Publications by authors named "David Balchin"

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J-domain proteins: from molecular mechanisms to diseases.
Janine Kirstein, Rina Rosenzweig, Paolo De Los Rios, Pierre Genevaux, Charlotte Adang, David Balchin

Cell Stress Chaperones· December 2025

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The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.
Grant A Pellowe, Tomas B Voisin, Laura Karpauskaite, Sarah L Maslen, Alžběta Roeselová, David Balchin

Nat Struct Mol Biol· November 2025

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GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.
Alžběta Roeselová, Sarah L Maslen, Jessica Zhiyun He, Gabija Jurkeviciute, Aleksandra Pajak, David Balchin

Nat Commun· November 2025

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Resolving chaperone-assisted protein folding on the ribosome at the peptide level.
Thomas E Wales, Aleksandra Pajak, Alžběta Roeselová, Santosh Shivakumaraswamy, Steven Howell, David Balchin

Nat Struct Mol Biol· December 2024

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Mechanism of chaperone coordination during cotranslational protein folding in bacteria.
Alžběta Roeselová, Sarah L Maslen, Santosh Shivakumaraswamy, Grant A Pellowe, Steven Howell, David Balchin

Mol Cell· July 2024

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Calmodulin regulates protease versus co-chaperone activity of a metacaspase.
Anna Maria Eisele-Bürger, Frederik Eisele, Sandra Malmgren Hill, Xinxin Hao, Kara L Schneider, David Balchin

Cell Rep· November 2023

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Recent advances in understanding catalysis of protein folding by molecular chaperones.
David Balchin, Manajit Hayer-Hartl, F Ulrich Hartl

FEBS Lett· September 2020

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Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF.
Amit K Singh, David Balchin, Rahmi Imamoglu, Manajit Hayer-Hartl, F Ulrich Hartl

J Mol Biol· March 2020

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Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein.
Rahmi Imamoglu, David Balchin, Manajit Hayer-Hartl, F Ulrich Hartl

Nat Commun· January 2020

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Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2.
Leonie Mönkemeyer, Courtney L Klaips, David Balchin, Roman Körner, F Ulrich Hartl

Mol Cell· April 2019

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Tc toxin activation requires unfolding and refolding of a β-propeller.
Christos Gatsogiannis, Felipe Merino, Daniel Roderer, David Balchin, Evelyn Schubert

Nature· November 2018

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Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC.
David Balchin, Goran Miličić, Mike Strauss, Manajit Hayer-Hartl, F Ulrich Hartl

Cell· September 2018

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In vivo aspects of protein folding and quality control.
David Balchin, Manajit Hayer-Hartl, F Ulrich Hartl

Science· July 2016

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S-Nitrosation destabilizes glutathione transferase P1-1.
David Balchin, Stoyan H Stoychev, Heini W Dirr

Biochemistry· December 2013

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S-nitrosation of glutathione transferase p1-1 is controlled by the conformation of a dynamic active site helix.
David Balchin, Louise Wallace, Heini W Dirr

J Biol Chem· May 2013

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Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent.
David Balchin, Heini W Dirr, Yasien Sayed

Biophys Chem· July 2011

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Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1.
David Balchin, Sylvia Fanucchi, Ikechukwu Achilonu, Roslin J Adamson, Jonathan Burke

Biochim Biophys Acta· December 2010

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Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer.
Samantha Gildenhuys, Louise A Wallace, Jonathan P Burke, David Balchin, Yasien Sayed

Biochemistry· June 2010

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