol. 9, 1083-1091.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 21
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • Dunah, A. W., Jeong, H., Griffin, A., Kim, Y. M., Standaert, D. G., et al. (2002). Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science 296, 2238-2243.
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3    Kim, Y.M.4    Standaert, D.G.5
  • 22
    • 0030815192 scopus 로고    scopus 로고
    • Albumin contamination of a purified human alpha 1-antitrypsin preparation does not affect either structural conformation or the electrophoretic mobility of the inhibitor
    • Finotti, P., and Pagetta, A. (1997). Albumin contamination of a purified human alpha 1-antitrypsin preparation does not affect either structural conformation or the electrophoretic mobility of the inhibitor. Clin. Chim. Acta 264, 133-148.
    • (1997) Clin. Chim. Acta , vol.264 , pp. 133-148
    • Finotti, P.1    Pagetta, A.2
  • 23
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • Flower, D. R., North, A. C., and Sansom, C. E. (2000). The lipocalin protein family: Structural and sequence overview. Biochim. Biophys. Acta 1482, 9-24.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 24
    • 0037150524 scopus 로고    scopus 로고
    • Neurodegeneration. A glutamine-rich trail leads to transcription factors
    • Freiman, R. N., and Tjian, R. (2002). Neurodegeneration. A glutamine-rich trail leads to transcription factors. Science 296, 2149-2150.
    • (2002) Science , vol.296 , pp. 2149-2150
    • Freiman, R.N.1    Tjian, R.2
  • 25
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi
    • Gervais, F. G., Singaraja, R., Xanthoudakis, S., Gutekunst, C. A., Leavitt, B. R., et al. (2002). Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi. Nat. Cell Biol. 4, 95-105.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 95-105
    • Gervais, F.G.1    Singaraja, R.2    Xanthoudakis, S.3    Gutekunst, C.A.4    Leavitt, B.R.5
  • 26
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 27
    • 0026601404 scopus 로고
    • Alpha 1-antitrypsin and alpha 1-antichymotrypsin are in the lesions of Alzheimer's disease
    • Gollin, P. A., Kalaria, R. N., Eikelenboom, P., Rozemuller, A., and Perry, G. (1992). Alpha 1-antitrypsin and alpha 1-antichymotrypsin are in the lesions of Alzheimer's disease. Neuroreport 3, 201-203.
    • (1992) Neuroreport , vol.3 , pp. 201-203
    • Gollin, P.A.1    Kalaria, R.N.2    Eikelenboom, P.3    Rozemuller, A.4    Perry, G.5
  • 28
    • 0030888517 scopus 로고    scopus 로고
    • Expression of the alpha 1-proteinase inhibitor gene family during evolution of the genus Mus
    • Goodwin, R. L., Barbour, K. W., and Berger, F. G. (1997). Expression of the alpha 1-proteinase inhibitor gene family during evolution of the genus Mus. Mol. Biol. Evol. 14, 420-427.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 420-427
    • Goodwin, R.L.1    Barbour, K.W.2    Berger, F.G.3
  • 29
    • 0029873571 scopus 로고    scopus 로고
    • Trinucleotide instability: A repeating theme in human inherited disorders
    • Gusella, J. F., and MacDonald, M. E. (1996). Trinucleotide instability: A repeating theme in human inherited disorders. Annu. Rev. Med. 47, 201-209.
    • (1996) Annu. Rev. Med. , vol.47 , pp. 201-209
    • Gusella, J.F.1    MacDonald, M.E.2
  • 30
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: Relationship to neuropathology
    • Gutekunst, C. A., Li, S. H., Yi, H., Mulroy, J. S., Kuemmerle, S., et al. (1999). Nuclear and neuropil aggregates in Huntington's disease: Relationship to neuropathology. J. Neurosci. 19, 2522-2534.
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Mulroy, J.S.4    Kuemmerle, S.5
  • 31
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 32
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes, P., and Wanker, E. E. (2003). The hunt for huntingtin function: Interaction partners tell many different stories. Trends Biochem. Sci. 28, 425-433.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 33
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • HDCRG The Huntington's Disease Collaborative Research Group
    • HDCRG (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 72, 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 34
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J., and Carrell, R. W. (2000). Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 35
    • 0035818997 scopus 로고    scopus 로고
    • Individual recognition in mice mediated by major urinary proteins
    • Hurst, J. L., Payne, C. E., Nevison, C. M., Marie, A. D., Humphries, R. E., et al. (2001). Individual recognition in mice mediated by major urinary proteins. Nature 414, 631-634.
