Publications
Journal Article (13)
1.
Journal Article
183 (2), pp. 457 - 473.e20 (2020)
Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes. Cell 2.
Journal Article
594, pp. 2770 - 2781 (2020)
Recent advances in understanding catalysis of protein folding by molecular chaperones. FEBS Letters 3.
Journal Article
25, pp. 407 - 416 (2020)
An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space. Cell Stress & Chaperones 4.
Journal Article
15 (4), e0230090 (2020)
Structure and conformational cycle of a bacteriophage-encoded chaperonin. PLOS ONE 5.
Journal Article
117 (8), pp. 4099 - 4108 (2020)
Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 6.
Journal Article
19 (5), pp. 733 - 741 (2020)
Amplifiers co-translationally enhance CFTR biosynthesis via PCBP1-mediated regulation of CFTR mRNA. Journal of cystic fibrosis 7.
Journal Article
45 (9), pp. 748 - 763 (2020)
Chaperone Machineries of Rubisco - The Most Abundant Enzyme. Trends in biochemical sciences 8.
Journal Article
401 (6-7), pp. 643 - 644 (2020)
Mitochondria and friends - a special issue in honor of Walter Neupert (1939-2019). BIOLOGICAL CHEMISTRY 9.
Journal Article
11 (1), 365 (2020)
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein. NATURE COMMUNICATIONS 10.
Journal Article
39 (8), e102811 (2020)
Cell-to-cell transmission of C9orf72 poly-(Gly-Ala) triggers key features of ALS/FTD. EMBO JOURNAL 11.
Journal Article
11 (1), 6271 (2020)
Sis1 potentiates the stress response to protein aggregation and elevated temperature. Nature Communications 12.
Journal Article
432 (7), pp. 2304 - 2318 (2020)
Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF. JOURNAL OF MOLECULAR BIOLOGY 13.
Journal Article
117 (2), pp. 1015 - 1020 (2020)
Proteome-wide observation of the phenomenon of life on the edge of solubility. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA