Hayer-Hartl M - Search Results

1

Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation.

Schaffar G, Breuer P, Boteva R, Behrends C, Tzvetkov N, Strippel N, Sakahira H, Siegers K, Hayer-Hartl M, Hartl FU. Schaffar G, et al. Mol Cell. 2004 Jul 2;15(1):95-105. doi: 10.1016/j.molcel.2004.06.029. Mol Cell. 2004. PMID: 15225551 Free article.

2

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

Hayer-Hartl MK, Martin J, Hartl FU. Hayer-Hartl MK, et al. Science. 1995 Aug 11;269(5225):836-41. doi: 10.1126/science.7638601. Science. 1995. PMID: 7638601

3

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.

Hayer-Hartl MK, Ewbank JJ, Creighton TE, Hartl FU. Hayer-Hartl MK, et al. EMBO J. 1994 Jul 1;13(13):3192-202. doi: 10.1002/j.1460-2075.1994.tb06618.x. EMBO J. 1994. PMID: 7913682 Free PMC article.

4

A comment on: 'The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan', by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12.

Hayer-Hartl MK, Hartl FU. Hayer-Hartl MK, et al. FEBS Lett. 1993 Mar 29;320(1):83-4; discussion 85. doi: 10.1016/0014-5793(93)81663-k. FEBS Lett. 1993. PMID: 8096465 Free article. No abstract available.

5

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

Hayer-Hartl MK, Weber F, Hartl FU. Hayer-Hartl MK, et al. EMBO J. 1996 Nov 15;15(22):6111-21. EMBO J. 1996. PMID: 8947033 Free PMC article.

6

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.

Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Harrison CJ, et al. Science. 1997 Apr 18;276(5311):431-5. doi: 10.1126/science.276.5311.431. Science. 1997. PMID: 9103205

7

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.

Weber F, Keppel F, Georgopoulos C, Hayer-Hartl MK, Hartl FU. Weber F, et al. Nat Struct Biol. 1998 Nov;5(11):977-85. doi: 10.1038/2952. Nat Struct Biol. 1998. PMID: 9808043

8

On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.

Hayer-Hartl MK, Ewalt KL, Hartl FU. Hayer-Hartl MK, et al. Biol Chem. 1999 May;380(5):531-40. doi: 10.1515/BC.1999.068. Biol Chem. 1999. PMID: 10384959

9

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. Muchowski PJ, et al. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7841-6. doi: 10.1073/pnas.140202897. Proc Natl Acad Sci U S A. 2000. PMID: 10859365 Free PMC article.

10

Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.

Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE. Sittler A, et al. Hum Mol Genet. 2001 Jun 1;10(12):1307-15. doi: 10.1093/hmg/10.12.1307. Hum Mol Genet. 2001. PMID: 11406612

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