H. Berglund

5.7k total citations · 1 hit paper
39 papers, 4.3k citations indexed

About

H. Berglund is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, H. Berglund has authored 39 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 11 papers in Materials Chemistry and 7 papers in Genetics. Recurrent topics in H. Berglund's work include Enzyme Structure and Function (9 papers), Protein purification and stability (7 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). H. Berglund is often cited by papers focused on Enzyme Structure and Function (9 papers), Protein purification and stability (7 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). H. Berglund collaborates with scholars based in Sweden, Canada and United Kingdom. H. Berglund's co-authors include Masoud Vedadi, F. Niesen, Torleif Härd, Susanne van den Berg, M. Hammarstrom, Per‐Åke Löfdahl, Esmeralda Woestenenk, P. Nordlund, Johan Weigelt and Abdellah Allali‐Hassani and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

H. Berglund

39 papers receiving 4.2k 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.

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

2007 1.9k citations F. Niesen, H. Berglund et al. Nature Protocols profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
H. Berglund Sweden	23	3.2k	659	469	458	373	39	4.3k
Jim Warwicker United Kingdom	37	4.1k 1.3×	797 1.2×	587 1.3×	297 0.6×	343 0.9×	125	5.2k
François Stricher Spain	25	4.0k 1.3×	600 0.9×	429 0.9×	746 1.6×	227 0.6×	32	4.9k
Lanette Fee United States	10	2.9k 0.9×	717 1.1×	244 0.5×	330 0.7×	372 1.0×	12	4.0k
B.M. Hallberg Sweden	32	3.2k 1.0×	444 0.7×	425 0.9×	374 0.8×	188 0.5×	63	4.6k
Milton T. Stubbs Germany	41	3.4k 1.1×	511 0.8×	216 0.5×	468 1.0×	607 1.6×	117	5.6k
David E. Anderson United States	23	2.5k 0.8×	729 1.1×	210 0.4×	530 1.2×	221 0.6×	43	3.4k
Stephen V. Evans Canada	31	2.9k 0.9×	470 0.7×	518 1.1×	301 0.7×	190 0.5×	106	4.4k
Stanley C. Gill United States	19	5.8k 1.8×	832 1.3×	519 1.1×	833 1.8×	458 1.2×	40	7.2k
Se Won Suh South Korea	40	4.2k 1.3×	906 1.4×	187 0.4×	496 1.1×	320 0.9×	196	5.7k
Boguslaw Stec United States	38	3.1k 1.0×	903 1.4×	347 0.7×	284 0.6×	304 0.8×	106	5.3k

Countries citing papers authored by H. Berglund

Since Specialization

Citations

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

Fields of papers citing papers by H. Berglund

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of H. Berglund

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

Berglund, H., Lova Segerström, Matthias Walle, et al.. (2023). Selection, characterization and in vivo evaluation of novel CD44v6-targeting antibodies for targeted molecular radiotherapy. Scientific Reports. 13(1). 20648–20648. 3 indexed citations

Swarbrick, Crystall M. D., Nathan Cowieson, Edward I. Patterson, et al.. (2014). Structural Basis for Regulation of the Human Acetyl-CoA Thioesterase 12 and Interactions with the Steroidogenic Acute Regulatory Protein-related Lipid Transfer (START) Domain. Journal of Biological Chemistry. 289(35). 24263–24274. 22 indexed citations

Tresaugues, L., S. Flodin, M. Welin, et al.. (2014). Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases. Structure. 22(5). 744–755. 40 indexed citations

Siponen, M.I., M. Wisniewska, L. Lehtiö, et al.. (2010). Structural Determination of Functional Domains in Early B-cell Factor (EBF) Family of Transcription Factors Reveals Similarities to Rel DNA-binding Proteins and a Novel Dimerization Motif. Journal of Biological Chemistry. 285(34). 25875–25879. 22 indexed citations

Berglund, H., Johannes Järemo, & Göran Bengtsson. (2009). Endemism Predicts Intrinsic Vulnerability to Nonindigenous Species on Islands. The American Naturalist. 174(1). 94–101. 32 indexed citations

Gräslund, S., H. Berglund, Alex F. C. Flores, et al.. (2007). The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins. Protein Expression and Purification. 58(2). 210–221. 94 indexed citations

Berglund, H., et al.. (2007). A general, robust method for the quality control of intact proteins using LC–ESI-MS. Journal of Chromatography B. 852(1-2). 188–194. 51 indexed citations

Niesen, F., H. Berglund, & Masoud Vedadi. (2007). The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nature Protocols. 2(9). 2212–2221. 1893 indexed citations breakdown →

Vedadi, Masoud, F. Niesen, Abdellah Allali‐Hassani, et al.. (2006). Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proceedings of the National Academy of Sciences. 103(43). 15835–15840. 471 indexed citations

10.

Hammarstrom, M., et al.. (2006). Effect of N-terminal solubility enhancing fusion proteins on yield of purified target protein. Journal of Structural and Functional Genomics. 7(1). 1–14. 69 indexed citations

11.

Woestenenk, Esmeralda, M. Hammarstrom, Susanne van den Berg, Torleif Härd, & H. Berglund. (2004). His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. Journal of Structural and Functional Genomics. 5(3). 217–229. 149 indexed citations

12.

Hammarstrom, M., et al.. (2002). Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Science. 11(2). 313–321. 271 indexed citations

13.

Woestenenk, Esmeralda, G. M. Gongadze, Dmitry Shcherbakov, et al.. (2002). The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold. Biochemical Journal. 363(3). 553–553. 14 indexed citations

14.

Berglund, H., et al.. (2000). The three-dimensional solution structure and dynamic properties of the human FADD death domain 1 1Edited by A. Fersht. Journal of Molecular Biology. 302(1). 171–188. 84 indexed citations

15.

Berglund, H., et al.. (1999). Conformational Dynamics and Molecular Recognition: Backbone Dynamics of the Estrogen Receptor DNA-binding Domain. Journal of Molecular Biology. 289(4). 963–979. 29 indexed citations

16.

Enroth, Helena, et al.. (1999). ¹³C-urea breath test results in pigs challenged withHelicobacter pylorior other urease producing bacteria. FEMS Immunology & Medical Microbiology. 23(3). 253–257. 1 indexed citations

17.

Sun, Licheng, Leif Hammarström, Thomas Norrby, et al.. (1997). Intramolecular electron transfer from coordinated manganese(ii) to photogenerated ruthenium(iii). Chemical Communications. 607–608. 34 indexed citations

18.

Styring, Stenbjörn, Licheng Sun, Leif Hammarström, et al.. (1997). Towards artificial photosynthesis — Light-induced intramolecular electron transfer from manganese (II) to ruthenium (III) in a binuclear complex. Journal of Chemical Sciences. 109(6). 389–396. 2 indexed citations

19.

Baumann, Herbert, Helena Kovacs, H. Berglund, et al.. (1993). Refined solution structure of the glucocorticoid receptor DNA-binding domain. Biochemistry. 32(49). 13463–13471. 73 indexed citations

20.

Patel, Naina, H. Berglund, Lennart Nilsson, et al.. (1992). Thermodynamics of interaction of a fluorescent DNA oligomer with the anti‐tumour drug netropsin. European Journal of Biochemistry. 203(3). 361–366. 20 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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