    • (2001) Nature , vol.414 , pp. 631-634
    • Hurst, J.L.1    Payne, C.E.2    Nevison, C.M.3    Marie, A.D.4    Humphries, R.E.5
  • 36
    • 0024521440 scopus 로고
    • Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki, T., Kume-Iwaki, A., Liem, R. K., and Goldman, J. E. (1989). Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71-78.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.3    Goldman, J.E.4
  • 37
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana, N. R., Tanaka, M., Wang, G., and Nukina, N. (2000). Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9, 2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 38
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J. L., and Craig, E. A. (1997). Protein folding in vivo: Unraveling complex pathways. Cell 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 40
    • 0036547749 scopus 로고    scopus 로고
    • Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin
    • Kalsheker, N., Morley, S., and Morgan, K. (2002). Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin. Biochem. Soc. Trans. 30, 93-98.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 93-98
    • Kalsheker, N.1    Morley, S.2    Morgan, K.3
  • 41
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt, M. C., Chen, F., and Cryns, V. L. (2001). The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 276, 16059-16063.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 42
    • 0032561079 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation
    • Kato, K., Ito, H., Kamei, K., Inaguma, Y., Iwamoto, I., and Saga, S. (1998). Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J. Biol. Chem. 273, 28346-28354.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28346-28354
    • Kato, K.1    Ito, H.2    Kamei, K.3    Inaguma, Y.4    Iwamoto, I.5    Saga, S.6
  • 43
    • 0032616443 scopus 로고    scopus 로고
    • Fractionated extraction of total tissue proteins from mouse and human for 2-D electrophoresis
    • Klose, J. (1999a). Fractionated extraction of total tissue proteins from mouse and human for 2-D electrophoresis. Methods Mol. Biol. 112, 67-85.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 67-85
    • Klose, J.1
  • 44
    • 0032924892 scopus 로고    scopus 로고
    • Genotypes and phenotypes
    • Klose, J. (1999b). Genotypes and phenotypes. Electrophoresis 20, 643-652.
    • (1999) Electrophoresis , vol.20 , pp. 643-652
    • Klose, J.1
  • 45
    • 0032612938 scopus 로고    scopus 로고
    • Large-gel 2-D electrophoresis
    • Klose, J. (1999c). Large-gel 2-D electrophoresis. Methods. Mol. Biol. 112, 147-172.
    • (1999) Methods. Mol. Biol. , vol.112 , pp. 147-172
    • Klose, J.1
  • 46
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome
    • Klose, J., and Kobalz, U. (1995). Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis 16, 1034-1059.
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 47
    • 0032956263 scopus 로고    scopus 로고
    • Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin
    • Koyama, Y., and Goldman, J. E. (1999). Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin. Am. J. Pathol. 154, 1563-1572.
    • (1999) Am. J. Pathol. , vol.154 , pp. 1563-1572
    • Koyama, Y.1    Goldman, J.E.2
  • 48
    • 0020687960 scopus 로고
    • Trypsin inhibition by mouse serum: Sexual dimorphism controlled by testosterone
    • Kueppers, F., and Mills, J. (1983). Trypsin inhibition by mouse serum: Sexual dimorphism controlled by testosterone. Science 219, 182-184.
    • (1983) Science , vol.219 , pp. 182-184
    • Kueppers, F.1    Mills, J.2
  • 49
    • 0032811511 scopus 로고    scopus 로고
    • Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice
    • Li, H., Li, S. H., Cheng, A. L., Mangiarini, L., Bates, G. P., and Li, X. J. (1999a). Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice. Hum. Mol. Genet. 8, 1227-1236.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1227-1236
    • Li, H.1    Li, S.H.2    Cheng, A.L.3    Mangiarini, L.4    Bates, G.P.5    Li, X.J.6
  • 50
    • 0034426013 scopus 로고    scopus 로고
    • Amino-terminal fragments of mutant huntington show selective accumulation in striatal neurons and synaptic toxicity
    • Li, H., Li, S. H., Johnston, H., Shelbourne, P. F., and Li, X. J. (2000). Amino-terminal fragments of mutant huntington show selective accumulation in striatal neurons and synaptic toxicity. Nat. Genet. 25, 385-389.
