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David Balchin
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In vivo aspects of protein folding and quality control
D Balchin, M Hayer-Hartl, FU Hartl
Science 353 (6294), aac4354, 2016
13342016
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
1272020
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
1072020
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
782018
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
472018
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
252019
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
232010
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
202010
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
172020
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
152013
S-Nitrosation Destabilizes Glutathione Transferase P1-1
D Balchin, SH Stoychev, HW Dirr
Biochemistry 52 (51), 9394-9402, 2013
92013
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
TE Wales, A Pajak, A Roeselová, S Shivakumaraswamy, S Howell, ...
bioRxiv, 2022.09. 23.509153, 2022
32022
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
32011
Mechanism of chaperone coordination during cotranslational protein folding in bacteria
A Roeselova, SL Maslen, S Shivakumaraswamy, GA Pellowe, S Howell, ...
bioRxiv, 2024.01. 22.576655, 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
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
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
2014
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