J. A. Jongejan

1.9k total citations
46 papers, 1.5k citations indexed

About

J. A. Jongejan is a scholar working on Molecular Biology, Biochemistry and Spectroscopy. According to data from OpenAlex, J. A. Jongejan has authored 46 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 8 papers in Biochemistry and 7 papers in Spectroscopy. Recurrent topics in J. A. Jongejan's work include Microbial metabolism and enzyme function (24 papers), Enzyme Catalysis and Immobilization (22 papers) and Microbial Metabolic Engineering and Bioproduction (11 papers). J. A. Jongejan is often cited by papers focused on Microbial metabolism and enzyme function (24 papers), Enzyme Catalysis and Immobilization (22 papers) and Microbial Metabolic Engineering and Bioproduction (11 papers). J. A. Jongejan collaborates with scholars based in Netherlands, Germany and Portugal. J. A. Jongejan's co-authors include Johannis A. Duine, Adrie J. J. Straathof, Johannes Frank, Joseph J. Heijnen, J. Frank Jzn, Johannis A. Duine, H. Groendijk, Kor H. Kalk, Wim G. J. Hol and Joost P.H. Drenth and has published in prestigious journals such as Journal of Biological Chemistry, Annual Review of Biochemistry and The EMBO Journal.

In The Last Decade

J. A. Jongejan

45 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J. A. Jongejan Netherlands 21 1.4k 398 223 197 131 46 1.5k
William S. McIntire United States 29 2.1k 1.6× 849 2.1× 339 1.5× 88 0.4× 156 1.2× 74 2.7k
Laura Morpurgo Italy 24 891 0.7× 299 0.8× 360 1.6× 42 0.2× 131 1.0× 83 1.6k
Jaap A. Jongejan Netherlands 23 956 0.7× 130 0.3× 85 0.4× 252 1.3× 105 0.8× 49 1.1k
Masaki Nojiri Japan 17 652 0.5× 144 0.4× 215 1.0× 95 0.5× 136 1.0× 34 1.1k
Michele A. McGuirl United States 22 1.1k 0.8× 509 1.3× 498 2.2× 28 0.1× 96 0.7× 40 1.5k
Christopher K. Savile Canada 14 1.6k 1.2× 288 0.7× 217 1.0× 94 0.5× 588 4.5× 21 2.0k
Qingcai Jiao China 19 652 0.5× 200 0.5× 48 0.2× 227 1.2× 168 1.3× 90 1.3k
Christopher J. Batie United States 17 821 0.6× 81 0.2× 455 2.0× 120 0.6× 33 0.3× 23 1.4k
Edgardo T. Farinas United States 17 838 0.6× 81 0.2× 269 1.2× 72 0.4× 150 1.1× 37 1.4k
Jeerus Sucharitakul Thailand 24 1.0k 0.8× 291 0.7× 252 1.1× 46 0.2× 121 0.9× 64 1.6k

Countries citing papers authored by J. A. Jongejan

Since Specialization
Citations

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

Fields of papers citing papers by J. A. Jongejan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. A. Jongejan

