Martin Högbom

4.6k total citations
103 papers, 3.3k citations indexed

About

Martin Högbom is a scholar working on Molecular Biology, Inorganic Chemistry and Materials Chemistry. According to data from OpenAlex, Martin Högbom has authored 103 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 68 papers in Molecular Biology, 35 papers in Inorganic Chemistry and 26 papers in Materials Chemistry. Recurrent topics in Martin Högbom's work include Metal-Catalyzed Oxygenation Mechanisms (35 papers), Enzyme Structure and Function (23 papers) and Porphyrin Metabolism and Disorders (17 papers). Martin Högbom is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (35 papers), Enzyme Structure and Function (23 papers) and Porphyrin Metabolism and Disorders (17 papers). Martin Högbom collaborates with scholars based in Sweden, United States and Germany. Martin Högbom's co-authors include P. Nordlund, Britt‐Marie Sjöberg, Julia J. Griese, Terese Bergfors, T. Alwyn Jones, Adrian Suárez Covarrubias, Martin Andersson, M.J. Tarry, Pål Stenmark and Astrid Gräslund and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Martin Högbom

100 papers receiving 3.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Martin Högbom Sweden 31 2.3k 843 499 476 378 103 3.3k
Derek T. Logan Sweden 38 3.0k 1.3× 909 1.1× 737 1.5× 548 1.2× 315 0.8× 119 4.8k
Ryosuke Nakashima Japan 17 4.1k 1.8× 632 0.7× 610 1.2× 721 1.5× 746 2.0× 45 6.3k
Scott Lovell United States 39 1.9k 0.8× 625 0.7× 506 1.0× 397 0.8× 542 1.4× 157 4.4k
S. Turley United States 27 1.7k 0.7× 500 0.6× 486 1.0× 306 0.6× 189 0.5× 43 2.9k
Lothar Esser United States 32 2.2k 1.0× 805 1.0× 565 1.1× 456 1.0× 626 1.7× 77 4.4k
J.B. Bonanno United States 37 2.5k 1.1× 573 0.7× 616 1.2× 419 0.9× 344 0.9× 81 4.5k
V.V. Barynin Russia 28 1.3k 0.6× 834 1.0× 623 1.2× 603 1.3× 207 0.5× 42 2.6k
Vilmos Fülöp United Kingdom 35 2.5k 1.1× 607 0.7× 644 1.3× 1.2k 2.5× 204 0.5× 120 4.7k
Hans E. Parge United States 23 2.0k 0.9× 468 0.6× 277 0.6× 551 1.2× 265 0.7× 44 3.7k
Peter Orth Germany 28 2.5k 1.1× 424 0.5× 518 1.0× 258 0.5× 391 1.0× 55 3.9k

Countries citing papers authored by Martin Högbom

Since Specialization
Citations

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

Fields of papers citing papers by Martin Högbom

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Martin Högbom. 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 Martin Högbom. The network helps show where Martin Högbom may publish in the future.

