John Löfblom

4.0k total citations · 1 hit paper
110 papers, 3.1k citations indexed

About

John Löfblom is a scholar working on Radiology, Nuclear Medicine and Imaging, Molecular Biology and Oncology. According to data from OpenAlex, John Löfblom has authored 110 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 94 papers in Radiology, Nuclear Medicine and Imaging, 68 papers in Molecular Biology and 29 papers in Oncology. Recurrent topics in John Löfblom's work include Monoclonal and Polyclonal Antibodies Research (92 papers), Glycosylation and Glycoproteins Research (45 papers) and HER2/EGFR in Cancer Research (24 papers). John Löfblom is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (92 papers), Glycosylation and Glycoproteins Research (45 papers) and HER2/EGFR in Cancer Research (24 papers). John Löfblom collaborates with scholars based in Sweden, Russia and United States. John Löfblom's co-authors include Stefan Ståhl, Fredrik Y. Frejd, Vladimir Tolmachev, Shalom Stahl, Joachim Feldwisch, J. Carlsson, Anna Orlova, Karl Andersson, Mathias Uhlén and Nina Kronqvist and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

John Löfblom

105 papers receiving 3.1k citations

Hit Papers

Affibody molecules: Engineered proteins for therapeutic, ... 2010 2026 2015 2020 2010 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John Löfblom Sweden 29 2.1k 1.9k 872 322 264 110 3.1k
Changshou Gao United States 29 1.6k 0.7× 1.7k 0.9× 885 1.0× 220 0.7× 422 1.6× 67 2.9k
Benjamin J. Hackel United States 29 1.3k 0.6× 1.8k 1.0× 540 0.6× 122 0.4× 403 1.5× 98 2.8k
Rob C. Roovers Netherlands 32 2.5k 1.1× 2.6k 1.4× 1.0k 1.2× 250 0.8× 1.1k 4.1× 49 4.2k
Joachim Feldwisch Sweden 29 2.2k 1.0× 1.5k 0.8× 1.2k 1.4× 114 0.4× 229 0.9× 66 3.3k
Susan L. Deutscher United States 30 1.4k 0.7× 2.2k 1.1× 594 0.7× 259 0.8× 866 3.3× 83 3.6k
Amin Hajitou United Kingdom 29 482 0.2× 1.7k 0.9× 663 0.8× 408 1.3× 261 1.0× 64 3.0k
Patrick Chames France 34 2.0k 0.9× 2.5k 1.3× 1.2k 1.4× 151 0.5× 1.3k 5.1× 91 4.3k
Herren Wu United States 40 3.0k 1.4× 3.0k 1.6× 1.3k 1.5× 126 0.4× 1.3k 5.1× 115 5.8k
Jagath R. Junutula United States 33 1.3k 0.6× 1.9k 1.0× 1.1k 1.3× 106 0.3× 336 1.3× 53 3.6k
Patrick Amstutz Switzerland 20 1.7k 0.8× 2.4k 1.3× 465 0.5× 243 0.8× 423 1.6× 23 3.2k

