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Items: 1 to 20 of 158

1.

Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers.

Behrends C, Langer CA, Boteva R, Böttcher UM, Stemp MJ, Schaffar G, Rao BV, Giese A, Kretzschmar H, Siegers K, Hartl FU.

Mol Cell. 2006 Sep 15;23(6):887-97.

2.

Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model.

Schiffer NW, Broadley SA, Hirschberger T, Tavan P, Kretzschmar HA, Giese A, Haass C, Hartl FU, Schmid B.

J Biol Chem. 2007 Mar 23;282(12):9195-203. Epub 2006 Dec 14.

3.

Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils.

Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hartl FU.

Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7841-6.

4.

Monitoring polyglutamine toxicity in yeast.

Duennwald ML.

Methods. 2011 Mar;53(3):232-7. doi: 10.1016/j.ymeth.2010.12.001. Epub 2010 Dec 6.

PMID:
21144902
5.
6.
7.

Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer.

Wacker JL, Zareie MH, Fong H, Sarikaya M, Muchowski PJ.

Nat Struct Mol Biol. 2004 Dec;11(12):1215-22. Epub 2004 Nov 14.

PMID:
15543156
8.

The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.

Tam S, Geller R, Spiess C, Frydman J.

Nat Cell Biol. 2006 Oct;8(10):1155-62. Epub 2006 Sep 17.

9.

The role of molecular chaperones in human misfolding diseases.

Broadley SA, Hartl FU.

FEBS Lett. 2009 Aug 20;583(16):2647-53. doi: 10.1016/j.febslet.2009.04.029. Epub 2009 Apr 23. Review.

10.

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.

Melville MW, McClellan AJ, Meyer AS, Darveau A, Frydman J.

Mol Cell Biol. 2003 May;23(9):3141-51.

11.
12.

Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.

Kitamura A, Kubota H, Pack CG, Matsumoto G, Hirayama S, Takahashi Y, Kimura H, Kinjo M, Morimoto RI, Nagata K.

Nat Cell Biol. 2006 Oct;8(10):1163-70. Epub 2006 Sep 17.

PMID:
16980958
13.

The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities.

Hageman J, van Waarde MA, Zylicz A, Walerych D, Kampinga HH.

Biochem J. 2011 Apr 1;435(1):127-42. doi: 10.1042/BJ20101247.

PMID:
21231916
14.

N-terminal polyglutamine-containing fragments inhibit androgen receptor transactivation function.

Schiffer NW, Céraline J, Hartl FU, Broadley SA.

Biol Chem. 2008 Dec;389(12):1455-66. doi: 10.1515/BC.2008.169.

PMID:
18844449
15.
16.

Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast.

Li WZ, Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F, et al.

J Biol Chem. 1994 Jul 15;269(28):18616-22.

17.

Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70.

Yamagishi N, Goto K, Nakagawa S, Saito Y, Hatayama T.

Exp Cell Res. 2010 Sep 10;316(15):2424-33. doi: 10.1016/j.yexcr.2010.06.003. Epub 2010 Jun 11.

PMID:
20542028
18.

Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro.

Evans CG, Wisén S, Gestwicki JE.

J Biol Chem. 2006 Nov 3;281(44):33182-91. Epub 2006 Sep 14.

19.

Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy.

Bao YP, Cook LJ, O'Donovan D, Uyama E, Rubinsztein DC.

J Biol Chem. 2002 Apr 5;277(14):12263-9. Epub 2002 Jan 16.

20.

p97 Homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat.

Nishikori S, Yamanaka K, Sakurai T, Esaki M, Ogura T.

Genes Cells. 2008 Aug;13(8):827-38. doi: 10.1111/j.1365-2443.2008.01214.x. Epub 2008 Jul 31.

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