    • (2000) Nat. Genet. , vol.25 , pp. 385-389
    • Li, H.1    Li, S.H.2    Johnston, H.3    Shelbourne, P.F.4    Li, X.J.5
  • 52
    • 0033500593 scopus 로고    scopus 로고
    • Selective discrimination learning impairments in mice expressing the human Huntington's disease mutation
    • Lione, L. A., Carter, R. J., Hunt, M. J., Bates, G. P., Morton, A. J., and Dunnett, S. B. (1999). Selective discrimination learning impairments in mice expressing the human Huntington's disease mutation. J. Neurosci. 19, 10428-10437.
    • (1999) J. Neurosci. , vol.19 , pp. 10428-10437
    • Lione, L.A.1    Carter, R.J.2    Hunt, M.J.3    Bates, G.P.4    Morton, A.J.5    Dunnett, S.B.6
  • 53
    • 0037101835 scopus 로고    scopus 로고
    • Dysregulation of gene expression in the R6/2 model of polyglutamine disease: Parallel changes in muscle and brain
    • Luthi-Carter, R., Hanson, S. A., Strand, A. D., Bergstrom, D. A., Chun, W., et al. (2002a). Dysregulation of gene expression in the R6/2 model of polyglutamine disease: Parallel changes in muscle and brain. Hum. Mol. Genet. 11, 1911-1926.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1911-1926
    • Luthi-Carter, R.1    Hanson, S.A.2    Strand, A.D.3    Bergstrom, D.A.4    Chun, W.5
  • 54
    • 0034702030 scopus 로고    scopus 로고
    • Decreased expression of striatal signaling genes in a mouse model of Huntington's disease
    • Luthi-Carter, R., Strand, A., Peters, N. L., Solano, S. M., Hollingsworth, Z. R., et al. (2000). Decreased expression of striatal signaling genes in a mouse model of Huntington's disease. Hum. Mol. Genet. 9, 1259-1271.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1259-1271
    • Luthi-Carter, R.1    Strand, A.2    Peters, N.L.3    Solano, S.M.4    Hollingsworth, Z.R.5
  • 55
    • 0037101837 scopus 로고    scopus 로고
    • Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects
    • Luthi-Carter, R., Strand, A. D., Hanson, S. A., Kooperberg, C., Schilling, G., et al. (2002b). Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum. Mol. Genet. 11, 1927-1937.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1927-1937
    • Luthi-Carter, R.1    Strand, A.D.2    Hanson, S.A.3    Kooperberg, C.4    Schilling, G.5
  • 56
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini, L., Sathasivam, K., Seller, M., Cozens, B., Harper, A., et al. (1996). Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493-506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5
  • 57
    • 0034742628 scopus 로고    scopus 로고
    • The relationship between alphaB-crystallin and neurofibrillary tangles in Alzheimer's disease
    • Mao, J. J., Katayama, S., Watanabe, C., Harada, Y., Noda, K., et al. (2001a). The relationship between alphaB-crystallin and neurofibrillary tangles in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 27, 180-188.
    • (2001) Neuropathol. Appl. Neurobiol. , vol.27 , pp. 180-188
    • Mao, J.J.1    Katayama, S.2    Watanabe, C.3    Harada, Y.4    Noda, K.5
  • 58
    • 0035900776 scopus 로고    scopus 로고
    • Human bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-induced apoptosis through down-regulation of the alpha B-crystallin gene
    • Mao, Y. W., Xiang, H., Wang, J., Korsmeyer, S., Reddan, J., and Li, D. W. (2001b). Human bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-induced apoptosis through down-regulation of the alpha B-crystallin gene. J. Biol. Chem. 276, 43435-43445.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43435-43445
    • Mao, Y.W.1    Xiang, H.2    Wang, J.3    Korsmeyer, S.4    Reddan, J.5    Li, D.W.6
  • 60
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson, M. P. (2000). Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1, 120-129.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 62
    • 0035751392 scopus 로고    scopus 로고
    • Huntington's disease. A sports star and a cook
    • McMurray, S. E., and McMurray, C. T. (2001). Huntington's disease. A sports star and a cook. Lancet 358(Suppl), S38.
    • (2001) Lancet , vol.358 , Issue.SUPPL.
    • McMurray, S.E.1    McMurray, C.T.2
  • 63
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy, M. P., Brzezinski, E. E., Hang, J., McDowell, M. T., and VanBogelen, R. A. (2003). Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 3, 1912-1919.
