Marcel Asso

1.9k total citations
57 papers, 1.6k citations indexed

About

Marcel Asso is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Spectroscopy. According to data from OpenAlex, Marcel Asso has authored 57 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 22 papers in Renewable Energy, Sustainability and the Environment and 13 papers in Spectroscopy. Recurrent topics in Marcel Asso's work include Metalloenzymes and iron-sulfur proteins (22 papers), Metal-Catalyzed Oxygenation Mechanisms (10 papers) and Photosynthetic Processes and Mechanisms (9 papers). Marcel Asso is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (22 papers), Metal-Catalyzed Oxygenation Mechanisms (10 papers) and Photosynthetic Processes and Mechanisms (9 papers). Marcel Asso collaborates with scholars based in France, Morocco and Portugal. Marcel Asso's co-authors include Patrick Bertrand, Bruno Guigliarelli, Claude Moré, Francis Blasco, E. Claude Hatchikian, Axel Magalon, Bruno Guigliarelli, André Fournel, Richard A. Rothery and François Dolé and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Chemical Physics.

In The Last Decade

Marcel Asso

54 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Marcel Asso France 24 780 655 414 287 184 57 1.6k
W H Orme-Johnson United States 23 951 1.2× 816 1.2× 462 1.1× 345 1.2× 130 0.7× 38 1.8k
Francis Blasco France 25 991 1.3× 946 1.4× 443 1.1× 310 1.1× 105 0.6× 32 1.9k
A. Andrew Pacheco United States 21 610 0.8× 444 0.7× 360 0.9× 207 0.7× 180 1.0× 40 1.4k
B.H. Huynh United States 19 903 1.2× 462 0.7× 338 0.8× 427 1.5× 109 0.6× 26 1.5k
B.H. Huynh United States 21 991 1.3× 823 1.3× 1.0k 2.5× 521 1.8× 112 0.6× 27 2.0k
Sergei V. Khangulov United States 18 628 0.8× 624 1.0× 623 1.5× 327 1.1× 72 0.4× 25 1.5k
Bruno Guigliarelli France 34 2.2k 2.8× 753 1.1× 645 1.6× 603 2.1× 607 3.3× 62 3.0k
Marie‐Hélène Charon France 11 1.3k 1.7× 639 1.0× 459 1.1× 424 1.5× 209 1.1× 19 2.0k
Sofia R. Pauleta Portugal 21 316 0.4× 414 0.6× 290 0.7× 233 0.8× 129 0.7× 66 1.2k
Christopher J. Batie United States 17 271 0.3× 821 1.3× 455 1.1× 170 0.6× 86 0.5× 23 1.4k

Countries citing papers authored by Marcel Asso

Since Specialization
Citations

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

Fields of papers citing papers by Marcel Asso

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Marcel Asso

This figure shows the co-authorship network connecting the top 25 collaborators of Marcel Asso. A scholar is included among the top collaborators of Marcel Asso 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 Marcel Asso. Marcel Asso 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.
Jakoncic, Jean, Larry C. Sieker, V. Stojanoff, et al.. (2006). Structure of a [2Fe–2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe–S cluster biogenesis and conformational changes observed upon reduction. JBIC Journal of Biological Inorganic Chemistry. 11(2). 235–246. 24 indexed citations
2.
Dermoun, Zorah, Gilles De Luca, Marcel Asso, et al.. (2002). The NADP-reducing hydrogenase from Desulfovibrio fructosovorans: functional interaction between the C-terminal region of HndA and the N-terminal region of HndD subunits. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1556(2-3). 217–225. 19 indexed citations
3.
Klonowska, Agnieszka, Christian Gaudin, André Fournel, et al.. (2002). Characterization of a low redox potential laccase from the basidiomycete C30. European Journal of Biochemistry. 269(24). 6119–6125. 64 indexed citations
4.
Bertrand, Patrick, François Dolé, Marcel Asso, & Bruno Guigliarelli. (2000). Is there a rate-limiting step in the catalytic cycle of [Ni-Fe] hydrogenases?. JBIC Journal of Biological Inorganic Chemistry. 5(6). 682–691. 26 indexed citations
5.
Jouanneau, Yves, Christine Meyer, Marcel Asso, Bruno Guigliarelli, & John C. Willison. (2000). Characterization of a nif‐regulated flavoprotein (FprA) from Rhodobacter capsulatus. European Journal of Biochemistry. 267(3). 780–787. 16 indexed citations
6.
Moré, Claude, et al.. (1999). EPR spectroscopy: A powerful technique for the structural and functional investigation of metalloproteins. Biospectroscopy. 5(S5). S3–S18. 32 indexed citations
7.
Rousset, Marc, Yaël Montet, Bruno Guigliarelli, et al.. (1998). [3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis. Proceedings of the National Academy of Sciences. 95(20). 11625–11630. 153 indexed citations
9.
Pieulle, Lætitia, et al.. (1995). Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1250(1). 49–59. 94 indexed citations
10.
Asso, Marcel, et al.. (1995). EPR and Redox Characterization of Ferredoxins I and II from Desulfovibrio vulgaris Miyazaki. Biochemical and Biophysical Research Communications. 211(1). 198–204. 11 indexed citations
11.
Bertrand, P., et al.. (1994). Individual redox characteristics and kinetic properties of the hemes in cytochromes c3: New methods of investigation. Biochimie. 76(6). 524–536. 12 indexed citations
14.
Guigliarelli, Bruno, et al.. (1992). EPR and redox characterization of iron‐sulfur centers in nitrate reductases A and Z from Escherichia coli. European Journal of Biochemistry. 207(1). 61–68. 93 indexed citations
15.
Asso, Marcel, Bruno Guigliarelli, Tatsuhiko Yagi, & Patrick Bertrand. (1992). EPR and redox properties of Desulfovibrio vulgaris Miyazaki hydrogenase: Comparison with the NiFe enzyme from Desulfovibrio gigas. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1122(1). 50–56. 43 indexed citations
16.
Asso, Marcel, et al.. (1985). Copper and Nickel Interactions with Aspartate Containing Tetrapeptide. Spectroscopy Letters. 18(10). 837–842. 1 indexed citations
17.
Asso, Marcel, et al.. (1984). Iron (II) Complex of Benzylpenicillin, Synthesis and Infrared Structural Characterisation. Spectroscopy Letters. 17(4-5). 271–278. 15 indexed citations
18.
Asso, Marcel, et al.. (1984). Etudes des complexes métalliques de Ac-Asp-Val-Asp-Ala-OH par potentiométrie et résonance magnétique nucléaire du 1H. Canadian Journal of Chemistry. 62(11). 2379–2384. 3 indexed citations
19.
Asso, Marcel, et al.. (1976). Conformation des complexes de lanthanides avec la l-phosphosérine et la phosphoéthanolamine en phase aqueuse. Journal de Chimie Physique. 73. 315–318. 6 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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