C. Johansson

3.6k total citations
33 papers, 2.4k citations indexed

About

C. Johansson is a scholar working on Molecular Biology, Biochemistry and Nutrition and Dietetics. According to data from OpenAlex, C. Johansson has authored 33 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 6 papers in Biochemistry and 4 papers in Nutrition and Dietetics. Recurrent topics in C. Johansson's work include Redox biology and oxidative stress (12 papers), Epigenetics and DNA Methylation (9 papers) and Cancer-related gene regulation (8 papers). C. Johansson is often cited by papers focused on Redox biology and oxidative stress (12 papers), Epigenetics and DNA Methylation (9 papers) and Cancer-related gene regulation (8 papers). C. Johansson collaborates with scholars based in United Kingdom, Sweden and United States. C. Johansson's co-authors include Arne Holmgren, Christopher Horst Lillig, Carsten Berndt, Maria Lönn, Christoph Hudemann, Udo Oppermann, K.L. Kavanagh, O. Gileadi, C. Gileadi and Johanna Ljung and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

C. Johansson

33 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
C. Johansson United Kingdom 22 1.8k 347 319 206 167 33 2.4k
Christoph Hudemann Germany 16 1.4k 0.7× 285 0.8× 279 0.9× 133 0.6× 86 0.5× 31 2.0k
Alexios Vlamis‐Gardikas Sweden 23 1.3k 0.7× 235 0.7× 246 0.8× 181 0.9× 76 0.5× 45 1.7k
Qing Cheng Sweden 26 1.4k 0.8× 492 1.4× 442 1.4× 109 0.5× 157 0.9× 58 2.1k
W. Todd Lowther United States 34 2.7k 1.5× 649 1.9× 236 0.7× 137 0.7× 353 2.1× 63 3.7k
José Antonio Bárcena Spain 25 1.3k 0.7× 330 1.0× 151 0.5× 66 0.3× 122 0.7× 61 1.8k
Rajib Sengupta India 20 980 0.5× 315 0.9× 148 0.5× 89 0.4× 50 0.3× 49 1.5k
Anand Bachhawat India 27 1.7k 0.9× 531 1.5× 189 0.6× 26 0.1× 106 0.6× 86 2.5k
Ho Hee Jang South Korea 25 2.0k 1.1× 206 0.6× 217 0.7× 59 0.3× 150 0.9× 52 2.5k
Jason G. McCoy United States 23 1.1k 0.6× 140 0.4× 82 0.3× 211 1.0× 72 0.4× 41 1.6k
A Delaunay France 22 1.8k 1.0× 238 0.7× 215 0.7× 47 0.2× 39 0.2× 40 2.4k

Countries citing papers authored by C. Johansson

Since Specialization
Citations

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

Fields of papers citing papers by C. Johansson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C. Johansson

