Hartl FU - 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. Among authors: hartl fu. 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. Among authors: hartl fu. 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. Among authors: hartl fu. 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. Among authors: hartl fu. 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. Among authors: hartl fu. 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. Among authors: hartl fu. Nat Struct Biol. 1998 Nov;5(11):977-85. doi: 10.1038/2952. Nat Struct Biol. 1998. PMID: 9808043

8

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains.

Teter SA, Houry WA, Ang D, Tradler T, Rockabrand D, Fischer G, Blum P, Georgopoulos C, Hartl FU. Teter SA, et al. Among authors: hartl fu. Cell. 1999 Jun 11;97(6):755-65. doi: 10.1016/s0092-8674(00)80787-4. Cell. 1999. PMID: 10380927 Free article.

9

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. Among authors: hartl fu. Biol Chem. 1999 May;380(5):531-40. doi: 10.1515/BC.1999.068. Biol Chem. 1999. PMID: 10384959

10

MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin.

Leroux MR, Fändrich M, Klunker D, Siegers K, Lupas AN, Brown JR, Schiebel E, Dobson CM, Hartl FU. Leroux MR, et al. Among authors: hartl fu. EMBO J. 1999 Dec 1;18(23):6730-43. doi: 10.1093/emboj/18.23.6730. EMBO J. 1999. PMID: 10581246 Free PMC article.

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