    • (2003) Proteomics , vol.3 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.3    McDowell, M.T.4    Vanbogelen, R.A.5
  • 64
    • 0030614502 scopus 로고    scopus 로고
    • Human alphaB-crystallin. Small heat shock protein and molecular chaperone
    • Muchowski, P. J., Bassuk, J. A., Lubsen, N. H., and Clark, J. I. (1997). Human alphaB-crystallin. Small heat shock protein and molecular chaperone. J. Biol. Chem. 272, 2578-2582.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2578-2582
    • Muchowski, P.J.1    Bassuk, J.A.2    Lubsen, N.H.3    Clark, J.I.4
  • 65
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C. W., and Tatton, W. G. (1999). Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci. 22, 123-144.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 66
  • 67
    • 0025438102 scopus 로고
    • Postnatal construction of neural circuitry in the mouse olfactory bulb
    • Pomeroy, S. L., LaMantia, A. S., and Purves, D. (1990). Postnatal construction of neural circuitry in the mouse olfactory bulb. J. Murosci. 10, 1952-1966.
    • (1990) J. Murosci. , vol.10 , pp. 1952-1966
    • Pomeroy, S.L.1    LaMantia, A.S.2    Purves, D.3
  • 68
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price, D. L., and Sisodia, S. S. (1998). Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neurosci. 21, 479-505.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 69
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • Reddy, P. H., Williams, M., Charles, V., Garrett, L., Pike-Buchanan, L., et al. (1998). Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA. Nat. Genet. 20, 198-202.
    • (1998) Nat. Genet. , vol.20 , pp. 198-202
    • Reddy, P.H.1    Williams, M.2    Charles, V.3    Garrett, L.4    Pike-Buchanan, L.5
  • 70
    • 0006607248 scopus 로고    scopus 로고
    • Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease
    • Renkawek, K., Stege, G. J., and Bosman, G. J. (1999). Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease. Neuroreport 10, 2273-2276.
    • (1999) Neuroreport , vol.10 , pp. 2273-2276
    • Renkawek, K.1    Stege, G.J.2    Bosman, G.J.3
  • 72
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., and Rabilloud, T. (2000). Membrane proteins and proteomics: Un amour impossible? Electrophoresis 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 74
    • 0031841153 scopus 로고    scopus 로고
    • Peptide mass fingerprint sequence coverage from differently stained proteins on two-dimensional electrophoresis patterns by matrix assisted laser desorption/ionization-mass spectrometry (AULDI-MS)
    • Scheler, C., Lamer, S., Pan, Z., Li, X. P., Salnikow, J., and Jungblut, P. (1998). Peptide mass fingerprint sequence coverage from differently stained proteins on two-dimensional electrophoresis patterns by matrix assisted laser desorption/ionization-mass spectrometry (AULDI-MS). Electrophoresis 19, 918-927.
    • (1998) Electrophoresis , vol.19 , pp. 918-927
    • Scheler, C.1    Lamer, S.2    Pan, Z.3    Li, X.P.4    Salnikow, J.5    Jungblut, P.6
  • 75
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling, G., Becher, M. W., Sharp, A. H., Jinnah, H. A., Duan, K., et al. (1999). Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8, 397-407.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3    Jinnah, H.A.4    Duan, K.5
  • 76
    • 0037134432 scopus 로고    scopus 로고
    • Concerted regulation of inhibitory activity of alpha 1-antitrypsin by the native strain distributed throughout the molecule
    • Seo, E. J., Lee, C., and Yu, M. H. (2002). Concerted regulation of inhibitory activity of alpha 1-antitrypsin by the native strain distributed throughout the molecule. J. Biol. Chem. 277, 14216-14220.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14216-14220
    • Seo, E.J.1    Lee, C.2    Yu, M.H.3
  • 77
    • 0029991245 scopus 로고    scopus 로고
    • Neurobiology of Huntington's disease
    • Sharp, A. H., and Ross, C. A. (1996). Neurobiology of Huntington's disease. Neurobiol. Dis. 3, 3-15.
    • (1996) Neurobiol. Dis. , vol.3 , pp. 3-15
    • Sharp, A.H.1    Ross, C.A.2
  • 78
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman, G. A., Bird, P. I., Carrell, R. W., Church, F. C., Coughlin, P. B., et al. (2001). The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276, 33293-33296.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5
  • 79
    • 0034745247 scopus 로고    scopus 로고
    • Acute-phase proteins before cerebral ischemia in stroke-prone rats: Identification by proteomics
    • Sironi, L., Tremoli, E., Miller, I., Guerrini, U., Calvio, A. M., et al. (2001). Acute-phase proteins before cerebral ischemia in stroke-prone rats: Identification by proteomics. Stroke 32, 753-760.
    • (2001) Stroke , vol.32 , pp. 753-760
    • Sironi, L.1    Tremoli, E.2    Miller, I.3    Guerrini, U.4    Calvio, A.M.5
  • 80
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
    • Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., et al. (2001). Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Mature 413, 739-743.