Countries citing papers authored by John Löfblom

Since Specialization
Citations

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

Fields of papers citing papers by John Löfblom

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John Löfblom

This figure shows the co-authorship network connecting the top 25 collaborators of John Löfblom. A scholar is included among the top collaborators of John Löfblom 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 John Löfblom. John Löfblom 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.
Odell, Luke R., et al.. (2024). Optimized method for fluorine-18 radiolabeling of Affibody molecules using RESCA. EJNMMI Radiopharmacy and Chemistry. 9(1). 73–73. 2 indexed citations
2.
Zhang, Jie, Sara S. Rinne, E. Bjorklund, et al.. (2024). Affibody-Drug Conjugates Targeting the Human Epidermal Growth Factor Receptor-3 Demonstrate Therapeutic Efficacy in Mice Bearing Low Expressing Xenografts. ACS Pharmacology & Translational Science. 7(10). 3228–3240. 2 indexed citations
3.
Mushtaq, Ameeq Ul, et al.. (2024). Cooperative folding as a molecular switch in an evolved antibody binder. Journal of Biological Chemistry. 300(11). 107795–107795. 2 indexed citations
4.
Zhang, Bo, Johanna Rokka, Maria� Rosestedt, et al.. (2023). Imaging of fibrogenesis in the liver by [18F]TZ-Z09591, an Affibody molecule targeting platelet derived growth factor receptor β. EJNMMI Radiopharmacy and Chemistry. 8(1). 23–23. 10 indexed citations
5.
Hulsart‐Billström, Gry, Bogdan Mitran, Bo Zhang, et al.. (2023). Noninvasive PET Detection of CD69-Positive Immune Cells Before Signs of Clinical Disease in Inflammatory Arthritis. Journal of Nuclear Medicine. 65(2). 294–299. 2 indexed citations
6.
Ståhl, Stefan, et al.. (2023). Engineering of Affibody Molecules. Cold Spring Harbor Protocols. 2024(11). pdb.top107760–pdb.top107760. 3 indexed citations
7.
Hedhammar, My, et al.. (2023). In vitro Blood–Brain barrier model based on recombinant spider silk protein nanomembranes for evaluation of transcytosis capability of biomolecules. Biochemical and Biophysical Research Communications. 669. 77–84. 3 indexed citations
8.
Lindberg, Hanna, et al.. (2023). Construction and Validation of a New Naïve Sequestrin Library for Directed Evolution of Binders against Aggregation-Prone Peptides. International Journal of Molecular Sciences. 24(1). 836–836. 1 indexed citations
9.
Ståhl, Stefan, et al.. (2023). Bacterial Cell Display for Selection of Affibody Molecules. Methods in molecular biology. 2681. 99–112. 2 indexed citations
10.
Rinne, Sara S., Ayman Abouzayed, Anzhelika Vorobyeva, et al.. (2022). Targeting Tumor Cells Overexpressing the Human Epidermal Growth Factor Receptor 3 with Potent Drug Conjugates Based on Affibody Molecules. Biomedicines. 10(6). 1293–1293. 5 indexed citations
11.
Hedhammar, My, et al.. (2019). VEGFR2-Specific Ligands Based on Affibody Molecules Demonstrate Agonistic Effects when Tetrameric in the Soluble Form or Immobilized via Spider Silk. ACS Biomaterials Science & Engineering. 5(12). 6474–6484. 5 indexed citations
12.
Löfblom, John, Ralf Rosenstein, Minh‐Thu Nguyen, Stefan Ståhl, & Friedrich Götz. (2017). Staphylococcus carnosus: from starter culture to protein engineering platform. Applied Microbiology and Biotechnology. 101(23-24). 8293–8307. 42 indexed citations
13.
Malm, Magdalena, Fredrik Y. Frejd, Stefan Ståhl, & John Löfblom. (2016). Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds. mAbs. 8(7). 1195–1209. 39 indexed citations
14.
Lindborg, Malin, Ingmarie Höidén‐Guthenberg, Heiko Bönisch, et al.. (2014). An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein. Proceedings of the National Academy of Sciences. 111(48). 17110–17115. 43 indexed citations
15.
Andersson, Karl, Zohreh Varasteh, Maria� Rosestedt, et al.. (2014). 111In-labeled NOTA-conjugated Affibody molecules for visualization of HER3 expression in malignant tumors. European Journal of Nuclear Medicine and Molecular Imaging. 41. 1 indexed citations
16.
Altai, Mohamed, Helena Wållberg, Hadis Honarvar, et al.. (2014). 188Re-ZHER2:V2, a Promising Affibody-Based Targeting Agent Against HER2-Expressing Tumors: Preclinical Assessment. Journal of Nuclear Medicine. 55(11). 1842–1848. 23 indexed citations
17.
Nilvebrant, Johan, et al.. (2014). Engineering of Bispecific Affinity Proteins with High Affinity for ERBB2 and Adaptable Binding to Albumin. PLoS ONE. 9(8). e103094–e103094. 50 indexed citations
18.
Jonsson, Andreas, et al.. (2014). A new prodrug form of Affibody molecules (pro-Affibody) is selectively activated by cancer-associated proteases. Cellular and Molecular Life Sciences. 72(7). 1405–1415. 21 indexed citations
19.
Orlova, Anna, Magdalena Malm, Hanna Lindberg, et al.. (2013). Feasibility of radionuclide imaging of HER3-expressing tumours using technetium-99m labeled affibody molecules. European Journal of Nuclear Medicine and Molecular Imaging. 40.
20.
Forsström, Björn, et al.. (2012). Parallel Immunizations of Rabbits Using the Same Antigen Yield Antibodies with Similar, but Not Identical, Epitopes. PLoS ONE. 7(12). e45817–e45817. 15 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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