Publications of M. Hayer-Hartl
All genres
Journal Article (76)
61.
Journal Article
45 (44), pp. 13356 - 13360 (2006)
A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding. Biochemistry 62.
Journal Article
45 (44), pp. 13356 - 13360 (2006)
A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding. Biochemistry 63.
Journal Article
125 (5), pp. 903 - 914 (2006)
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 64.
Journal Article
122 (2), pp. 209 - 220 (2005)
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 65.
Journal Article
328 (2), pp. 477 - 483 (2005)
How to orient the functional GroEL-SRI mutant for atomic force microscopy investigations. Biochemical and Biophysical Research Communications 66.
Journal Article
13 (8), pp. 2139 - 2148 (2004)
A mobile loop order-disorder transition modulates the speed of chaperonin cycling. Protein Science 67.
Journal Article
15 (1), pp. 95 - 105 (2004)
Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation. Molecular Cell 68.
Journal Article
117 (2), pp. 199 - 209 (2004)
Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed. Cell 69.
Journal Article
279 (2), pp. 1090 - 1099 (2004)
Functional characterization of an archaeal GroEL/GroES chaperonin system - Significance of substrate encapsulation. Journal of Biological Chemistry 70.
Journal Article
278 (35), pp. 33256 - 33267 (2003)
Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei. Journal of Biological Chemistry 71.
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 72.
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 73.
Journal Article
21 (14), pp. 3659 - 3671 (2002)
The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation. EMBO Journal 74.
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 75.
Journal Article
295 (5561), pp. 1852 - 1858 (2002)
Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 76.
Journal Article
107 (2), pp. 223 - 233 (2001)
Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding. Cell Book Chapter (2)
77.
Book Chapter
2563, 2563 Ed., pp. 269 - 296 (Eds. Zhou, H.-X.; Spille, J.-H.; Banerjee, P. R.). Springer US, New York, NY (2023)
Phase Separation of Rubisco by the Folded SSUL Domains of CcmM in Beta-Carboxysome Biogenesis. In: Phase-Separated Biomolecular Condensates: Methods in Molecular Biology, Vol. 78.
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)
Meeting Abstract (2)
79.
Meeting Abstract
34 (S1), p. 1 - 1. Annual Meeting on Experimental Biology, San Diego, CA, April 04, 2020 - April 07, 2020. The Federation, Bethesda, Md. (2020)
Cellular Machineries Devoted to Rubisco - the Most Abundant Enzyme. In The FASEB Journal, 80.
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,