    • (2001) Mature , vol.413 , pp. 739-743
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3    Poelman, M.4    McCampbell, A.5
  • 81
    • 0029643751 scopus 로고
    • Government backs proteome proposal
    • Swinbanks, D. (1995). Government backs proteome proposal. Nature 378, 653.
    • (1995) Nature , vol.378 , pp. 653
    • Swinbanks, D.1
  • 82
    • 0019982840 scopus 로고
    • Mouse plasma trypsin inhibitors. Isolation and characterization of alpha-1-antitrypsin and contraspin, a novel trypsin inhibitor
    • Takahara, H., and Sinohara, H. (1982). Mouse plasma trypsin inhibitors. Isolation and characterization of alpha-1-antitrypsin and contraspin, a novel trypsin inhibitor. J. Biol. Chem. 257, 2438-2446.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2438-2446
    • Takahara, H.1    Sinohara, H.2
  • 83
    • 0027381482 scopus 로고
    • Molecular analysis of juvenile Huntington disease: The major influence on (CAG)n repeat length is the sex of the affected parent
    • Telenius, H., Kremer, H. P., Theilmann, J., Andrew, S. E., Almqvist, E., et al. (1993). Molecular analysis of juvenile Huntington disease: The major influence on (CAG)n repeat length is the sex of the affected parent. Hum. Mol. Genet. 2, 1535-1540.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1535-1540
    • Telenius, H.1    Kremer, H.P.2    Theilmann, J.3    Andrew, S.E.4    Almqvist, E.5
  • 84
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J., and Salvesen, G. S. (1983). Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52, 655-709.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 86
    • 0031867231 scopus 로고    scopus 로고
    • Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways
    • Velier, J., Kim, M., Schwarz, C., Kim, T. W., Sapp, E., et al. (1998). Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways. Exp. Neurol. 152, 34-40.
    • (1998) Exp. Neurol. , vol.152 , pp. 34-40
    • Velier, J.1    Kim, M.2    Schwarz, C.3    Kim, T.W.4    Sapp, E.5
  • 89
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease: Mechanisms and correlations
    • Wanker, E. E. (2000). Protein aggregation and pathogenesis of Huntington's disease: Mechanisms and correlations. Biol. Chem. 381, 937-942.
    • (2000) Biol. Chem. , vol.381 , pp. 937-942
    • Wanker, E.E.1
  • 90
    • 8244222683 scopus 로고
    • Sex and proteinuria of mice
    • Wicks, L. F. (1941). Sex and proteinuria of mice. Proc. Soc. Exp. Biol. Med. 48, 395-400.
    • (1941) Proc. Soc. Exp. Biol. Med. , vol.48 , pp. 395-400
    • Wicks, L.F.1
  • 91
    • 0021260498 scopus 로고
    • Regulation by sex hormones of serum levels of contrapsin and alpha 1-antiprotease in the mouse
    • Yamamoto, K., and Sinohara, H. (1984). Regulation by sex hormones of serum levels of contrapsin and alpha 1-antiprotease in the mouse. Biochim. Biophys. Acta 798, 231-234.
    • (1984) Biochim. Biophys. Acta , vol.798 , pp. 231-234
    • Yamamoto, K.1    Sinohara, H.2
  • 93
    • 0036582045 scopus 로고    scopus 로고
    • Alterations in the mouse and human proteome caused by Huntington's disease
    • Zabel, C., Chamrad, D. C., Priller, J., Woodman, B., Meyer, H. E., et al. (2002). Alterations in the mouse and human proteome caused by Huntington's disease. Mol. Cell Proteomics 1, 366-375.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 366-375
    • Zabel, C.1    Chamrad, D.C.2    Priller, J.3    Woodman, B.4    Meyer, H.E.5
  • 94
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H. Y., and Orr, H. T. (2000). Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217-247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 95
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease
    • Zuccato, C., Ciammola, A., Rigamonti, D., Leavitt, B. R., Goffredo, D., et al. (2001). Loss of huntingtin-mediated BDNF gene transcription in Huntington's disease. Science 293, 493-498.
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3    Leavitt, B.R.4    Goffredo, D.5
  • 96
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato, C., Tartari, M., Crotti, A., Goffredo, D., Valenza, M., et al. (2003). Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35, 76-83.
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zuccato, C.1    Tartari, M.2    Crotti, A.3    Goffredo, D.4    Valenza, M.5


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