Andrew J. Baldwin

10.8k total citations · 4 hit papers
87 papers, 7.5k citations indexed

About

Andrew J. Baldwin is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Andrew J. Baldwin has authored 87 papers receiving a total of 7.5k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 18 papers in Materials Chemistry and 17 papers in Spectroscopy. Recurrent topics in Andrew J. Baldwin's work include Protein Structure and Dynamics (32 papers), Heat shock proteins research (17 papers) and Enzyme Structure and Function (14 papers). Andrew J. Baldwin is often cited by papers focused on Protein Structure and Dynamics (32 papers), Heat shock proteins research (17 papers) and Enzyme Structure and Function (14 papers). Andrew J. Baldwin collaborates with scholars based in United Kingdom, United States and Canada. Andrew J. Baldwin's co-authors include Carol V. Robinson, Justin L. P. Benesch, Lewis E. Kay, Timothy J. Nott, Timothy D. Craggs, Erik G. Marklund, Patrick Farber, Julie D. Forman‐Kay, Matteo T. Degiacomi and Georg Hochberg and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Andrew J. Baldwin

87 papers receiving 7.4k citations

Hit Papers

Phase Transition of a Disordered Nuage Protein Generates ... 2014 2026 2018 2022 2015 2015 2014 2017 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Andrew J. Baldwin United Kingdom 38 5.7k 1.4k 1.2k 651 567 87 7.5k
Gianluigi Veglia United States 47 4.9k 0.9× 2.1k 1.5× 1.4k 1.2× 705 1.1× 468 0.8× 216 7.6k
Elizabeth A. Komives United States 51 5.4k 0.9× 1.1k 0.8× 1.2k 1.1× 486 0.7× 661 1.2× 197 7.8k
Jonathan P. Waltho United Kingdom 45 4.6k 0.8× 720 0.5× 1.3k 1.2× 626 1.0× 448 0.8× 143 6.0k
Xavier Salvatella Spain 40 3.5k 0.6× 1.0k 0.7× 1.1k 1.0× 547 0.8× 302 0.5× 90 4.8k
Lorna J. Smith United Kingdom 35 4.8k 0.8× 1.3k 0.9× 2.9k 2.6× 448 0.7× 542 1.0× 101 6.8k
Asim Okur United States 14 5.5k 1.0× 809 0.6× 1.6k 1.4× 293 0.5× 322 0.6× 17 7.1k
Neil A. Farrow United States 30 3.8k 0.7× 849 0.6× 1.1k 0.9× 264 0.4× 463 0.8× 51 5.6k
Frank Sobott United Kingdom 49 4.5k 0.8× 2.5k 1.8× 970 0.8× 458 0.7× 474 0.8× 169 7.2k
John Christodoulou United Kingdom 39 3.7k 0.7× 505 0.4× 922 0.8× 1.0k 1.6× 592 1.0× 111 5.5k
Vladimı́r Saudek Czechia 39 6.0k 1.1× 996 0.7× 932 0.8× 937 1.4× 818 1.4× 96 8.4k

Countries citing papers authored by Andrew J. Baldwin

Since Specialization
Citations

This map shows the geographic impact of Andrew J. Baldwin'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 Andrew J. Baldwin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Andrew J. Baldwin more than expected).

Fields of papers citing papers by Andrew J. Baldwin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Andrew J. Baldwin. 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 Andrew J. Baldwin. The network helps show where Andrew J. Baldwin may publish in the future.

