Inger Sandlie

7.3k total citations · 1 hit paper
131 papers, 5.5k citations indexed

About

Inger Sandlie is a scholar working on Radiology, Nuclear Medicine and Imaging, Molecular Biology and Immunology. According to data from OpenAlex, Inger Sandlie has authored 131 papers receiving a total of 5.5k indexed citations (citations by other indexed papers that have themselves been cited), including 100 papers in Radiology, Nuclear Medicine and Imaging, 74 papers in Molecular Biology and 61 papers in Immunology. Recurrent topics in Inger Sandlie's work include Monoclonal and Polyclonal Antibodies Research (100 papers), Glycosylation and Glycoproteins Research (48 papers) and T-cell and B-cell Immunology (31 papers). Inger Sandlie is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (100 papers), Glycosylation and Glycoproteins Research (48 papers) and T-cell and B-cell Immunology (31 papers). Inger Sandlie collaborates with scholars based in Norway, United States and United Kingdom. Inger Sandlie's co-authors include Jan Terje Andersen, Ole Henrik Brekke, Terje E. Michaelsen, Kine Marita Knudsen Sand, Bjarne Bogen, Malin Bern, Jeannette Nilsen, Geir Åge Løset, Stian Foss and Richard S. Blumberg and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Inger Sandlie

131 papers receiving 5.3k citations

Hit Papers

align trajectories sort by overperformance

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.

The Neonatal Fc Receptor (FcRn): A Misnomer?

2019 297 citations Michał Pyzik, Kine Marita Knudsen Sand et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Inger Sandlie	2.9k	2.9k	2.1k	649	476	131	5.5k
Jan Terje Andersen	2.3k 0.8×	2.5k 0.9×	1.5k 0.7×	605 0.9×	441 0.9×	102	4.7k
Janine Schuurman	3.2k 1.1×	2.4k 0.8×	2.6k 1.2×	1.4k 2.1×	560 1.2×	98	6.9k
Jeanette H.W. Leusen	1.7k 0.6×	1.8k 0.6×	3.0k 1.4×	893 1.4×	434 0.9×	144	5.1k
Shreeram Akilesh	1.9k 0.6×	2.0k 0.7×	1.8k 0.8×	552 0.9×	449 0.9×	72	4.8k
Pierre Bruhns	2.6k 0.9×	2.1k 0.7×	4.3k 2.0×	729 1.1×	452 0.9×	81	6.8k
Thomas Kieber‐Emmons	1.5k 0.5×	2.6k 0.9×	1.5k 0.7×	568 0.9×	506 1.1×	175	4.6k
Mark D. Hulett	1.0k 0.3×	4.8k 1.7×	2.2k 1.1×	533 0.8×	502 1.1×	127	7.6k
Jean‐Luc Teillaud	2.2k 0.7×	2.0k 0.7×	2.8k 1.3×	1.5k 2.2×	396 0.8×	164	5.7k
Hans H. Wandall	994 0.3×	5.0k 1.7×	2.0k 1.0×	633 1.0×	395 0.8×	125	6.7k
Hannah J. Gould	2.7k 0.9×	3.6k 1.3×	4.5k 2.1×	550 0.8×	224 0.5×	215	11.0k

Countries citing papers authored by Inger Sandlie

Since Specialization

Citations

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

Fields of papers citing papers by Inger Sandlie

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Inger Sandlie

This figure shows the co-authorship network connecting the top 25 collaborators of Inger Sandlie. A scholar is included among the top collaborators of Inger Sandlie 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 Inger Sandlie. Inger Sandlie 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

Foss, Stian, J.H. Marco Jansen, Mitchell Evers, et al.. (2025). Engineering of anticancer human immunoglobulin A equipped with albumin for enhanced plasma half-life. PNAS Nexus. 4(2). pgaf042–pgaf042. 3 indexed citations

Gjølberg, Torleif Tollefsrud, et al.. (2025). Targeting the Neonatal Fc Receptor in Autoimmune Diseases: Pipeline and Progress. BioDrugs. 39(3). 373–409. 3 indexed citations

Kolderup, Anette, Marina Vaysburd, Donna L. Mallery, et al.. (2023). A pan-SARS-CoV-2-specific soluble angiotensin-converting enzyme 2-albumin fusion engineered for enhanced plasma half-life and needle-free mucosal delivery. PNAS Nexus. 2(12). pgad403–pgad403. 5 indexed citations

Foss, Stian, Maria Bottermann, Ruth Watkinson, et al.. (2022). Potent TRIM21 and complement-dependent intracellular antiviral immunity requires the IgG3 hinge. Science Immunology. 7(70). eabj1640–eabj1640. 20 indexed citations

