Publications of F. U. Hartl
All genres
Journal Article (194)
181.
Journal Article
112 (1), pp. 41 - 50 (2003)
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 182.
Journal Article
99 (Suppl. 4), pp. 16412 - 16418 (2002)
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proceedings of the National Academy of Sciences of the United States of America 183.
Journal Article
158 (7), pp. 1277 - 1285 (2002)
CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. Journal of Cell Biology 184.
Journal Article
277 (36), pp. 33115 - 33126 (2002)
Structural plasticity and noncovalent substrate binding in the GroEL apical domain - A study using electrospray ionization mass spectrometry and fluorescence binding studies. Journal of Biological Chemistry 185.
Journal Article
277 (36), pp. 33220 - 33227 (2002)
Prediction of novel bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. Journal of Biological Chemistry 186.
Journal Article
9 (9), pp. 640 - 642 (2002)
Chaperones and transcriptional regulation by nuclear receptors. Nature Structural Biology 187.
Journal Article
277 (22), pp. 19265 - 19275 (2002)
Ligand discrimination by TPR domains - Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes. Journal of Biological Chemistry 188.
Journal Article
10 (Suppl. Suppl. 1), p. 270 - 270 (2002)
Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. European Journal of Human Genetics 189.
Journal Article
295 (5561), pp. 1852 - 1858 (2002)
Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 190.
Journal Article
295 (5555), pp. 669 - 671 (2002)
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 191.
Journal Article
107 (2), pp. 223 - 233 (2001)
Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding. Cell 192.
Journal Article
269 (5225), pp. 832 - 836 (1995)
Functional significance of symmetrical versus asymmetrical groel-groes chaperonin complexes. Science 193.
Journal Article
227 (3), pp. 848 - 856 (1995)
The thermosome of thermoplasma acidophilum and its relationship to the eukaryotic chaperonin tric. European Journal of Biochemistry 194.
Journal Article
11 (13), pp. 4757 - 4765 (1992)
Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO Journal. Book Chapter (4)
195.
Book Chapter
Chaperonins. In: The Encyclopedia of Biological Chemistry, Vol. 3, 2. Aufl. Ed., pp. 456 - 460 (Eds. Lennarz, W. J.; Lane, M. D.). Academic Press, London (2013)
196.
Book Chapter
Molecular Chaperone Functions in Protein Folding and Proteostasis. In: ANNUAL REVIEW OF BIOCHEMISTRY, VOL 82, pp. 323 - 355. ANNUAL REVIEWS, 4139 EL CAMINO WAY, PO BOX 10139, PALO ALTO, CA 94303-0897 USA (2013)
197.
Book Chapter
Molekulare Mechanismen des Alterns. In: Die Zukunft des Alterns, pp. 101 - 136 (Ed. Gruss, P.). C.H. Beck, München (2007)
198.
Book Chapter
Proteinfaltung in der Zelle: Die Rolle molekularer Chaperone. In: Deutsche Akademie der Naturforscher Leopoldina, Jahrbuch 2006, pp. 321 - 328 (Ed. TerMeulen, V.). Wissenschaftliche Verlagsges., Halle/Saale (2007)
Meeting Abstract (5)
199.
Meeting Abstract
11, p. 14 - 14. Wiley (2021)
Molecular chaperone functions in protein folding and proteome surveillance. In FEBS Open Bio, 200.
Meeting Abstract
18 (8, Suppl. 2), p. S46 - S46. Symposium, San Francisco. American Society for Biochemistry and Molecular Biology, Bethesda, MD (2019)
Proteome-wide analysis of protein stability in E. coli using pulse proteolysis. In Molecular and Cellular Proteomics,