Sofia Karlström

987 total citations
9 papers, 698 citations indexed

About

Sofia Karlström is a scholar working on Organic Chemistry, Pharmacology and Computational Theory and Mathematics. According to data from OpenAlex, Sofia Karlström has authored 9 papers receiving a total of 698 indexed citations (citations by other indexed papers that have themselves been cited), including 3 papers in Organic Chemistry, 3 papers in Pharmacology and 3 papers in Computational Theory and Mathematics. Recurrent topics in Sofia Karlström's work include Catalytic Cross-Coupling Reactions (3 papers), Alzheimer's disease research and treatments (3 papers) and Computational Drug Discovery Methods (3 papers). Sofia Karlström is often cited by papers focused on Catalytic Cross-Coupling Reactions (3 papers), Alzheimer's disease research and treatments (3 papers) and Computational Drug Discovery Methods (3 papers). Sofia Karlström collaborates with scholars based in Sweden, Spain and United Kingdom. Sofia Karlström's co-authors include Carmén Nájera, Juan Gil‐Moltó, Larry R. Falvello, Karin Kolmodin, Fredrik Jeppsson, Juliette Janson, Britt‐Marie Swahn, Susanna Eketjäll, Johanna Fälting and Stefan von Berg and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Neuroscience and Cancer Research.

In The Last Decade

Sofia Karlström

9 papers receiving 688 citations

Peers

Sofia Karlström
Jong‐Min Suh South Korea
Alexander M. Porte United States
Paul Oakley United Kingdom
J.B.H. Warneck United Kingdom
Daniel S. La United States
G. Marconi Germany
Jong‐Min Suh South Korea
Sofia Karlström
Citations per year, relative to Sofia Karlström Sofia Karlström (= 1×) peers Jong‐Min Suh

Countries citing papers authored by Sofia Karlström

Since Specialization
Citations

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

Fields of papers citing papers by Sofia Karlström

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sofia Karlström

This figure shows the co-authorship network connecting the top 25 collaborators of Sofia Karlström. A scholar is included among the top collaborators of Sofia Karlström 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 Sofia Karlström. Sofia Karlström is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

9 of 9 papers shown
1.
Engström, Olof, Oscar Belda, Mikaela Rapp, et al.. (2020). Discovery of USP7 small-molecule allosteric inhibitors. Bioorganic & Medicinal Chemistry Letters. 30(20). 127471–127471. 10 indexed citations
2.
Öberg, Fredrik, Sofia Karlström, Ian Henderson, et al.. (2016). Abstract 3011: Development of selective small-molecule inhibitors of cellular MALT1 protease activity. Cancer Research. 76(14_Supplement). 3011–3011. 2 indexed citations
3.
Eklund, Göran, Jonas Malmquist, Britt‐Marie Swahn, et al.. (2013). Biotransformation of Two β-Secretase Inhibitors Including Ring Opening and Contraction of a Pyrimidine Ring. Drug Metabolism and Disposition. 41(5). 1134–1147. 4 indexed citations
4.
Eketjäll, Susanna, Juliette Janson, Fredrik Jeppsson, et al.. (2013). AZ-4217: A High Potency BACE Inhibitor Displaying Acute Central Efficacy in Different In Vivo Models and Reduced Amyloid Deposition in Tg2576 Mice. Journal of Neuroscience. 33(24). 10075–10084. 34 indexed citations
5.
Jeppsson, Fredrik, Susanna Eketjäll, Juliette Janson, et al.. (2012). Discovery of AZD3839, a Potent and Selective BACE1 Inhibitor Clinical Candidate for the Treatment of Alzheimer Disease. Journal of Biological Chemistry. 287(49). 41245–41257. 107 indexed citations
6.
Gravenfors, Ylva, Jenny Viklund, Sofia Karlström, et al.. (2012). New Aminoimidazoles as β-Secretase (BACE-1) Inhibitors Showing Amyloid-β (Aβ) Lowering in Brain. Journal of Medicinal Chemistry. 55(21). 9297–9311. 56 indexed citations
7.
Gil‐Moltó, Juan, Sofia Karlström, & Carmén Nájera. (2005). Di(2-pyridyl)methylamine–palladium dichloride complex covalently anchored to a styrene-maleic anhydride co-polymer as recoverable catalyst for C–C cross-coupling reactions in water. Tetrahedron. 61(51). 12168–12176. 112 indexed citations
8.
Nájera, Carmén, Juan Gil‐Moltó, & Sofia Karlström. (2004). Suzuki–Miyaura and Related Cross‐Couplings in Aqueous Solvents Catalyzed by Di(2‐pyridyl)methylamine‐Palladium Dichloride Complexes. Advanced Synthesis & Catalysis. 346(13-15). 1798–1811. 118 indexed citations
9.
Nájera, Carmén, Juan Gil‐Moltó, Sofia Karlström, & Larry R. Falvello. (2003). Di-2-pyridylmethylamine-Based Palladium Complexes as New Catalysts for Heck, Suzuki, and Sonogashira Reactions in Organic and Aqueous Solvents. Organic Letters. 5(9). 1451–1454. 255 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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