Tore Vänngård

5.7k total citations · 1 hit paper
98 papers, 4.7k citations indexed

About

Tore Vänngård is a scholar working on Molecular Biology, Electrochemistry and Cell Biology. According to data from OpenAlex, Tore Vänngård has authored 98 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 24 papers in Electrochemistry and 20 papers in Cell Biology. Recurrent topics in Tore Vänngård's work include Photosynthetic Processes and Mechanisms (37 papers), Electrochemical Analysis and Applications (24 papers) and Enzyme-mediated dye degradation (17 papers). Tore Vänngård is often cited by papers focused on Photosynthetic Processes and Mechanisms (37 papers), Electrochemical Analysis and Applications (24 papers) and Enzyme-mediated dye degradation (17 papers). Tore Vänngård collaborates with scholars based in Sweden, United States and Finland. Tore Vänngård's co-authors include Bo G. Malmström, Roland Aasa, Lars‐Erik Andréasson, Bengt Reinhammar, Richard Malkin, Paul Saltman, Karl-Erik Falk, Göran Karlsson, Rolf Brändén and Robert C. Bray and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Tore Vänngård

98 papers receiving 4.3k citations

Hit Papers

align trajectories

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.

EPR signal intensity and powder shapes: A reexamination

1975 465 citations Roland Aasa, Tore Vänngård profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Tore Vänngård Sweden	41	2.5k	813	746	672	668	98	4.7k
Roland Aasa Sweden	34	2.4k 1.0×	838 1.0×	336 0.5×	468 0.7×	657 1.0×	74	4.3k
Philip George United States	46	2.2k 0.9×	713 0.9×	324 0.4×	668 1.0×	1.0k 1.5×	197	7.3k
Anders Ehrenberg Sweden	37	2.5k 1.0×	806 1.0×	268 0.4×	228 0.3×	453 0.7×	105	4.2k
Bo G. Malmström Sweden	56	5.4k 2.2×	1.5k 1.9×	1.0k 1.4×	1.2k 1.7×	1.1k 1.7×	173	8.9k
James A. Fee United States	44	3.0k 1.2×	2.1k 2.6×	264 0.4×	681 1.0×	797 1.2×	125	5.5k
E. J. Land United Kingdom	46	2.3k 0.9×	284 0.3×	415 0.6×	480 0.7×	1.8k 2.7×	150	7.3k
David B. Goodin United States	36	2.7k 1.1×	968 1.2×	447 0.6×	351 0.5×	552 0.8×	81	4.1k
Stephen G. Mayhew Ireland	37	3.3k 1.3×	577 0.7×	461 0.6×	287 0.4×	1.1k 1.6×	116	5.3k
Peter Hemmerich Germany	45	3.9k 1.6×	272 0.3×	718 1.0×	183 0.3×	774 1.2×	187	6.9k
António V. Xavier Portugal	52	4.0k 1.6×	1.5k 1.9×	283 0.4×	715 1.1×	1.6k 2.5×	191	8.1k

Countries citing papers authored by Tore Vänngård

Since Specialization

Citations

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

Fields of papers citing papers by Tore Vänngård

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tore Vänngård

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

All Works

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20 of 20 papers shown

Reinhammar, Bengt, et al.. (1997). The type 2 copper of ascorbate oxidase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1337(2). 191–197. 8 indexed citations

Karpefors, Martin, J.A. Fee, Roland Aasa, et al.. (1996). Electron paramagnetic resonance studies of the soluble CuA protein from the cytochrome ba3 of Thermus thermophilus. Biophysical Journal. 71(5). 2823–2829. 27 indexed citations

Sjölin, L., Vratislav Langer, Nicklas Bonander, et al.. (1995). Structure of the azurin mutant nickel–Trp48Met fromPseudomonas aeruginosaat 2.2 Å resolution. Acta Crystallographica Section D Biological Crystallography. 51(5). 711–717. 14 indexed citations

