Hartl FU - Search Results

1

The native 3D organization of bacterial polysomes.

Brandt F, Etchells SA, Ortiz JO, Elcock AH, Hartl FU, Baumeister W. Brandt F, et al. Among authors: hartl fu. Cell. 2009 Jan 23;136(2):261-71. doi: 10.1016/j.cell.2008.11.016. Cell. 2009. PMID: 19167328 Free article.

2

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

Langer T, Pfeifer G, Martin J, Baumeister W, Hartl FU. Langer T, et al. Among authors: hartl fu. EMBO J. 1992 Dec;11(13):4757-65. doi: 10.1002/j.1460-2075.1992.tb05581.x. EMBO J. 1992. PMID: 1361169 Free PMC article.

3

The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC.

Waldmann T, Nimmesgern E, Nitsch M, Peters J, Pfeifer G, Müller S, Kellermann J, Engel A, Hartl FU, Baumeister W. Waldmann T, et al. Among authors: hartl fu. Eur J Biochem. 1995 Feb 1;227(3):848-56. doi: 10.1111/j.1432-1033.1995.tb20210.x. Eur J Biochem. 1995. PMID: 7867646 Free article.

4

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.

5

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.

Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Scheufler C, et al. Among authors: hartl fu. Cell. 2000 Apr 14;101(2):199-210. doi: 10.1016/S0092-8674(00)80830-2. Cell. 2000. PMID: 10786835 Free article.

6

Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.

Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I. Siegert R, et al. Among authors: hartl fu. Cell. 2000 Nov 10;103(4):621-32. doi: 10.1016/s0092-8674(00)00165-3. Cell. 2000. PMID: 11106732 Free article.

7

Hsp90: a specialized but essential protein-folding tool.

Young JC, Moarefi I, Hartl FU. Young JC, et al. Among authors: hartl fu. J Cell Biol. 2001 Jul 23;154(2):267-73. doi: 10.1083/jcb.200104079. J Cell Biol. 2001. PMID: 11470816 Free PMC article. Review.

8

Dual function of protein confinement in chaperonin-assisted protein folding.

Brinker A, Pfeifer G, Kerner MJ, Naylor DJ, Hartl FU, Hayer-Hartl M. Brinker A, et al. Among authors: hartl fu. Cell. 2001 Oct 19;107(2):223-33. doi: 10.1016/s0092-8674(01)00517-7. Cell. 2001. PMID: 11672529 Free article.

9

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.

Young JC, Hoogenraad NJ, Hartl FU. Young JC, et al. Among authors: hartl fu. Cell. 2003 Jan 10;112(1):41-50. doi: 10.1016/s0092-8674(02)01250-3. Cell. 2003. PMID: 12526792 Free article.

10

A stress sensor for the bacterial periplasm.

Young JC, Hartl FU. Young JC, et al. Among authors: hartl fu. Cell. 2003 Apr 4;113(1):1-2. doi: 10.1016/s0092-8674(03)00192-2. Cell. 2003. PMID: 12679025 Free article. Review.

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My NCBI Filters

Text availability

Article attribute

Article type

Publication date

301 results

Search Page