Jaap J. Beintema

5.9k total citations
143 papers, 4.7k citations indexed

About

Jaap J. Beintema is a scholar working on Molecular Biology, Surgery and Immunology. According to data from OpenAlex, Jaap J. Beintema has authored 143 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 108 papers in Molecular Biology, 31 papers in Surgery and 28 papers in Immunology. Recurrent topics in Jaap J. Beintema's work include RNA and protein synthesis mechanisms (32 papers), Pancreatic function and diabetes (31 papers) and Protein Structure and Dynamics (28 papers). Jaap J. Beintema is often cited by papers focused on RNA and protein synthesis mechanisms (32 papers), Pancreatic function and diabetes (31 papers) and Protein Structure and Dynamics (28 papers). Jaap J. Beintema collaborates with scholars based in Netherlands, United States and Indonesia. Jaap J. Beintema's co-authors include Peter A. Jekel, Wim Gaastra, Jan Hofsteenge, J.M. Vereijken, Anke C. Terwisscha van Scheltinga, Bauke W. Dijkstra, Wicher J. Weijer, Nell M. Soeter, Henk J. Bak and Masachika IRIE and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Jaap J. Beintema

142 papers receiving 4.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jaap J. Beintema Netherlands	36	3.1k	885	658	493	489	143	4.7k
Jerry L. Hedrick United States	41	3.1k 1.0×	434 0.5×	422 0.6×	479 1.0×	774 1.6×	115	6.5k
Teni Boulikas United States	36	4.8k 1.5×	519 0.6×	586 0.9×	344 0.7×	870 1.8×	77	7.7k
Fumio Sakiyama Japan	38	3.8k 1.2×	1.5k 1.7×	1.3k 1.9×	294 0.6×	571 1.2×	140	6.7k
Wei‐Chiang Shen United States	43	4.5k 1.4×	612 0.7×	791 1.2×	225 0.5×	535 1.1×	131	6.8k
Daniel Thomas France	44	3.4k 1.1×	398 0.4×	720 1.1×	207 0.4×	453 0.9×	162	5.5k
Byung‐Ha Oh South Korea	44	4.4k 1.4×	1.3k 1.5×	607 0.9×	478 1.0×	583 1.2×	98	7.1k
Roger A. Laine United States	42	3.3k 1.0×	582 0.7×	1.1k 1.6×	305 0.6×	646 1.3×	168	6.0k
N. Martin Young Canada	47	4.3k 1.4×	949 1.1×	445 0.7×	374 0.8×	354 0.7×	142	6.3k
Andrew A. Gooley Australia	39	4.4k 1.4×	639 0.7×	436 0.7×	207 0.4×	388 0.8×	111	6.7k
Brigitte Wittmann‐Liebold Germany	44	6.3k 2.0×	755 0.9×	425 0.6×	525 1.1×	1.3k 2.6×	171	7.8k

Countries citing papers authored by Jaap J. Beintema

Since Specialization

Citations

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

Fields of papers citing papers by Jaap J. Beintema

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jaap J. Beintema

This figure shows the co-authorship network connecting the top 25 collaborators of Jaap J. Beintema. A scholar is included among the top collaborators of Jaap J. Beintema 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 Jaap J. Beintema. Jaap J. Beintema 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

Cho, Soochin, Jaap J. Beintema, & Jianzhi Zhang. (2004). The ribonuclease A superfamily of mammals and birds: identifying new members and tracing evolutionary histories. Genomics. 85(2). 208–220. 147 indexed citations

Arif, Siti Arija M., Robert G. Hamilton, Faridah Yusof, et al.. (2004). Isolation and Characterization of the Early Nodule-specific Protein Homologue (Hev b 13), an Allergenic Lipolytic Esterase from Hevea brasiliensis Latex. Journal of Biological Chemistry. 279(23). 23933–23941. 50 indexed citations

