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Items: 1 to 20 of 67

1.

Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein.

Davidson JD, Riley B, Burright EN, Duvick LA, Zoghbi HY, Orr HT.

Hum Mol Genet. 2000 Sep 22;9(15):2305-12.

PMID:
11001934
2.

The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up.

Riley BE, Xu Y, Zoghbi HY, Orr HT.

J Biol Chem. 2004 Oct 1;279(40):42290-301. Epub 2004 Jul 26.

3.

Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4).

Woznik M, Rödner C, Lemon K, Rima B, Mankertz A, Finsterbusch T.

J Gen Virol. 2010 Nov;91(Pt 11):2773-81. doi: 10.1099/vir.0.024638-0. Epub 2010 Aug 11.

PMID:
20702650
4.

SUMO-1 interacts with mutant ataxin-1 and colocalizes to its aggregates in Purkinje cells of SCA1 transgenic mice.

Kang S, Hong S.

Arch Ital Biol. 2010 Dec;148(4):351-63. doi: 10.4449/aib.v148i4.1201.

PMID:
21308649
5.

Ataxin-7 interacts with a Cbl-associated protein that it recruits into neuronal intranuclear inclusions.

Lebre AS, Jamot L, Takahashi J, Spassky N, Leprince C, Ravisé N, Zander C, Fujigasaki H, Kussel-Andermann P, Duyckaerts C, Camonis JH, Brice A.

Hum Mol Genet. 2001 May 15;10(11):1201-13.

PMID:
11371513
6.

A novel protein with RNA-binding motifs interacts with ataxin-2.

Shibata H, Huynh DP, Pulst SM.

Hum Mol Genet. 2000 May 22;9(9):1303-13. Erratum in: Hum Mol Genet 2000 Jul 22;9(12):1903.

PMID:
10814712
7.

Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice.

Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, Clark HB, Zoghbi HY, Orr HT.

Cell. 1998 Oct 2;95(1):41-53.

8.

Relationship between ataxin-1 nuclear inclusions and Purkinje cell specific proteins in SCA-1 transgenic mice.

Vig PJ, Subramony SH, Qin Z, McDaniel DO, Fratkin JD.

J Neurol Sci. 2000 Mar 15;174(2):100-10.

PMID:
10727695
9.

Progress in pathogenesis studies of spinocerebellar ataxia type 1.

Cummings CJ, Orr HT, Zoghbi HY.

Philos Trans R Soc Lond B Biol Sci. 1999 Jun 29;354(1386):1079-81. Review.

10.

Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex.

Matilla A, Gorbea C, Einum DD, Townsend J, Michalik A, van Broeckhoven C, Jensen CC, Murphy KJ, Ptácek LJ, Fu YH.

Hum Mol Genet. 2001 Nov 15;10(24):2821-31.

PMID:
11734547
11.

Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.

Mizutani A, Wang L, Rajan H, Vig PJ, Alaynick WA, Thaler JP, Tsai CC.

EMBO J. 2005 Sep 21;24(18):3339-51. Epub 2005 Aug 25.

12.

A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.

Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, Kubo A, Kornbluth S, Rose MD.

FEBS Lett. 2000 Feb 11;467(2-3):348-55.

13.

The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1.

Matilla A, Koshy BT, Cummings CJ, Isobe T, Orr HT, Zoghbi HY.

Nature. 1997 Oct 30;389(6654):974-8. Erratum in: Nature 1998 Feb 19;391(6669):818.

PMID:
9353121
14.

Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1.

Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY.

Nat Genet. 1998 Jun;19(2):148-54.

PMID:
9620770
15.

Identification of a self-association region within the SCA1 gene product, ataxin-1.

Burright EN, Davidson JD, Duvick LA, Koshy B, Zoghbi HY, Orr HT.

Hum Mol Genet. 1997 Apr;6(4):513-8.

PMID:
9097953
16.

Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice.

Emamian ES, Kaytor MD, Duvick LA, Zu T, Tousey SK, Zoghbi HY, Clark HB, Orr HT.

Neuron. 2003 May 8;38(3):375-87.

17.

RNA association and nucleocytoplasmic shuttling by ataxin-1.

Irwin S, Vandelft M, Pinchev D, Howell JL, Graczyk J, Orr HT, Truant R.

J Cell Sci. 2005 Jan 1;118(Pt 1):233-42.

18.

USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product.

Hong S, Kim SJ, Ka S, Choi I, Kang S.

Mol Cell Neurosci. 2002 Jun;20(2):298-306.

PMID:
12093161
19.
20.

Delphilin: a novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor delta 2 subunit.

Miyagi Y, Yamashita T, Fukaya M, Sonoda T, Okuno T, Yamada K, Watanabe M, Nagashima Y, Aoki I, Okuda K, Mishina M, Kawamoto S.

J Neurosci. 2002 Feb 1;22(3):803-14.

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