Publikationen von F. U. Hartl
Alle Typen
Zeitschriftenartikel (194)
181.
Zeitschriftenartikel
112 (1), S. 41 - 50 (2003)
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 182.
Zeitschriftenartikel
99 (Suppl. 4), S. 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.
Zeitschriftenartikel
158 (7), S. 1277 - 1285 (2002)
CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. Journal of Cell Biology 184.
Zeitschriftenartikel
277 (36), S. 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.
Zeitschriftenartikel
277 (36), S. 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.
Zeitschriftenartikel
9 (9), S. 640 - 642 (2002)
Chaperones and transcriptional regulation by nuclear receptors. Nature Structural Biology 187.
Zeitschriftenartikel
277 (22), S. 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.
Zeitschriftenartikel
10 (Suppl. Suppl. 1), S. 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.
Zeitschriftenartikel
295 (5561), S. 1852 - 1858 (2002)
Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 190.
Zeitschriftenartikel
295 (5555), S. 669 - 671 (2002)
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 191.
Zeitschriftenartikel
107 (2), S. 223 - 233 (2001)
Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding. Cell 192.
Zeitschriftenartikel
269 (5225), S. 832 - 836 (1995)
Functional significance of symmetrical versus asymmetrical groel-groes chaperonin complexes. Science 193.
Zeitschriftenartikel
227 (3), S. 848 - 856 (1995)
The thermosome of thermoplasma acidophilum and its relationship to the eukaryotic chaperonin tric. European Journal of Biochemistry 194.
Zeitschriftenartikel
11 (13), S. 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. Buchkapitel (4)
195.
Buchkapitel
Chaperonins. In: The Encyclopedia of Biological Chemistry, Vol. 3, 2. Aufl. Aufl., S. 456 - 460 (Hg. Lennarz, W. J.; Lane, M. D.). Academic Press, London (2013)
196.
Buchkapitel
Molecular Chaperone Functions in Protein Folding and Proteostasis. In: ANNUAL REVIEW OF BIOCHEMISTRY, VOL 82, S. 323 - 355. ANNUAL REVIEWS, 4139 EL CAMINO WAY, PO BOX 10139, PALO ALTO, CA 94303-0897 USA (2013)
197.
Buchkapitel
Molekulare Mechanismen des Alterns. In: Die Zukunft des Alterns, S. 101 - 136 (Hg. Gruss, P.). C.H. Beck, München (2007)
198.
Buchkapitel
Proteinfaltung in der Zelle: Die Rolle molekularer Chaperone. In: Deutsche Akademie der Naturforscher Leopoldina, Jahrbuch 2006, S. 321 - 328 (Hg. TerMeulen, V.). Wissenschaftliche Verlagsges., Halle/Saale (2007)
Meeting Abstract (5)
199.
Meeting Abstract
11, S. 14 - 14. Wiley (2021)
Molecular chaperone functions in protein folding and proteome surveillance. In FEBS Open Bio, 200.
Meeting Abstract
18 (8, Suppl. 2), S. 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,