H.-P. Hersleth

1.2k total citations
33 papers, 1.0k citations indexed

About

H.-P. Hersleth is a scholar working on Molecular Biology, Inorganic Chemistry and Cell Biology. According to data from OpenAlex, H.-P. Hersleth has authored 33 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 17 papers in Inorganic Chemistry and 12 papers in Cell Biology. Recurrent topics in H.-P. Hersleth's work include Metal-Catalyzed Oxygenation Mechanisms (15 papers), Hemoglobin structure and function (12 papers) and Enzyme Structure and Function (8 papers). H.-P. Hersleth is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (15 papers), Hemoglobin structure and function (12 papers) and Enzyme Structure and Function (8 papers). H.-P. Hersleth collaborates with scholars based in Norway, Sweden and United States. H.-P. Hersleth's co-authors include Carl Henrik Görbitz, Kristoffer Andersson, Ulf Ryde, Åsmund K. Røhr, K. Kristoffer Andersson, Marta Hammerstad, Patrik Rydberg, Niels H. Andersen, G.R. Andersen and Cristiano L. P. Oliveira and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

H.-P. Hersleth

31 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
H.-P. Hersleth Norway 15 541 369 304 257 92 33 1.0k
Kunihiko Tajima Japan 22 620 1.1× 292 0.8× 518 1.7× 101 0.4× 90 1.0× 112 1.6k
Jaroslava Mikšovská United States 21 729 1.3× 88 0.2× 280 0.9× 189 0.7× 77 0.8× 80 1.3k
Sue A. Roberts United States 22 641 1.2× 373 1.0× 378 1.2× 359 1.4× 26 0.3× 53 1.8k
Nozomi Saito Japan 31 412 0.8× 392 1.1× 153 0.5× 173 0.7× 31 0.3× 124 2.7k
Michael R. DeFelippis United States 23 811 1.5× 131 0.4× 259 0.9× 118 0.5× 180 2.0× 30 1.4k
Richard A. Bunce United States 26 964 1.8× 255 0.7× 151 0.5× 252 1.0× 33 0.4× 166 2.5k
Djemel Hamdane France 24 1.1k 2.0× 338 0.9× 238 0.8× 651 2.5× 37 0.4× 57 1.9k
Jonathan A. R. Worrall United Kingdom 27 1.5k 2.7× 227 0.6× 468 1.5× 251 1.0× 34 0.4× 79 2.1k
Koji Inaka Japan 22 959 1.8× 117 0.3× 541 1.8× 121 0.5× 35 0.4× 75 1.6k
I. Ascone France 17 419 0.8× 120 0.3× 408 1.3× 80 0.3× 57 0.6× 59 926

Countries citing papers authored by H.-P. Hersleth

Since Specialization
Citations

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

Fields of papers citing papers by H.-P. Hersleth

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by H.-P. Hersleth. 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 H.-P. Hersleth. The network helps show where H.-P. Hersleth may publish in the future.

