Jos Buijs

3.5k total citations
66 papers, 2.8k citations indexed

About

Jos Buijs is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Spectroscopy. According to data from OpenAlex, Jos Buijs has authored 66 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 25 papers in Radiology, Nuclear Medicine and Imaging and 14 papers in Spectroscopy. Recurrent topics in Jos Buijs's work include Monoclonal and Polyclonal Antibodies Research (23 papers), Mass Spectrometry Techniques and Applications (12 papers) and Radiopharmaceutical Chemistry and Applications (10 papers). Jos Buijs is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (23 papers), Mass Spectrometry Techniques and Applications (12 papers) and Radiopharmaceutical Chemistry and Applications (10 papers). Jos Buijs collaborates with scholars based in Sweden, Netherlands and United Kingdom. Jos Buijs's co-authors include Vladimir Hlady, Willem Norde, J. W. Th. Lichtenbelt, Sven Oscarsson, J. Lyklema, Christopher T. Elliott, Mark Mooney, P. Håkansson, Chen Situ and Herbert P. Jennissen and has published in prestigious journals such as Nucleic Acids Research, PLoS ONE and Journal of Applied Physics.

In The Last Decade

Jos Buijs

64 papers receiving 2.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jos Buijs Sweden 31 1.4k 919 557 542 324 66 2.8k
Lin Yan China 27 1.5k 1.1× 1.1k 1.2× 315 0.6× 845 1.6× 68 0.2× 105 4.1k
Charles M. Roth United States 28 1.5k 1.1× 1.1k 1.2× 177 0.3× 168 0.3× 156 0.5× 74 3.0k
Chi Wu Hong Kong 44 1.9k 1.4× 924 1.0× 118 0.2× 637 1.2× 234 0.7× 164 6.4k
D. D. Lasič Slovenia 21 2.5k 1.9× 906 1.0× 330 0.6× 348 0.6× 190 0.6× 38 4.5k
Ronald C. Chatelier Australia 27 560 0.4× 616 0.7× 164 0.3× 953 1.8× 143 0.4× 54 2.3k
Raphaël Lévy United Kingdom 30 1.6k 1.2× 974 1.1× 241 0.4× 121 0.2× 103 0.3× 69 3.7k
Giuseppe Spoto Italy 34 1.7k 1.3× 1.3k 1.4× 124 0.2× 110 0.2× 222 0.7× 110 3.7k
Dietmar Appelhans Germany 42 2.6k 1.9× 1.3k 1.4× 130 0.2× 866 1.6× 234 0.7× 263 6.0k
Mina Okochi Japan 29 1.3k 1.0× 1.2k 1.3× 164 0.3× 92 0.2× 131 0.4× 144 2.9k
Mitsuo Umetsu Japan 33 1.9k 1.4× 1.1k 1.2× 724 1.3× 54 0.1× 163 0.5× 155 4.1k