This figure shows the co-authorship network connecting the top 25 collaborators of C. Johansson. A scholar is included among the top collaborators of C. Johansson 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 C. Johansson. C. Johansson 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.
Salah, E., C. Johansson, Elisabete Pires, et al.. (2024). JmjC catalysed histone H2a N-methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships. Communications Biology. 7(1). 1583–1583. 3 indexed citations
2.
Xiong, Yan, Holger Greschik, C. Johansson, et al.. (2024). Discovery of a Potent, Selective, and Cell-Active SPIN1 Inhibitor. Journal of Medicinal Chemistry. 67(7). 5837–5853. 2 indexed citations
3.
Salah, E., et al.. (2023). The catalytic domains of all human KDM5 JmjC demethylases catalyse N‐methyl arginine demethylation. FEBS Letters. 597(7). 933–946. 8 indexed citations
4.
Payne, N. Connor, C. Johansson, Sofia A. Santos, et al.. (2022). Elucidating the path to Plasmodium prolyl-tRNA synthetase inhibitors that overcome halofuginone resistance. Nature Communications. 13(1). 4976–4976. 16 indexed citations
5.
Cottone, Lucia, Adam P. Cribbs, Garima Khandelwal, et al.. (2020). Inhibition of Histone H3K27 Demethylases Inactivates Brachyury (TBXT) and Promotes Chordoma Cell Death. Cancer Research. 80(20). 4540–4551. 35 indexed citations
6.
Yang, Shyh‐Ming, Natalia J. Martinez, Adam Yasgar, et al.. (2018). Discovery of Orally Bioavailable, Quinoline-Based Aldehyde Dehydrogenase 1A1 (ALDH1A1) Inhibitors with Potent Cellular Activity. Journal of Medicinal Chemistry. 61(11). 4883–4903. 70 indexed citations
7.
Kumar, Kiran, Bas J. G. E. Pieters, Anthony Tumber, et al.. (2017). Investigatingd-lysine stereochemistry for epigenetic methylation, demethylation and recognition. Chemical Communications. 53(99). 13264–13267. 26 indexed citations
8.
Tarhonskaya, Hanna, Radosław P. Nowak, C. Johansson, et al.. (2017). Studies on the Interaction of the Histone Demethylase KDM5B with Tricarboxylic Acid Cycle Intermediates. Journal of Molecular Biology. 429(19). 2895–2906. 36 indexed citations
9.
Nowak, Radosław P., Anthony Tumber, C. Johansson, et al.. (2016). Advances and challenges in understanding histone demethylase biology. Current Opinion in Chemical Biology. 33. 151–159. 24 indexed citations
10.
Walport, Louise J., Richard J. Hopkinson, M. Vollmar, et al.. (2014). Human UTY(KDM6C) Is a Male-specific Nϵ-Methyl Lysyl Demethylase. Journal of Biological Chemistry. 289(26). 18302–18313. 155 indexed citations
11.
Bräutigam, Lars, C. Johansson, M.A. McDonough, et al.. (2013). An unusual mode of iron–sulfur-cluster coordination in a teleost glutaredoxin. Biochemical and Biophysical Research Communications. 436(3). 491–496. 14 indexed citations
12.
Soundararajan, M., A.P. Turnbull, O. Fedorov, C. Johansson, & D. Doyle. (2008). RhoB can adopt a Mg2+ free conformation prior to GEF binding. Proteins Structure Function and Bioinformatics. 72(1). 498–505. 9 indexed citations
13.
Gileadi, O., N. Burgess-Brown, G. Berridge, et al.. (2008). High Throughput Production of Recombinant Human Proteins for Crystallography. Methods in molecular biology. 426. 221–246. 77 indexed citations
14.
Elgán, Tobias H., et al.. (2007). Redox properties and evolution of human glutaredoxins. Proteins Structure Function and Bioinformatics. 68(4). 879–892. 46 indexed citations
15.
Hashemy, Seyed Isaac, C. Johansson, Carsten Berndt, Christopher Horst Lillig, & Arne Holmgren. (2007). Oxidation and S-Nitrosylation of Cysteines in Human Cytosolic and Mitochondrial Glutaredoxins. Journal of Biological Chemistry. 282(19). 14428–14436. 84 indexed citations
16.
Porat, Amir, Christopher Horst Lillig, C. Johansson, et al.. (2007). The Reducing Activity of Glutaredoxin 3 toward Cytoplasmic Substrate Proteins Is Restricted by Methionine 43. Biochemistry. 46(11). 3366–3377. 14 indexed citations
17.
Johansson, C., Arne Holmgren, Carsten Berndt, et al.. (2005). Thiol redox control via thioredoxin and glutaredoxin systems. Biochemical Society Transactions. 33(6). 1375–1375. 320 indexed citations
18.
Johansson, C., Christopher Horst Lillig, & Arne Holmgren. (2004). Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase. Journal of Biological Chemistry. 279(9). 7537–7543. 249 indexed citations
19.
Porras, Pablo, José Rafael Pedrajas, Emilia Martínez‐Galisteo, et al.. (2002). Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency. Biochemical and Biophysical Research Communications. 295(5). 1046–1051. 46 indexed citations
20.
Lundberg, M., C. Johansson, Joya Chandra, et al.. (2001). Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear Isoforms. Journal of Biological Chemistry. 276(28). 26269–26275. 276 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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