Eric G. Huizinga

5.3k total citations · 1 hit paper
57 papers, 4.0k citations indexed

About

Eric G. Huizinga is a scholar working on Hematology, Molecular Biology and Immunology. According to data from OpenAlex, Eric G. Huizinga has authored 57 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Hematology, 20 papers in Molecular Biology and 16 papers in Immunology. Recurrent topics in Eric G. Huizinga's work include Platelet Disorders and Treatments (24 papers), Cell Adhesion Molecules Research (11 papers) and Complement system in diseases (10 papers). Eric G. Huizinga is often cited by papers focused on Platelet Disorders and Treatments (24 papers), Cell Adhesion Molecules Research (11 papers) and Complement system in diseases (10 papers). Eric G. Huizinga collaborates with scholars based in Netherlands, United States and United Kingdom. Eric G. Huizinga's co-authors include Piet Gros, Jan J. Sixma, Roland A. Romijn, Philip G. de Groot, Raoul J. de Groot, Marion E. Schiphorst, T. Harma C. Brondijk, Martijn A. Langereis, Shizuko Tsuji and Anja Roos and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Eric G. Huizinga

56 papers receiving 4.0k 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.

Human coronaviruses OC43 and HKU1 bind to 9- O -acetylated sialic acids via a conserved receptor-binding site in spike protein domain A

2019 276 citations Yifei Lang, Wentao Li et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Eric G. Huizinga Netherlands	33	1.3k	1.3k	1.1k	699	368	57	4.0k
Hisami Ikeda Japan	38	971 0.7×	1.8k 1.4×	1.6k 1.4×	681 1.0×	282 0.8×	170	5.9k
Ricardo A. Feldman United States	34	517 0.4×	2.1k 1.7×	847 0.8×	395 0.6×	154 0.4×	87	4.8k
Dominique Blanchard France	38	1.5k 1.1×	1.9k 1.6×	3.2k 2.8×	269 0.4×	295 0.8×	151	6.6k
Toni Antalis United States	40	876 0.7×	2.5k 2.0×	838 0.8×	387 0.6×	576 1.6×	91	5.7k
Christoph Driessen Switzerland	45	1.4k 1.1×	2.9k 2.3×	1.5k 1.3×	234 0.3×	218 0.6×	144	5.8k
Penelope E. Stein United Kingdom	27	893 0.7×	2.2k 1.7×	424 0.4×	238 0.3×	220 0.6×	48	4.5k
Hans‐Martin Jäck Germany	43	458 0.3×	2.7k 2.1×	2.3k 2.0×	1.7k 2.4×	112 0.3×	154	6.5k
Pablo Fuentes‐Prior Spain	37	780 0.6×	2.5k 2.0×	1.1k 1.0×	355 0.5×	157 0.4×	77	5.0k
Virgil L. Woods United States	50	451 0.3×	3.7k 2.9×	542 0.5×	646 0.9×	441 1.2×	121	6.5k
Nicole M. Thielens France	47	1.1k 0.9×	1.5k 1.2×	4.2k 3.8×	535 0.8×	169 0.5×	182	6.2k

Countries citing papers authored by Eric G. Huizinga

Since Specialization

Citations

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

Fields of papers citing papers by Eric G. Huizinga

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eric G. Huizinga. 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 Eric G. Huizinga. The network helps show where Eric G. Huizinga may publish in the future.

Co-authorship network of co-authors of Eric G. Huizinga

This figure shows the co-authorship network connecting the top 25 collaborators of Eric G. Huizinga. A scholar is included among the top collaborators of Eric G. Huizinga 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 Eric G. Huizinga. Eric G. Huizinga 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

Brondijk, T. Harma C., et al.. (2022). Structural insights into collagen binding by platelet receptor glycoprotein VI. Blood. 139(20). 3087–3098. 28 indexed citations

Lang, Yifei, Wentao Li, Zeshi Li, et al.. (2020). Coronavirus hemagglutinin-esterase and spike proteins coevolve for functional balance and optimal virion avidity. Proceedings of the National Academy of Sciences. 117(41). 25759–25770. 57 indexed citations

Huizinga, Eric G., et al.. (2019). Structure and flexibility of the extracellular region of the PirB receptor. Journal of Biological Chemistry. 294(12). 4634–4643. 5 indexed citations

