Hartl FU - Search Results

1

Real-time observation of trigger factor function on translating ribosomes.

Kaiser CM, Chang HC, Agashe VR, Lakshmipathy SK, Etchells SA, Hayer-Hartl M, Hartl FU, Barral JM. Kaiser CM, et al. Among authors: hartl fu. Nature. 2006 Nov 23;444(7118):455-60. doi: 10.1038/nature05225. Epub 2006 Oct 15. Nature. 2006. PMID: 17051157

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

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

Martin J, Mayhew M, Langer T, Hartl FU. Martin J, et al. Among authors: hartl fu. Nature. 1993 Nov 18;366(6452):228-33. doi: 10.1038/366228a0. Nature. 1993. PMID: 7901770

4

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

Martin J, Geromanos S, Tempst P, Hartl FU. Martin J, et al. Among authors: hartl fu. Nature. 1993 Nov 18;366(6452):279-82. doi: 10.1038/366279a0. Nature. 1993. PMID: 7901771

5

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.

6

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.

7

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.

8

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

9

Recombination of protein domains facilitated by co-translational folding in eukaryotes.

Netzer WJ, Hartl FU. Netzer WJ, et al. Among authors: hartl fu. Nature. 1997 Jul 24;388(6640):343-9. doi: 10.1038/41024. Nature. 1997. PMID: 9237751

10

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

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