This figure shows the co-authorship network connecting the top 25 collaborators of J. A. Jongejan. A scholar is included among the top collaborators of J. A. Jongejan 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 J. A. Jongejan. J. A. Jongejan 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.
Jongejan, Aldo, J. A. Jongejan, & Wilfred R. Hagen. (2001). Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation. Journal of Computational Chemistry. 22(15). 1732–1749. 9 indexed citations
2.
Machado, Sônia Salgueiro, et al.. (2001). Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation step in the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus. Enzyme and Microbial Technology. 28(2-3). 233–239. 9 indexed citations
3.
Jongejan, Aldo, et al.. (1998). Homology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni. Protein Engineering Design and Selection. 11(3). 185–198. 15 indexed citations
4.
Orrenius, Christian, et al.. (1998). Simple conformation space search protocols for the evaluation of enantioselectivity of lipases. Protein Engineering Design and Selection. 11(12). 1147–1153. 13 indexed citations
5.
Orrenius, S, et al.. (1998). Lipase Mediated Resolution of γ-Branched Chain Fatty Acid Methyl Esters. Biocatalysis and Biotransformation. 16(2). 145–162. 18 indexed citations
6.
Wolff, Anders, et al.. (1997). Simple dissolution-reaction model for enzymatic conversion of suspension of solid substrate. Biotechnology and Bioengineering. 56(4). 433–440. 12 indexed citations
7.
Groen, Barend W., et al.. (1995). Identification of Topaquinone, As Illustrated for Pig Kidney Diamine Oxidase and Escherichia coli Amine Oxidase. Analytical Biochemistry. 230(1). 159–166. 12 indexed citations
8.
Jongejan, J. A., et al.. (1994). Studies on the production of (S)-(+)-solketal (2,2-dimethyl-1,3-dioxolane-4-methanol) by enantioselective oxidation of racemic solketal with Comamonas testosteroni. Applied Microbiology and Biotechnology. 42(1). 8–15. 2 indexed citations
9.
Huber, Claudia, Jorge Caldeira, J. A. Jongejan, & Helmut Simon. (1994). Further characterization of two different, reversible aldehyde oxidoreductases from Clostridium formicoaceticum, one containing tungsten and the other molybdenum. Archives of Microbiology. 162(5). 303–309. 27 indexed citations
10.
Geerlof, Arie, et al.. (1992). Kinetic Resolution of Racemic GlycerolDerivatives with Lipase and Quinohemoprotein Alcohol Dehydrogenasea. Annals of the New York Academy of Sciences. 672(1). 462–470. 7 indexed citations
11.
Jongejan, J. A., et al.. (1989). PQQ and quinoproteins : proceedings of the First International Symposium on PQQ and Quinoproteins, Delft, the Netherlands, 1988. Kluwer Academic Publishers eBooks. 1 indexed citations
12.
Duine, Johannis A. & J. A. Jongejan. (1989). Pyrroloquinoline Quinone: A Novel Cofactor. Vitamins and hormones. 45. 223–262. 19 indexed citations
13.
Duine, Johannis A. & J. A. Jongejan. (1989). QUINOPROTEINS, ENZYMES WITH PYRROLO-QUINOLINE QUINONE AS COFACTOR. Annual Review of Biochemistry. 58(1). 403–426. 112 indexed citations
14.
Vellieux, F.M.D., H. Groendijk, Kor H. Kalk, et al.. (1989). Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution.. The EMBO Journal. 8(8). 2171–2178. 109 indexed citations
15.
Jongejan, J. A., et al.. (1988). Dopamine β‐hydroxylase from bovine adrenal medulla contains covalently‐bound pyrroloquinoline quinone. FEBS Letters. 231(2). 303–307. 39 indexed citations
16.
Duine, Johannis A., et al.. (1987). Enzymology of Quinoproteins. Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects. 59. 169–212. 70 indexed citations
17.
Jongejan, J. A., et al.. (1986). Hydrazone formation of 2,4‐dinitrophenylhydrazine with pyrroloquinoline quinone in porcine kidney diamine oxidase. FEBS Letters. 206(1). 111–114. 56 indexed citations
18.
Koningsveld, H. van, et al.. (1985). Structure of the 2,4-dinitrophenylhydrazine adduct of pyrroloquinolinequinone (PQQ) dimethyl ethyl triester, C24H18N6O11. Acta Crystallographica Section C Crystal Structure Communications. 41(1). 89–92. 6 indexed citations
19.
Jongejan, J. A., et al.. (1984). Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group. FEBS Letters. 170(2). 305–309. 185 indexed citations
20.
Duine, Johannis A., Johannes Frank, & J. A. Jongejan. (1983). Detection and determination of pyrroloquinoline quinone, the coenzyme of quinoproteins. Analytical Biochemistry. 133(1). 239–243. 44 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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