Gjølberg, Torleif Tollefsrud, Rahel Frick, Stian Foss, et al.. (2022). Biophysical differences in IgG1 Fc-based therapeutics relate to their cellular handling, interaction with FcRn and plasma half-life. Communications Biology. 5(1). 832–832. 14 indexed citations

Sand, Kine Marita Knudsen, Michael Gruber, Inger Sandlie, et al.. (2022). Contribution of the ex vivo placental perfusion model in understanding transplacental immunoglobulin G transfer. Placenta. 127. 77–87. 4 indexed citations

Frick, Rahel, Lene S. Høydahl, Jan Petersen, et al.. (2021). A high-affinity human TCR-like antibody detects celiac disease gluten peptide–MHC complexes and inhibits T cell activation. Science Immunology. 6(62). 18 indexed citations

Hubbard, Jonathan J., Michał Pyzik, Timo Räth, et al.. (2020). FcRn is a CD32a coreceptor that determines susceptibility to IgG immune complex–driven autoimmunity. The Journal of Experimental Medicine. 217(10). 34 indexed citations

Høydahl, Lene S., Lisa Richter, Rahel Frick, et al.. (2018). Plasma Cells Are the Most Abundant Gluten Peptide MHC-expressing Cells in Inflamed Intestinal Tissues From Patients With Celiac Disease. Gastroenterology. 156(5). 1428–1439.e10. 61 indexed citations

10.

Gunnarsen, Kristin Støen, Lene S. Høydahl, Louise F. Risnes, et al.. (2017). A TCRα framework–centered codon shapes a biased T cell repertoire through direct MHC and CDR3β interactions. JCI Insight. 2(17). 12 indexed citations

11.

Foss, Stian, Ruth Watkinson, Algirdas Grevys, et al.. (2016). TRIM21 Immune Signaling Is More Sensitive to Antibody Affinity Than Its Neutralization Activity. The Journal of Immunology. 196(8). 3452–3459. 34 indexed citations

12.

Foss, Stian, Algirdas Grevys, Kine Marita Knudsen Sand, et al.. (2015). Enhanced FcRn-dependent transepithelial delivery of IgG by Fc-engineering and polymerization. Journal of Controlled Release. 223. 42–52. 23 indexed citations

13.

Andersen, Jan Terje, María González-Pajuelo, Stian Foss, et al.. (2013). Selection of Nanobodies that Target Human Neonatal Fc Receptor. Scientific Reports. 3(1). 1118–1118. 8 indexed citations

14.

Yazaki, Paul J., Divya Channappa, Chi Wai Cheung, et al.. (2012). A series of anti-CEA/anti-DOTA bispecific antibody formats evaluated for pre-targeting: comparison of tumor uptake and blood clearance. Protein Engineering Design and Selection. 26(3). 187–193. 29 indexed citations

15.

Jung, Sang Taek, William Kelton, Tae Hyun Kang, et al.. (2012). Effective Phagocytosis of Low Her2 Tumor Cell Lines with Engineered, Aglycosylated IgG Displaying High FcγRIIa Affinity and Selectivity. ACS Chemical Biology. 8(2). 368–375. 59 indexed citations

16.

Baker, Kristi, Shuo‐Wang Qiao, Timothy Kuo, et al.. (2011). Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8 ⁻ CD11b ⁺ dendritic cells. Proceedings of the National Academy of Sciences. 108(24). 9927–9932. 175 indexed citations

17.

Ghumra, Ashfaq, Jean‐Philippe Semblat, Richard S. McIntosh, et al.. (2008). Identification of Residues in the Cμ4 Domain of Polymeric IgM Essential for Interaction with Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1). The Journal of Immunology. 181(3). 1988–2000. 53 indexed citations

18.

Schjetne, Karoline W., et al.. (2005). Induction of central T cell tolerance: Recombinant antibodies deliver peptides for deletion of antigen-specific CD4+8+ thymocytes. European Journal of Immunology. 35(11). 3142–3152. 5 indexed citations

19.

Løset, Geir Åge, Kenneth H. Roux, Ping Zhu, Terje E. Michaelsen, & Inger Sandlie. (2004). Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor. The Journal of Immunology. 172(5). 2925–2934. 40 indexed citations

20.

Inés, Concepción de, et al.. (2001). Recombinant chimeric OKT3 scFv IgM antibodies mediate immune suppression while reducing T cell activationin vitro. European Journal of Immunology. 31(1). 94–106. 12 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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