Jekel, Peter A., Jan Hofsteenge, & Jaap J. Beintema. (2003). The patatin-like protein from the latex of Hevea brasiliensis (Hev b 7) is not a vacuolar protein. Phytochemistry. 63(5). 517–522. 7 indexed citations

Bokma, Evert, et al.. (1997). Hevamine, a chitinase from the rubber tree Hevea brasiliensis, cleaves peptidoglycan between the C‐1 of N‐acetylglucosamine and C‐4 of N‐acetylmuramic acid and therefore is not a lysozyme. FEBS Letters. 411(2-3). 161–163. 28 indexed citations

Siebert, Hans‐Christian, Claus‐Wilhelm von der Lieth, Robert Kaptein, et al.. (1997). Role of aromatic amino acids in carbohydrate binding of plant lectins: Laser photo chemically induced dynamic nuclear polarization study of hevein domain-containing lectins. Proteins Structure Function and Bioinformatics. 28(2). 268–284. 43 indexed citations

Subroto, Toto, et al.. (1995). Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis). FEBS Letters. 363(3). 211–213. 30 indexed citations

Perton, Frank G., et al.. (1995). Short Communication. Biological Chemistry Hoppe-Seyler. 376(4). 243–258. 5 indexed citations

Okorokov, Andrei L., Kostya I. Panov, Robert te Poele, et al.. (1995). An Efficient System for Active Bovine Pancreatic Ribonuclease Expression in Escherichia coli. Protein Expression and Purification. 6(4). 472–480. 10 indexed citations

Jekel, Peter A., et al.. (1992). Primary structure of hemocyanin subunit c from Panulirus interruptus. European Journal of Biochemistry. 206(1). 243–249. 37 indexed citations

10.

Rozeboom, H.J., et al.. (1990). Crystallization of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. Journal of Molecular Biology. 212(3). 441–443. 23 indexed citations

11.

Dokter, Wim H.A., et al.. (1989). Partial amino acid sequence of a hemocyanin subunit from Palinurus vulgaris. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 94(3). 593–597. 7 indexed citations

12.

IRIE, Masachika, Kazuko Ohgi, Hideaki Watanabe, et al.. (1988). Primary Structure of a Non-Secretory Ribonuclease from Bovine Kidney1. The Journal of Biochemistry. 104(2). 289–296. 40 indexed citations

13.

Jekel, Peter A., Henk J. Bak, Nell M. Soeter, J.M. Vereijken, & Jaap J. Beintema. (1988). Panulirus interruptus hemocyanin. European Journal of Biochemistry. 178(2). 403–412. 42 indexed citations

14.

Schmid, F., et al.. (1986). Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.. Proceedings of the National Academy of Sciences. 83(4). 872–876. 71 indexed citations

15.

Beintema, Jaap J. & J.M. van der Laan. (1986). Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases. FEBS Letters. 194(2). 338–346. 11 indexed citations

16.

Linzen, Bernt, Nell M. Soeter, Austen Riggs, et al.. (1985). The Structure of Arthropod Hemocyanins. Science. 229(4713). 519–524. 211 indexed citations

17.

Gaykema, W. P. J., Wim G. J. Hol, J.M. Vereijken, et al.. (1984). 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature. 309(5963). 23–29. 256 indexed citations

18.

Welling, Gjalt W., Johannes A. Lenstra, & Jaap J. Beintema. (1976). Activity and antigenicity of ribonuclease hybrids. FEBS Letters. 63(1). 89–94. 5 indexed citations

19.

Beintema, Jaap J., et al.. (1976). Carbohydrate in Pancreatic Ribonucleases. European Journal of Biochemistry. 63(2). 441–448. 62 indexed citations

20.

Wierenga, Rik K., J D Huizinga, Wim Gaastra, G. W. Welling, & Jaap J. Beintema. (1973). Affinity chromatography of porcine pancreatic ribonuclease reinvestigation of the N‐terminal amino acid sequence. FEBS Letters. 31(2). 181–185. 73 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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