Co-authorship network of co-authors of Andrew J. Baldwin

This figure shows the co-authorship network connecting the top 25 collaborators of Andrew J. Baldwin. A scholar is included among the top collaborators of Andrew J. Baldwin 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 Andrew J. Baldwin. Andrew J. Baldwin is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Karunanithy, Gogulan, Olga Tkachenko, M. Barber, et al.. (2025). UnidecNMR: automatic peak detection for NMR spectra in 1-4 dimensions. Nature Communications. 16(1). 449–449. 2 indexed citations
2.
Karunanithy, Gogulan, et al.. (2025). Seedless: on-the-fly pulse calculation for NMR experiments. Nature Communications. 16(1). 7276–7276. 1 indexed citations
3.
Moynié, L., Sean A. Burnap, Mikhail A. Kutuzov, et al.. (2024). Covalent penicillin-protein conjugates elicit anti-drug antibodies that are clonally and functionally restricted. Nature Communications. 15(1). 6851–6851. 1 indexed citations
4.
5.
El‐Baba, Tarick J., Corinne A. Lutomski, Sean A. Burnap, et al.. (2023). Uncovering the Role of N-Glycan Occupancy on the Cooperative Assembly of Spike and Angiotensin Converting Enzyme 2 Complexes: Insights from Glycoengineering and Native Mass Spectrometry. Journal of the American Chemical Society. 145(14). 8021–8032. 13 indexed citations
6.
Baldwin, Andrew J. & Jonathan A. Jones. (2023). Efficiently computing the Uhlmann fidelity for density matrices. Physical review. A. 107(1). 10 indexed citations
7.
Rowbotham, Jack S., Miguel A. Ramirez, Gogulan Karunanithy, et al.. (2023). Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR. Chemical Science. 14(43). 12160–12165. 5 indexed citations
8.
Giltrap, Andrew M., Yibo Zeng, Daniel Oehlrich, et al.. (2022). Reductive site-selective atypical C , Z -type/N2-C2 cleavage allows C-terminal protein amidation. Science Advances. 8(14). eabl8675–eabl8675. 7 indexed citations
9.
Karunanithy, Gogulan, Alison Howarth, Amber L. Thompson, et al.. (2021). Cell-permeable lanthanide–platinum(iv) anti-cancer prodrugs. Dalton Transactions. 50(25). 8761–8767. 8 indexed citations
10.
Isenegger, Patrick G., Brian Josephson, Lukas Lercher, et al.. (2021). Post-translational insertion of boron in proteins to probe and modulate function. Nature Chemical Biology. 17(12). 1245–1261. 27 indexed citations
11.
Josephson, Brian, Charlie Fehl, Patrick G. Isenegger, et al.. (2020). Light-driven post-translational installation of reactive protein side chains. Nature. 585(7826). 530–537. 137 indexed citations
12.
Collier, M, T. Reid Alderson, Timothy M. Allison, et al.. (2019). HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C. Science Advances. 5(5). eaav8421–eaav8421. 54 indexed citations
13.
Imiołek, Mateusz, Gogulan Karunanithy, Wai‐Lung Ng, et al.. (2018). Selective Radical Trifluoromethylation of Native Residues in Proteins. Journal of the American Chemical Society. 140(5). 1568–1571. 110 indexed citations
14.
Hochberg, Georg, Dale A. Shepherd, Erik G. Marklund, et al.. (2018). Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science. 359(6378). 930–935. 47 indexed citations
15.
Brady, Jacob P., Patrick Farber, Ashok Sekhar, et al.. (2017). Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation. Proceedings of the National Academy of Sciences. 114(39). E8194–E8203. 376 indexed citations breakdown →
16.
Degiacomi, Matteo T., Carla Schmidt, Andrew J. Baldwin, & Justin L. P. Benesch. (2017). Accommodating Protein Dynamics in the Modeling of Chemical Crosslinks. Structure. 25(11). 1751–1757.e5. 34 indexed citations
17.
Karunanithy, Gogulan, Brian Lyons, Ritu Raj, et al.. (2017). Monitoring the Disassembly of Virus-like Particles by 19F-NMR. Journal of the American Chemical Society. 139(15). 5277–5280. 21 indexed citations
18.
Hochberg, Georg, Heath Ecroyd, Dezerae Cox, et al.. (2014). Dynamics and chaperone function in the small heat-shock protein αb-crystallin. Research Online (University of Wollongong). 1 indexed citations
19.
Baldwin, Andrew J. & Lewis E. Kay. (2013). An R1ρ expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates. Journal of Biomolecular NMR. 55(2). 211–218. 31 indexed citations
20.

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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