Hartl FU - Search Results

1

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

2

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. Langer T, et al. Among authors: hartl fu. Nature. 1992 Apr 23;356(6371):683-9. doi: 10.1038/356683a0. Nature. 1992. PMID: 1349157 Free article.

3

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate.

Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Martin J, et al. Among authors: hartl fu. Nature. 1991 Jul 4;352(6330):36-42. doi: 10.1038/352036a0. Nature. 1991. PMID: 1676490

4

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.

Ostermann J, Horwich AL, Neupert W, Hartl FU. Ostermann J, et al. Among authors: hartl fu. Nature. 1989 Sep 14;341(6238):125-30. doi: 10.1038/341125a0. Nature. 1989. PMID: 2528694 Free article.

5

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

Engel A, Hayer-Hartl MK, Goldie KN, Pfeifer G, Hegerl R, Müller S, da Silva AC, Baumeister W, Hartl FU. Engel A, et al. Among authors: hartl fu. Science. 1995 Aug 11;269(5225):832-6. doi: 10.1126/science.7638600. Science. 1995. PMID: 7638600

6

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

7

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding.

Hlodan R, Tempst P, Hartl FU. Hlodan R, et al. Among authors: hartl fu. Nat Struct Biol. 1995 Jul;2(7):587-95. doi: 10.1038/nsb0795-587. Nat Struct Biol. 1995. PMID: 7664127

8

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

9

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

10

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.

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