Sanders, Donita, et al.. (1995). Multi-frequency EPR Evidence for a Binuclear CuA Center in Cytochrome c Oxidase: Studies with a 63Cu- and 65Cu-Enriched, Soluble Domain of the Cytochrome ba3 Subunit II from Thermus thermophilus. Biochemical and Biophysical Research Communications. 212(1). 77–83. 19 indexed citations

Bonander, Nicklas, Göran Karlsson, & Tore Vänngård. (1995). Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1251(1). 48–54. 21 indexed citations

Pascher, Torbjörn, Göran Karlsson, Margareta Nordling, Bo G. Malmström, & Tore Vänngård. (1993). Reduction potentials and their pH dependence in site‐directed‐mutant forms of azurin from Pseudomonas aeruginosa. European Journal of Biochemistry. 212(2). 289–296. 141 indexed citations

Wydrzynski, Thomas J., et al.. (1989). H2O2 formation by Photosystem II. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 973(1). 23–28. 54 indexed citations

Pascher, Torbjörn, Jörgen Bergström, Bo G. Malmström, Tore Vänngård, & Lennart Lundberg. (1989). Modification of the electron‐transfer sites of Pseudomonas aeruginosa azurin by site‐directed mutagenesis. FEBS Letters. 258(2). 266–268. 17 indexed citations

Falk, Karl-Erik, Tore Vänngård, & Jonas Ångström. (1977). Heme spin‐states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements. FEBS Letters. 75(1-2). 23–27. 45 indexed citations

10.

Aasa, Roland, Rolf Brändén, Joke Deinum, et al.. (1976). A 17O-effect on the EPR spectrum of the intermediate in the dioxygen-laccase reaction. Biochemical and Biophysical Research Communications. 70(4). 1204–1209. 46 indexed citations

11.

Aasa, Roland, Rolf Brändén, Joke Deinum, et al.. (1976). A paramagnetic intermediate in the reduction of oxygen by reduced laccase. FEBS Letters. 61(2). 115–119. 48 indexed citations

12.

Deinum, Joke & Tore Vänngård. (1973). The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin. Biochimica et Biophysica Acta (BBA) - Protein Structure. 310(2). 321–330. 69 indexed citations

13.

Andréasson, Lars‐Erik, et al.. (1972). The reaction of ferrocytochrome c with cytochrome oxidase: A new look. FEBS Letters. 28(3). 297–301. 50 indexed citations

14.

Stigbrand, Torgny, et al.. (1971). On the state of copper in the blue protein umecyanin. FEBS Letters. 12(5). 260–262. 22 indexed citations

15.

Malkin, Richard, et al.. (1968). The requirement of the “non‐blue” copper (II) for the activity of fungal laccase. FEBS Letters. 1(1). 50–54. 55 indexed citations

16.

Ehrenberg, A. S. C., et al.. (1967). Magnetic resonance in biological systems : proceedings of the Second International Conference held at the Wenner-Gren Center Stockholm, June, 1966. 5 indexed citations

17.

Lund, Anders & Tore Vänngård. (1965). Note on the Determination of the Principal Fine and Hyperfine Coupling Constants in ESR. The Journal of Chemical Physics. 42(8). 2979–2980. 62 indexed citations

18.

Aasa, Roland, Bo G. Malmström, Paul Saltman, & Tore Vänngård. (1963). The specific binding of iron(III) and copper(II) to transferrin and conalbumin. Biochimica et Biophysica Acta. 75. 203–222. 316 indexed citations

19.

Christensen, Nina, et al.. (1963). An Intermediate formed in Sulphonation of Iodobenzene.. Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry. 17. 2253–2263. 6 indexed citations

20.

Aasa, Roland, et al.. (1961). Electron Spin Resonance Line-Widths in Solutions of Copper and Silver Dithiocarbamates. Nature. 190(4772). 258–259. 16 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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