Co-authorship network of co-authors of H.-P. Hersleth

This figure shows the co-authorship network connecting the top 25 collaborators of H.-P. Hersleth. A scholar is included among the top collaborators of H.-P. Hersleth 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 H.-P. Hersleth. H.-P. Hersleth 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.
Weirich, Sara, Marta Hammerstad, H.-P. Hersleth, et al.. (2025). Orthologues of the human protein histidine methyltransferase METTL9 display distinct substrate specificities. Journal of Biological Chemistry. 301(7). 110318–110318.
2.
3.
Hammerstad, Marta & H.-P. Hersleth. (2021). Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold – A functionally diverse group. Archives of Biochemistry and Biophysics. 702. 108826–108826. 20 indexed citations
4.
Hammerstad, Marta, Åsmund K. Røhr, & H.-P. Hersleth. (2019). A Research‐inspired biochemistry laboratory module–combining expression, purification, crystallization, structure‐solving, and characterization of a flavodoxin‐like protein. Biochemistry and Molecular Biology Education. 47(3). 318–332. 3 indexed citations
5.
6.
Hammerstad, Marta, et al.. (2017). Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST). BIO-PROTOCOL. 7(8). e2223–e2223. 3 indexed citations
7.
Hersleth, H.-P., et al.. (2014). Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) fromBacillus cereus. Acta Crystallographica Section F Structural Biology Communications. 70(6). 777–780. 3 indexed citations
8.
Can, Mehmet, J. Krucinska, Giorgio Zoppellaro, et al.. (2013). Structural Characterization of Nitrosomonas europaea Cytochrome c‐552 Variants with Marked Differences in Electronic Structure. ChemBioChem. 14(14). 1828–1838. 8 indexed citations
9.
Andersen, Christian Brix Folsted, Marianne Jensby Nielsen, Cristiano L. P. Oliveira, et al.. (2012). Structure of the haptoglobin–haemoglobin complex. Nature. 489(7416). 456–459. 184 indexed citations
10.
Røhr, Åsmund K., H.-P. Hersleth, & K. Kristoffer Andersson. (2010). Tracking Flavin Conformations in Protein Crystal Structures with Raman Spectroscopy and QM/MM Calculations. Angewandte Chemie International Edition. 49(13). 2324–2327. 65 indexed citations
11.
Hersleth, H.-P. & Kristoffer Andersson. (2010). How different oxidation states of crystalline myoglobin are influenced by X-rays. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(6). 785–796. 48 indexed citations
12.
Hersleth, H.-P., Ya‐Wen Hsiao, Ulf Ryde, Carl Henrik Görbitz, & K. Kristoffer Andersson. (2008). The Influence of X‐Rays on the Structural Studies of Peroxide‐Derived Myoglobin Intermediates. Chemistry & Biodiversity. 5(10). 2067–2089. 14 indexed citations
13.
Hersleth, H.-P., Ya‐Wen Hsiao, Ulf Ryde, Carl Henrik Görbitz, & Kristoffer Andersson. (2008). The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection. Biochemical Journal. 412(2). 257–264. 46 indexed citations
14.
Hersleth, H.-P., Takeshi Uchida, Åsmund K. Røhr, et al.. (2007). Crystallographic and Spectroscopic Studies of Peroxide-derived Myoglobin Compound II and Occurrence of Protonated FeIV–O. Journal of Biological Chemistry. 282(32). 23372–23386. 50 indexed citations
15.
Hersleth, H.-P., Åsmund K. Røhr, Peter P. Schmidt, et al.. (2007). Reactive complexes in myoglobin and nitric oxide synthase. Inorganica Chimica Acta. 361(4). 831–843. 6 indexed citations
16.
Hersleth, H.-P., Ulf Ryde, Patrik Rydberg, Carl Henrik Görbitz, & Kristoffer Andersson. (2006). Structures of the high-valent metal-ion haem–oxygen intermediates in peroxidases, oxygenases and catalases. Journal of Inorganic Biochemistry. 100(4). 460–476. 137 indexed citations
17.
Hersleth, H.-P., Takeshi Uchida, Åsmund K. Røhr, et al.. (2005). Structure of the intermediates in the myoglobin-peroxide reaction. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c214–c214. 1 indexed citations
18.
Nilsson, Kristina, H.-P. Hersleth, Thomas H. Rod, Kristoffer Andersson, & Ulf Ryde. (2004). The Protonation Status of Compound II in Myoglobin, Studied by a Combination of Experimental Data and Quantum Chemical Calculations: Quantum Refinement. Biophysical Journal. 87(5). 3437–3447. 50 indexed citations
19.
Hersleth, H.-P., Bjørn Dalhus, Carl Henrik Görbitz, & Kristoffer Andersson. (2002). An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2. JBIC Journal of Biological Inorganic Chemistry. 7(3). 299–304. 53 indexed citations
20.
Görbitz, Carl Henrik & H.-P. Hersleth. (2000). Selective solvent inclusion as a tool for mapping molecular properties in crystal structures: a diethylstilbestrol example. Acta Crystallographica Section B Structural Science. 56(6). 1094–1102. 7 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Kunihiko Tajima Breakdown of academic impact, for papers by Jaroslava Mikšovská Breakdown of academic impact, for papers by Sue A. Roberts Breakdown of academic impact, for papers by Nozomi Saito Breakdown of academic impact, for papers by Michael R. DeFelippis Breakdown of academic impact, for papers by Richard A. Bunce Breakdown of academic impact, for papers by Djemel Hamdane Breakdown of academic impact, for papers by Jonathan A. R. Worrall Breakdown of academic impact, for papers by Koji Inaka Breakdown of academic impact, for papers by I. Ascone
Rankless by CCL
2026