Jakobi, Arjen J. & Eric G. Huizinga. (2012). A Rapid Cloning Method Employing Orthogonal End Protection. PLoS ONE. 7(6). e37617–e37617. 4 indexed citations

Jakobi, Arjen J., Alireza Mashaghi, Sander J. Tans, & Eric G. Huizinga. (2011). Calcium modulates force sensing by the von Willebrand factor A2 domain. Nature Communications. 2(1). 385–385. 76 indexed citations

Langereis, Martijn A., Qinghong Zeng, Gerrit J. Gerwig, et al.. (2009). Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases. Proceedings of the National Academy of Sciences. 106(37). 15897–15902. 40 indexed citations

Wijk, Richard van, et al.. (2008). Fifteen novel mutations inPKLRassociated with pyruvate kinase (PK) deficiency: Structural implications of amino acid substitutions in PK. Human Mutation. 30(3). 446–453. 24 indexed citations

Milder, Fin J., H.C.A. Raaijmakers, Arie Schouten, et al.. (2006). Structure of Complement Component C2a: Implications for Convertase Formation and Substrate Binding. Structure. 14(10). 1587–1597. 35 indexed citations

Staelens, Steven, Michael A. Hadders, S Vauterin, et al.. (2005). Paratope Determination of the Antithrombotic Antibody 82D6A3 Based on the Crystal Structure of Its Complex with the von Willebrand Factor A3-Domain. Journal of Biological Chemistry. 281(4). 2225–2231. 24 indexed citations

10.

Janssen, B.J.C., Eric G. Huizinga, H.C.A. Raaijmakers, et al.. (2005). Structures of complement component C3 provide insights into the function and evolution of immunity. Nature. 437(7058). 505–511. 418 indexed citations

11.

Lenting, Peter J., Erik Westein, Virginie Terraube, et al.. (2004). An Experimental Model to Study the in Vivo Survival of von Willebrand Factor. Journal of Biological Chemistry. 279(13). 12102–12109. 123 indexed citations

12.

Huizinga, Eric G., et al.. (2003). . Japanese Journal of Thrombosis and Hemostasis. 14(2). 101–106.

13.

Wijk, Roelof Van, Eric G. Huizinga, Wijnanda A. Kors, et al.. (2003). Distinct phenotypic expression of two de novo missense mutations affecting the dimer interface of glucose-6-phosphate dehydrogenase. Blood Cells Molecules and Diseases. 32(1). 112–117. 14 indexed citations

14.

Vanhoorelbeke, Karen, Hans Ulrichts, Roland A. Romijn, Eric G. Huizinga, & Hans Deckmyn. (2003). The GPIbα–thrombin interaction: far from crystal clear. Trends in Molecular Medicine. 10(1). 33–39. 22 indexed citations

15.

Vanhoorelbeke, Karen, Hilde Depraetere, Roland A. Romijn, et al.. (2003). A Consensus Tetrapeptide Selected by Phage Display Adopts the Conformation of a Dominant Discontinuous Epitope of a Monoclonal Anti-VWF Antibody That Inhibits the von Willebrand Factor-Collagen Interaction. Journal of Biological Chemistry. 278(39). 37815–37821. 36 indexed citations

16.

Oubrie, Arthur, H.J. Rozeboom, Kor H. Kalk, Eric G. Huizinga, & Bauke W. Dijkstra. (2002). Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni. Journal of Biological Chemistry. 277(5). 3727–3732. 70 indexed citations

17.

Oubrie, Arthur, Eric G. Huizinga, H.J. Rozeboom, et al.. (2001). Crystallization of quinohaemoprotein alcohol dehydrogenase fromComamonas testosteroni: crystals with unique optical properties. Acta Crystallographica Section D Biological Crystallography. 57(11). 1732–1734. 1 indexed citations

18.

Huizinga, Eric G., Arie Schouten, Thomas Connolly, et al.. (2001). The structure of leech anti-platelet protein, an inhibitor of haemostasis. Acta Crystallographica Section D Biological Crystallography. 57(8). 1071–1078. 12 indexed citations

19.

Romijn, Roland A., Barend Bouma, Piet Gros, et al.. (2001). Identification of the Collagen-binding Site of the von Willebrand Factor A3-domain. Journal of Biological Chemistry. 276(13). 9985–9991. 78 indexed citations

20.

Chen, Ling, R. C. E. Durley, Barbara Poliks, et al.. (1992). Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin. Biochemistry. 31(21). 4959–4964. 128 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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