Co-authorship network of co-authors of Martin Högbom

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Högbom. A scholar is included among the top collaborators of Martin Högbom 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 Martin Högbom. Martin Högbom 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.
John, Juliane, Daniel Lundin, Rui M. Branca, et al.. (2025). Characterization of a second class Ie ribonucleotide reductase. Communications Biology. 8(1). 281–281.
2.
Abou‐Hamdan, Abbas, Olivier Biner, Dan Sjöstrand, et al.. (2025). Molecular Principles of Proton-Coupled Quinone Reduction in the Membrane-Bound Superoxide Oxidase. Journal of the American Chemical Society. 147(8). 6866–6879. 1 indexed citations
3.
Król, Sylwia, Ana P. Gámiz‐Hernández, Dan Sjöstrand, et al.. (2024). Inhibition mechanism of potential antituberculosis compound lansoprazole sulfide. Proceedings of the National Academy of Sciences. 121(47). e2412780121–e2412780121. 1 indexed citations
4.
Gámiz‐Hernández, Ana P., et al.. (2024). Long-range charge transfer mechanism of the III2IV2 mycobacterial supercomplex. Nature Communications. 15(1). 5276–5276. 8 indexed citations
5.
Moréno, Alexis, Benjamin Wiseman, Atanu Banerjee, et al.. (2023). Purification and characterization of Cdr1, the drug-efflux pump conferring azole resistance in Candida species. Biochimie. 220. 167–178. 6 indexed citations
6.
Srinivas, Vivek, Annika Johansson, Anders Nordström, et al.. (2022). Comparative structural analysis provides new insights into the function of R2‐like ligand‐binding oxidase. FEBS Letters. 596(12). 1600–1610. 3 indexed citations
7.
Chaptal, Vincent, Benjamin Wiseman, Cédric Orelle, et al.. (2022). Substrate-bound and substrate-free outward-facing structures of a multidrug ABC exporter. Science Advances. 8(4). eabg9215–eabg9215. 29 indexed citations
8.
Martínez‐Carranza, Markel, Venkateswara Rao Jonna, Daniel Lundin, et al.. (2020). A ribonucleotide reductase from Clostridium botulinum reveals distinct evolutionary pathways to regulation via the overall activity site. Journal of Biological Chemistry. 295(46). 15576–15587. 11 indexed citations
9.
Shilova, Anastasya, Hugo Lebrette, Oskar Aurelius, et al.. (2020). Current status and future opportunities for serial crystallography at MAX IV Laboratory. Journal of Synchrotron Radiation. 27(5). 1095–1102. 10 indexed citations
10.
Xu, Hongyi, Hugo Lebrette, Max T. B. Clabbers, et al.. (2019). Solving a new R2lox protein structure by microcrystal electron diffraction. Science Advances. 5(8). eaax4621–eaax4621. 63 indexed citations
11.
Bennett, M.D. & Martin Högbom. (2017). Crystal structure of the essential biotin‐dependent carboxylase AccA3 from Mycobacterium tuberculosis. FEBS Open Bio. 7(5). 620–626. 5 indexed citations
12.
Griese, Julia J., et al.. (2015). Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor. Journal of Biological Chemistry. 290(42). 25254–25272. 27 indexed citations
13.
Griese, Julia J., Vivek Srinivas, & Martin Högbom. (2014). Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins. JBIC Journal of Biological Inorganic Chemistry. 19(6). 759–774. 19 indexed citations
14.
Berntsson, Ronnie P.‐A., et al.. (2013). Structural insight into DNA binding and oligomerization of the multifunctional Cox protein of bacteriophage P2. Nucleic Acids Research. 42(4). 2725–2735. 8 indexed citations
15.
16.
Svensson, L., Ann‐Sofie Jemth, Matthieu Desroses, et al.. (2011). Crystal structure of human MTH1 and the 8-oxo-dGMP product complex. FEBS Letters. 585(16). 2617–2621. 67 indexed citations
17.
Högbom, Martin, et al.. (2009). A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold. Proceedings of the National Academy of Sciences. 106(14). 5633–5638. 68 indexed citations
18.
Wagner, Samuel, Mirjam Klepsch, Susan Schlegel, et al.. (2008). Tuning Escherichia coli for membrane protein overexpression. Proceedings of the National Academy of Sciences. 105(38). 14371–14376. 343 indexed citations
19.
Högbom, Martin, U.B. Ericsson, Robert Lam, et al.. (2005). A High Throughput Method for the Detection of Metalloproteins on a Microgram Scale. Molecular & Cellular Proteomics. 4(6). 827–834. 34 indexed citations
20.
Högbom, Martin, Martin Andersson, Matthias Kolberg, et al.. (2003). Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-Å x-ray data. Proceedings of the National Academy of Sciences. 100(6). 3209–3214. 130 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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