메뉴 건너뛰기




Volumn 51, Issue 1-2, 1997, Pages 8-14

Huntington's disease gene product, huntingtin, associates with microtubules in vitro

Author keywords

CAG repeat; Calmodulin; Glyceraldehyde 3 phosphate dehydrogenase; Huntingtin; Huntington's disease; Microtubule; Polyglutamine; Tubulin

Indexed keywords

GENE PRODUCT; PROTEIN; TUBULIN;

EID: 0030819255     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(97)00205-2     Document Type: Article
Times cited : (51)

References (38)
  • 1
    • 0024450903 scopus 로고
    • The functional anatomy of basal ganglia disorders
    • Albin R.L., Young A.B., Penney J.B. The functional anatomy of basal ganglia disorders. Trends Neurosci. 12:1989;366-375.
    • (1989) Trends Neurosci. , vol.12 , pp. 366-375
    • Albin, R.L.1    Young, A.B.2    Penney, J.B.3
  • 2
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell. 72:1993;971-983.
    • (1993) Cell , vol.72 , pp. 971-983
    • Huntington'S Disease Collaborative Research Group1
  • 4
    • 0029991245 scopus 로고    scopus 로고
    • Neurobiology of Huntington's disease
    • Sharp A.H., Ross C.A. Neurobiology of Huntington's disease. Neurobiol. Dis. 3:1996;3-15.
    • (1996) Neurobiol. Dis. , vol.3 , pp. 3-15
    • Sharp, A.H.1    Ross, C.A.2
  • 5
  • 9
    • 0028904293 scopus 로고
    • Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein
    • Jou Y.-S., Myers R.M. Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein. Hum. Mol. Genet. 4:1995;465-469.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 465-469
    • Jou, Y.-S.1    Myers, R.M.2
  • 15
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • Zeitlin S., Liu J.-P., Chapman D.L., Papaioannou V.E., Efstratiadis A. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. Nature Genet. 11:1995;155-163.
    • (1995) Nature Genet. , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.-P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 16
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz M.F., Johnson T., Suzuki M., Finch J.T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA. 91:1994;5355-5358.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 17
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases
    • Stott K., Blackburn J.M., Butler P.J.G., Perutz M. Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases. Proc. Natl. Acad. Sci. USA. 92:1995;6509-6513.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 19
    • 0018725413 scopus 로고
    • The presence of an adenosine-5′-triphosphatase dependent on 6S tubulin and calcium ions in rat brain microtubules
    • Ihara Y., Fujii T., Arai T., Tanaka R., Kaziro Y. The presence of an adenosine-5′-triphosphatase dependent on 6S tubulin and calcium ions in rat brain microtubules. J. Biochem. (Tokyo). 86:1979;587-590.
    • (1979) J. Biochem. (Tokyo) , vol.86 , pp. 587-590
    • Ihara, Y.1    Fujii, T.2    Arai, T.3    Tanaka, R.4    Kaziro, Y.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0023953283 scopus 로고
    • Direct protein microsequencing from Immobilon-P transfer membrane
    • LeGendre N., Matsudaira P. Direct protein microsequencing from Immobilon-P transfer membrane. BioTechniques. 6:1988;154-159.
    • (1988) BioTechniques , vol.6 , pp. 154-159
    • Legendre, N.1    Matsudaira, P.2
  • 23
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods. 10:1984;203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 24
    • 0025963550 scopus 로고
    • Production and specificity of monoclonal antibodies against calmodulin from Dictyostelium discoideum
    • Hulen D., Baron A., Salisbury J., Clarke M. Production and specificity of monoclonal antibodies against calmodulin from Dictyostelium discoideum. Cell Motil. Cytoskeleton. 18:1991;113-122.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 113-122
    • Hulen, D.1    Baron, A.2    Salisbury, J.3    Clarke, M.4
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 27
    • 0020318730 scopus 로고
    • The interaction between calmodulin and microtubule proteins : IV. Quantitative analysis of the binding between calmodulin and tubulin dimer
    • Kumagai H., Nishida E., Sakai H. The interaction between calmodulin and microtubule proteins. IV. Quantitative analysis of the binding between calmodulin and tubulin dimer J. Biochem. (Tokyo). 91:1982;1329-1336.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1329-1336
    • Kumagai, H.1    Nishida, E.2    Sakai, H.3
  • 28
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B., Matilla T., Burright E.N., Merry D.E., Fischbeck K.H., Orr H.T., Zoghbi H.Y. Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Human Mol. Genet. 5:1996;1311-1318.
    • (1996) Human Mol. Genet. , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3    Merry, D.E.4    Fischbeck, K.H.5    Orr, H.T.6    Zoghbi, H.Y.7
  • 29
    • 0020758755 scopus 로고
    • A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
    • Kumagai H., Sakai H. A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase. J. Biochem. (Tokyo). 93:1983;1259-1269.
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 1259-1269
    • Kumagai, H.1    Sakai, H.2
  • 31
    • 0029899868 scopus 로고    scopus 로고
    • Huntingtin-associated protein (HAP1): Discrete neuronal localizations in the brain resemble those of neuronal nitric oxide synthase
    • Li X.J., Sharp A.H., Li S.H., Dawson T.M., Snyder S.H., Ross C.A. Huntingtin-associated protein (HAP1): discrete neuronal localizations in the brain resemble those of neuronal nitric oxide synthase. Proc. Natl. Acad. Sci. USA. 93:1996;4839-4844.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4839-4844
    • Li, X.J.1    Sharp, A.H.2    Li, S.H.3    Dawson, T.M.4    Snyder, S.H.5    Ross, C.A.6
  • 35
    • 0029441693 scopus 로고
    • Control of electron transfer in neuronal nitric oxide synthase by calmodulin, substrate, substrate analogs, and nitric oxide
    • Stuehr D.J., Abu-Soud H.M., Rousseau D.L., Feldman P.L., Wang J. Control of electron transfer in neuronal nitric oxide synthase by calmodulin, substrate, substrate analogs, and nitric oxide. Adv. Pharmacol. 34:1995;207-213.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 207-213
    • Stuehr, D.J.1    Abu-Soud, H.M.2    Rousseau, D.L.3    Feldman, P.L.4    Wang, J.5
  • 36
    • 0022624049 scopus 로고
    • On the mechanism of calmodulin-induced inhibition of microtubule assembly in vitro
    • Kumagai H., Nishida E., Kotani S., Sakai H. On the mechanism of calmodulin-induced inhibition of microtubule assembly in vitro. J. Biochem. (Tokyo). 99:1986;521-525.
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 521-525
    • Kumagai, H.1    Nishida, E.2    Kotani, S.3    Sakai, H.4
  • 37
    • 0022235642 scopus 로고
    • Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins
    • Kotani S., Nishida E., Kumagai H., Sakai H. Calmodulin inhibits interaction of actin with MAP2 and tau, two major microtubule-associated proteins. J. Biol. Chem. 260:1985;10779-10783.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10779-10783
    • Kotani, S.1    Nishida, E.2    Kumagai, H.3    Sakai, H.4
  • 38
    • 0021357249 scopus 로고
    • Calmodulin binds to both microtubule-associated protein 2 and tau proteins
    • Lee Y.C., Wolff J. Calmodulin binds to both microtubule-associated protein 2 and tau proteins. J. Biol. Chem. 259:1984;1226-1230.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1226-1230
    • Lee, Y.C.1    Wolff, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.