| In vivo aspects of protein folding and quality control D Balchin, M Hayer-Hartl, FU Hartl Science 353 (6294), aac4354, 2016 | 1475 | 2016 |
| Recent advances in understanding catalysis of protein folding by molecular chaperones D Balchin, M Hayer‐Hartl, FU Hartl FEBS letters 594 (17), 2770-2781, 2020 | 156 | 2020 |
| Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein R Imamoglu, D Balchin, M Hayer-Hartl, FU Hartl Nature Communications 11 (1), 365, 2020 | 128 | 2020 |
| Pathway of actin folding directed by the eukaryotic chaperonin TRiC D Balchin, G Miličić, M Strauss, M Hayer-Hartl, FU Hartl Cell 174 (6), 1507-1521. e16, 2018 | 95 | 2018 |
| Tc toxin activation requires unfolding and refolding of a β-propeller C Gatsogiannis, F Merino, D Roderer, D Balchin, E Schubert, A Kuhlee, ... Nature 563 (7730), 209-213, 2018 | 54 | 2018 |
| Chaperone function of Hgh1 in the biogenesis of eukaryotic elongation factor 2 L Mönkemeyer, CL Klaips, D Balchin, R Körner, FU Hartl, A Bracher Molecular cell 74 (1), 88-100. e9, 2019 | 34 | 2019 |
| Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1 D Balchin, S Fanucchi, I Achilonu, RJ Adamson, J Burke, M Fernandes, ... Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1804 (12), 2228-2233, 2010 | 23 | 2010 |
| Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer S Gildenhuys, LA Wallace, JP Burke, D Balchin, Y Sayed, HW Dirr Biochemistry 49 (24), 5074-5081, 2010 | 23 | 2010 |
| Efficient catalysis of protein folding by GroEL/ES of the obligate chaperonin substrate MetF AK Singh, D Balchin, R Imamoglu, M Hayer-Hartl, FU Hartl Journal of molecular biology 432 (7), 2304-2318, 2020 | 19 | 2020 |
| S-nitrosation of glutathione transferase p1-1 is controlled by the conformation of a dynamic active site helix D Balchin, L Wallace, HW Dirr Journal of Biological Chemistry 288 (21), 14973-14984, 2013 | 16 | 2013 |
| S-Nitrosation Destabilizes Glutathione Transferase P1-1 D Balchin, SH Stoychev, HW Dirr Biochemistry 52 (51), 9394-9402, 2013 | 11 | 2013 |
| Resolving chaperone-assisted protein folding on the ribosome at the peptide level TE Wales, A Pajak, A Roeselová, S Shivakumaraswamy, S Howell, ... Nature Structural & Molecular Biology 31 (12), 1888-1897, 2024 | 9 | 2024 |
| Mechanism of chaperone coordination during cotranslational protein folding in bacteria A Roeselová, SL Maslen, S Shivakumaraswamy, GA Pellowe, S Howell, ... Molecular Cell, 2024 | 4 | 2024 |
| Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent D Balchin, HW Dirr, Y Sayed Biophysical Chemistry 156 (2-3), 153-158, 2011 | 3 | 2011 |
| GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome A Roeselova, SL Maslen, JZ He, G Jurkeviciute, M Skehel, RI Enchev, ... bioRxiv, 2024.08. 12.607569, 2024 | 1 | 2024 |
| Calmodulin regulates protease versus co-chaperone activity of a metacaspase AM Eisele-Bürger, F Eisele, SM Hill, X Hao, KL Schneider, R Imamoglu, ... Cell Reports 42 (11), 2023 | 1 | 2023 |
| The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking GA Pellowe, TB Voisin, L Karpauskaite, SL Maslen, A Roeselova, ... bioRxiv, 2024.09. 19.613857, 2024 | | 2024 |
| Using Hydrogen-Deuterium Exchange (HDX) Mass Spectrometry (MS) to Investigate Cotranslational Folding T Wales, A Pajak, A Roeselova, S Shiwakumaraswamy, S Howell, ... PROTEIN SCIENCE 32 (12), 2023 | | 2023 |
| Introduction: Molecular Chaperones and Protein Quality Control D Balchin, MA Rangel, RS Samant | | 2023 |
| Regulation of glutathione transferase P1-1 by S-nitrosation D Balchin PQDT-Global, 2013 | | 2013 |
Ulrich HartlDirector, Max Planck Institute of BiochemistryVerified email at biochem.mpg.de