Countries citing papers authored by Jos Buijs

Since Specialization
Citations

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

Fields of papers citing papers by Jos Buijs

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jos Buijs

This figure shows the co-authorship network connecting the top 25 collaborators of Jos Buijs. A scholar is included among the top collaborators of Jos Buijs 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 Jos Buijs. Jos Buijs 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.
Cerofolini, Linda, W. Kaiser, Wim Vranken, et al.. (2025). Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications. Nucleic Acids Research. 53(15). 1 indexed citations
2.
Morrison, Jamie I., Nermina Babić, Nicole G. Metzendorf, et al.. (2024). A shorter linker in the bispecific antibody RmAb158-scFv8D3 improves TfR-mediated blood-brain barrier transcytosis in vitro. Scientific Reports. 14(1). 30613–30613. 6 indexed citations
4.
Encarnação, João Crispim, U. Helena Danielson, Grzegorz Dubin, et al.. (2020). A real‐time cell‐binding assay reveals dynamic features of STxB–Gb3 cointernalization and STxB‐mediated cargo delivery into cancer cells. FEBS Letters. 594(15). 2406–2420. 2 indexed citations
5.
Nordling, Sofia, Johan Brännström, Fredrik Carlsson, et al.. (2018). Enhanced protection of the renal vascular endothelium improves early outcome in kidney transplantation: Preclinical investigations in pig and mouse. Scientific Reports. 8(1). 5220–5220. 19 indexed citations
6.
Honarvar, Hadis, Enrica Calce, Nunzianna Doti, et al.. (2018). Evaluation of HER2-specific peptide ligand for its employment as radiolabeled imaging probe. Scientific Reports. 8(1). 2998–2998. 25 indexed citations
7.
Björkelund, Hanna, et al.. (2017). Novel Real-Time Proximity Assay for Characterizing Multiple Receptor Interactions on Living Cells. Analytical Chemistry. 89(24). 13212–13218. 6 indexed citations
8.
Garousi, Javad, Karl Andersson, Johan Hygum Dam, et al.. (2017). The use of radiocobalt as a label improves imaging of EGFR using DOTA-conjugated Affibody molecule. Scientific Reports. 7(1). 5961–5961. 30 indexed citations
9.
Brooks, Jonathan, et al.. (2017). Real-time Characterization of Antibody Binding to Receptors on Living Immune Cells. Frontiers in Immunology. 8. 455–455. 45 indexed citations
10.
Yakes, Betsy Jean, Jos Buijs, Christopher T. Elliott, & Katrina Campbell. (2016). Surface plasmon resonance biosensing: Approaches for screening and characterising antibodies for food diagnostics. Talanta. 156-157. 55–63. 34 indexed citations
11.
Garousi, Javad, Kenrick F. Anderson, Johan Hygum Dam, et al.. (2015). The use of radiocobalt as a label improves PET imaging of EGFR using DOTA-conjugated affibody molecules. European Journal of Nuclear Medicine and Molecular Imaging. 42. 1 indexed citations
12.
Garousi, Javad, Sarah Lindbo, Johan Nilvebrant, et al.. (2015). ADAPT, a Novel Scaffold Protein-Based Probe for Radionuclide Imaging of Molecular Targets That Are Expressed in Disseminated Cancers. Cancer Research. 75(20). 4364–4371. 53 indexed citations
13.
Garousi, Javad, Sarah Lindbo, Anna Orlova, et al.. (2014). Development of ADAPT6 as a new scaffold protein for radionuclide molecular imaging. European Journal of Nuclear Medicine and Molecular Imaging. 41.
14.
Wang, Ellen, Hanna Björkelund, Urs B. Hagemann, et al.. (2014). Automated functional characterization of radiolabeled antibodies. Nuclear Medicine Communications. 35(7). 767–776. 8 indexed citations
15.
Campbell, Katrina, Terry McGrath, Östen Jansson, et al.. (2010). Use of a novel micro-fluidic device to create arrays for multiplex analysis of large and small molecular weight compounds by surface plasmon resonance. Biosensors and Bioelectronics. 26(6). 3029–3036. 37 indexed citations
16.
Oscarsson, Sven, et al.. (2005). Structure, stability, and orientation of BSA adsorbed to silica. Journal of Colloid and Interface Science. 289(1). 26–35. 112 indexed citations
17.
Buijs, Jos. (2005). SPR-MS in functional proteomics. Briefings in Functional Genomics and Proteomics. 4(1). 39–47. 42 indexed citations
18.
Buijs, Jos, et al.. (2003). Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry. Journal of Colloid and Interface Science. 263(2). 441–448. 39 indexed citations
19.
Oscarsson, Sven, et al.. (2001). Thermodynamic Analysis of Proteins Adsorbed on Silica Particles: Electrostatic Effects. Journal of Colloid and Interface Science. 237(1). 98–103. 95 indexed citations
20.
Hlady, Vladimir, Jos Buijs, & Herbert P. Jennissen. (1999). [26] Methods for studying protein adsorption. Methods in enzymology on CD-ROM/Methods in enzymology. 309. 402–429. 98 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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