David Balchin

2.2k total citations · 1 hit paper
17 papers, 1.5k citations indexed

About

David Balchin is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, David Balchin has authored 17 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 3 papers in Materials Chemistry and 2 papers in Oncology. Recurrent topics in David Balchin's work include Heat shock proteins research (9 papers), Glutathione Transferases and Polymorphisms (5 papers) and Protein Structure and Dynamics (4 papers). David Balchin is often cited by papers focused on Heat shock proteins research (9 papers), Glutathione Transferases and Polymorphisms (5 papers) and Protein Structure and Dynamics (4 papers). David Balchin collaborates with scholars based in Germany, South Africa and United Kingdom. David Balchin's co-authors include F. Ulrich Hartl, Manajit Hayer‐Hartl, Goran Miličić, Mike Strauss, Heini W. Dirr, Louise Wallace, Anne Kuhlee, Christos Gatsogiannis, Evelyn Schubert and Felipe Merino and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David Balchin

15 papers receiving 1.5k citations

Hit Papers

In vivo aspects of protein folding and quality control 2016 2026 2019 2022 2016 250 500 750 1000
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. In vivo aspects of protein folding and quality control
    2016 1.0k citations David Balchin, Manajit Hayer‐Hartl et al. Science profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
David Balchin Germany 11 1.2k 329 272 131 120 17 1.5k
Can Kayatekin United States 15 1.2k 1.0× 215 0.7× 242 0.9× 160 1.2× 84 0.7× 23 1.5k
Marta Carroni Sweden 19 872 0.7× 183 0.6× 191 0.7× 114 0.9× 60 0.5× 28 1.2k
Peter Sheffield United States 12 975 0.8× 293 0.9× 182 0.7× 71 0.5× 63 0.5× 28 1.3k
Paul LaPointe Canada 16 1.4k 1.1× 731 2.2× 152 0.6× 130 1.0× 136 1.1× 35 1.9k
Abdussalam Azem Israel 32 2.3k 1.9× 311 0.9× 528 1.9× 86 0.7× 184 1.5× 85 2.7k
Kausik Chakraborty India 19 810 0.7× 188 0.6× 227 0.8× 94 0.7× 112 0.9× 32 1.1k
Florian Stengel Germany 30 2.5k 2.1× 533 1.6× 439 1.6× 158 1.2× 102 0.8× 69 3.2k
Vishwas R. Agashe Germany 11 1.6k 1.3× 353 1.1× 449 1.7× 86 0.7× 253 2.1× 11 1.9k
Rina Rosenzweig Israel 22 2.2k 1.8× 604 1.8× 406 1.5× 141 1.1× 202 1.7× 35 2.6k
Marco Retzlaff Germany 9 839 0.7× 212 0.6× 126 0.5× 63 0.5× 85 0.7× 10 1.0k

Countries citing papers authored by David Balchin

Since Specialization
Citations

This map shows the geographic impact of David Balchin's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by David Balchin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites David Balchin more than expected).

Fields of papers citing papers by David Balchin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David Balchin. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by David Balchin. The network helps show where David Balchin may publish in the future.

Co-authorship network of co-authors of David Balchin

This figure shows the co-authorship network connecting the top 25 collaborators of David Balchin. A scholar is included among the top collaborators of David Balchin based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with David Balchin. David Balchin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

17 of 17 papers shown
1.
Maslen, Sarah, et al.. (2025). GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome. Nature Communications. 16(1). 9976–9976.
2.
Maslen, Sarah, Mark Skehel, Chloë Roustan, et al.. (2025). The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking. Nature Structural & Molecular Biology. 32(11). 2296–2307.
3.
Wales, Thomas E., Aleksandra Pajak, Steven Howell, et al.. (2024). Resolving chaperone-assisted protein folding on the ribosome at the peptide level. Nature Structural & Molecular Biology. 31(12). 1888–1897. 9 indexed citations
4.
Maslen, Sarah, Steven Howell, Dhira Joshi, et al.. (2024). Mechanism of chaperone coordination during cotranslational protein folding in bacteria. Molecular Cell. 84(13). 2455–2471.e8. 13 indexed citations
5.
Eisele, Frederik, Sandra Malmgren Hill, Xinxin Hao, et al.. (2023). Calmodulin regulates protease versus co-chaperone activity of a metacaspase. Cell Reports. 42(11). 113372–113372. 3 indexed citations
6.
Balchin, David, et al.. (2020). Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein. Nature Communications. 11(1). 365–365. 103 indexed citations
7.
Balchin, David, Manajit Hayer‐Hartl, & F. Ulrich Hartl. (2020). Recent advances in understanding catalysis of protein folding by molecular chaperones. FEBS Letters. 594(17). 2770–2781. 112 indexed citations
8.
Singh, Amit Kumar, et al.. (2020). Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF. Journal of Molecular Biology. 432(7). 2304–2318. 15 indexed citations
9.
Mönkemeyer, Leonie, Courtney L. Klaips, David Balchin, et al.. (2019). Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. Molecular Cell. 74(1). 88–100.e9. 24 indexed citations
10.
Balchin, David, Goran Miličić, Mike Strauss, Manajit Hayer‐Hartl, & F. Ulrich Hartl. (2018). Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC. Cell. 174(6). 1507–1521.e16. 66 indexed citations
11.
Gatsogiannis, Christos, Felipe Merino, Daniel Roderer, et al.. (2018). Tc toxin activation requires unfolding and refolding of a β-propeller. Nature. 563(7730). 209–213. 37 indexed citations
12.
Balchin, David, Manajit Hayer‐Hartl, & F. Ulrich Hartl. (2016). In vivo aspects of protein folding and quality control. Science. 353(6294). aac4354–aac4354. 1045 indexed citations breakdown →
13.
Balchin, David, Louise Wallace, & Heini W. Dirr. (2013). S-Nitrosation of Glutathione Transferase P1-1 Is Controlled by the Conformation of a Dynamic Active Site Helix. Journal of Biological Chemistry. 288(21). 14973–14984. 10 indexed citations
14.
Balchin, David, Stoyan Stoychev, & Heini W. Dirr. (2013). S-Nitrosation Destabilizes Glutathione Transferase P1-1. Biochemistry. 52(51). 9394–9402. 9 indexed citations
15.
Balchin, David, Heini W. Dirr, & Yasien Sayed. (2011). Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent. Biophysical Chemistry. 156(2-3). 153–158. 3 indexed citations
16.
Balchin, David, Sylvia Fanucchi, Ikechukwu Achilonu, et al.. (2010). Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804(12). 2228–2233. 14 indexed citations
17.
Gildenhuys, Samantha, et al.. (2010). Class Pi Glutathione Transferase Unfolds via a Dimeric and Not Monomeric Intermediate: Functional Implications for an Unstable Monomer. Biochemistry. 49(24). 5074–5081. 15 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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