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Volumn 22, Issue 3, 2005, Pages 242-247

Research on screening and identification of proteins interacting with ataxin-3

Author keywords

Ataxin 3; Intranuclear aggregation; Machado Joseph disease; Small ubiquitin like modifier 1; Spinocerebellar ataxia type 3; Yeast two hybrid

Indexed keywords

ATAXIN 3; CELL PROTEIN; COMPLEMENTARY DNA; NEURONAL AMILORIDE SENSITIVE CATION CHANNEL; RHODOPSIN GUANOSINE DIPHOSPHATE DISSOCIATION INHIBITOR ALPHA; SUMO 1 PROTEIN; UNCLASSIFIED DRUG;

EID: 20644455541     PISSN: 10039406     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (17)
  • 1
    • 0034093161 scopus 로고    scopus 로고
    • Frequency of SCA1, SCA2, SCA3/MJD, SCA6, SCA7, and DRPLA CAG trinucleotide repeat expansion in patients with hereditary spinocerebellar ataxia from Chinese kindreds
    • Tang B, Liu C, Shen L, et al. Frequency of SCA1, SCA2, SCA3/MJD, SCA6, SCA7, and DRPLA CAG trinucleotide repeat expansion in patients with hereditary spinocerebellar ataxia from Chinese kindreds. Arch Neurol, 2000, 57:540-544.
    • (2000) Arch Neurol , vol.57 , pp. 540-544
    • Tang, B.1    Liu, C.2    Shen, L.3
  • 2
    • 0345436080 scopus 로고    scopus 로고
    • High level expression of expanded full-length ataxin-3 in vitro causes cell death and formation of intranuclear inclusions in neuronal cells
    • Evert BO, Wullner U, Schulz JB, et al. High level expression of expanded full-length ataxin-3 in vitro causes cell death and formation of intranuclear inclusions in neuronal cells. Hum Mol Genet, 1999, 8:1169-1176.
    • (1999) Hum Mol Genet , vol.8 , pp. 1169-1176
    • Evert, B.O.1    Wullner, U.2    Schulz, J.B.3
  • 3
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • Wang G, Sawai N, Kotliarova S, et al. Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum Mol Genet, 2000, 9:1795-1803.
    • (2000) Hum Mol Genet , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3
  • 4
    • 0027139884 scopus 로고
    • Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton
    • Leffers H, Nielsen MS, Andersen AH, et al. Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton. Exp Cell Res, 1993, 209:165-174.
    • (1993) Exp Cell Res , vol.209 , pp. 165-174
    • Leffers, H.1    Nielsen, M.S.2    Andersen, A.H.3
  • 5
    • 0031029967 scopus 로고    scopus 로고
    • BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels
    • Garcia-Anoveros J, Derfler B, Neville-Golden J, et al. BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels. Proc Natl Acad Sci U S A, 1997, 94:1459-1464.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1459-1464
    • Garcia-Anoveros, J.1    Derfler, B.2    Neville-Golden, J.3
  • 6
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh ET, Gong L, Kamitani T. Ubiquitin-like proteins: new wines in new bottles. Gene, 2000, 248:1-14.
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 7
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquituin conjugation
    • Stelter P, Ulrich HD. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquituin conjugation. Nature, 2003, 425:188-191.
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 8
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F, Macfarlan T, Pittman RN, et al. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J Biol Chem, 2002, 277:45004-45012.
    • (2002) J Biol Chem , vol.277 , pp. 45004-45012
    • Li, F.1    Macfarlan, T.2    Pittman, R.N.3
  • 9
    • 0035937523 scopus 로고    scopus 로고
    • Interference by Huntington and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
    • Nucifora FC Jr, Sasaki M, Peters MF, et al. Interference by Huntington and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science, 2001, 291:2423-2428.
    • (2001) Science , vol.291 , pp. 2423-2428
    • Nucifora Jr., F.C.1    Sasaki, M.2    Peters, M.F.3
  • 10
    • 0033818112 scopus 로고    scopus 로고
    • Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription
    • Shimohata T, Nakajima Y, Yamada M, et al. Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription. Nat Genet, 2000, 26:29-36.
    • (2000) Nat Genet , vol.26 , pp. 29-36
    • Shimohata, T.1    Nakajima, Y.2    Yamada, M.3
  • 11
    • 0030666001 scopus 로고    scopus 로고
    • Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures
    • Skinner PJ, Koshy BT, Cummings CJ, et al. Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures. Nature, 1997, 389:971-974.
    • (1997) Nature , vol.389 , pp. 971-974
    • Skinner, P.J.1    Koshy, B.T.2    Cummings, C.J.3
  • 12
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr ST, Senut MC, Whitelegge JP, et al. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol, 2001, 153:283-294.
    • (2001) J Cell Biol , vol.153 , pp. 283-294
    • Suhr, S.T.1    Senut, M.C.2    Whitelegge, J.P.3
  • 13
    • 0036296111 scopus 로고    scopus 로고
    • Enhanced SUMOylation in polyglutamine diseases
    • Ueda H, Goto J, Hashida H, et al. Enhanced SUMOylation in polyglutamine diseases. Biochem Biophys Res Commun, 2002, 293:307-313.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 307-313
    • Ueda, H.1    Goto, J.2    Hashida, H.3
  • 14
    • 0037015833 scopus 로고    scopus 로고
    • SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death
    • Terashima T, Kawai H, Fujitani M, et al. SUMO-1 co-localized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death. Neuro Report, 2002, 13:2359-2364.
    • (2002) Neuro Report , vol.13 , pp. 2359-2364
    • Terashima, T.1    Kawai, H.2    Fujitani, M.3
  • 15
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H, Karvonen U, Janne OA, et al. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci U S A, 2000, 97:14145-14150.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3
  • 16
    • 0036850456 scopus 로고    scopus 로고
    • Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
    • Chan HY, Warrick JM, Andriola I, et al. Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum Mol Genet, 2002, 11:2895-2904.
    • (2002) Hum Mol Genet , vol.11 , pp. 2895-2904
    • Chan, H.Y.1    Warrick, J.M.2    Andriola, I.3
  • 17
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan JS, Agrawal N, Pallos J, et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science, 2004, 304:100-104.
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.