Mirva J. Saaranen

1.1k total citations
20 papers, 763 citations indexed

About

Mirva J. Saaranen is a scholar working on Molecular Biology, Cell Biology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Mirva J. Saaranen has authored 20 papers receiving a total of 763 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 14 papers in Cell Biology and 3 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Mirva J. Saaranen's work include Endoplasmic Reticulum Stress and Disease (14 papers), Protein purification and stability (4 papers) and Redox biology and oxidative stress (4 papers). Mirva J. Saaranen is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (14 papers), Protein purification and stability (4 papers) and Redox biology and oxidative stress (4 papers). Mirva J. Saaranen collaborates with scholars based in Finland, United Kingdom and Austria. Mirva J. Saaranen's co-authors include Lloyd W. Ruddock, Anna‐Riikka Karala, Anna–Kaisa Lappi, Kirsi E.H. Salo, Heli I. Alanen, Van Dat Nguyen, Lei Wang, Chih-chen Wang, Irina Raykhel and Sohvi Hörkkö and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Scientific Reports.

In The Last Decade

Mirva J. Saaranen

20 papers receiving 758 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mirva J. Saaranen Finland 12 488 362 98 78 73 20 763
Yoichiro Harada Japan 21 789 1.6× 280 0.8× 237 2.4× 55 0.7× 31 0.4× 48 1.0k
Scott K. Wooden United States 13 613 1.3× 427 1.2× 112 1.1× 58 0.7× 64 0.9× 15 844
Marcel van Lith United Kingdom 15 417 0.9× 371 1.0× 310 3.2× 42 0.5× 30 0.4× 24 897
Sabina Coppari Italy 8 410 0.8× 403 1.1× 118 1.2× 51 0.7× 10 0.1× 8 724
Valérie Le Fourn Switzerland 14 399 0.8× 113 0.3× 65 0.7× 49 0.6× 73 1.0× 18 564
Gloria N. Sando United States 9 446 0.9× 198 0.5× 60 0.6× 43 0.6× 31 0.4× 9 732
Rupert L. Mayer Austria 17 393 0.8× 109 0.3× 72 0.7× 45 0.6× 43 0.6× 29 684
Darina L. Lazarova United States 19 860 1.8× 342 0.9× 37 0.4× 24 0.3× 12 0.2× 24 1.2k
John W. Newell Switzerland 7 481 1.0× 138 0.4× 245 2.5× 35 0.4× 18 0.2× 8 835

Countries citing papers authored by Mirva J. Saaranen

Since Specialization
Citations

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

Fields of papers citing papers by Mirva J. Saaranen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mirva J. Saaranen. 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 Mirva J. Saaranen. The network helps show where Mirva J. Saaranen may publish in the future.

Co-authorship network of co-authors of Mirva J. Saaranen

This figure shows the co-authorship network connecting the top 25 collaborators of Mirva J. Saaranen. A scholar is included among the top collaborators of Mirva J. Saaranen 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 Mirva J. Saaranen. Mirva J. Saaranen 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.
Biedendieck, Rebekka, et al.. (2025). Toward Antibody Production in Genome-Minimized Bacillus subtilis Strains. ACS Synthetic Biology. 14(3). 740–755. 3 indexed citations
2.
Saaranen, Mirva J., et al.. (2024). Komagataella phaffii Erp41 is a protein disulfide isomerase with unprecedented disulfide bond catalyzing activity when coupled to glutathione. Journal of Biological Chemistry. 300(3). 105746–105746. 1 indexed citations
3.
Saaranen, Mirva J., et al.. (2024). Escherichia coli Cytoplasmic Expression of Disulfide-Bonded Proteins: Side-by-Side Comparison between Two Competing Strategies. Journal of Microbiology and Biotechnology. 34(5). 1126–1134. 3 indexed citations
4.
Saaranen, Mirva J., et al.. (2023). Highly efficient export of a disulfide‐bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli. MicrobiologyOpen. 12(2). e1350–e1350. 7 indexed citations
5.
Saaranen, Mirva J., et al.. (2023). Cytoplasmic production of Fabs in chemically defined media in fed-batch fermentation. Protein Expression and Purification. 215. 106404–106404. 3 indexed citations
6.
Saaranen, Mirva J., et al.. (2023). Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast. Scientific Reports. 13(1). 14298–14298. 2 indexed citations
7.
Saaranen, Mirva J., Heli I. Alanen, Kirsi E.H. Salo, et al.. (2022). Introduction of a More Glutaredoxin-like Active Site to PDI Results in Competition between Protein Substrate and Glutathione Binding. Antioxidants. 11(10). 1920–1920. 4 indexed citations
8.
Sowa, Sven T., et al.. (2021). High-resolution Crystal Structure of Human pERp1, A Saposin-like Protein Involved in IgA, IgM and Integrin Maturation in the Endoplasmic Reticulum. Journal of Molecular Biology. 433(5). 166826–166826. 10 indexed citations
9.
Khadka, Prakash, et al.. (2020). Production of Extracellular Matrix Proteins in the Cytoplasm of E. coli: Making Giants in Tiny Factories. International Journal of Molecular Sciences. 21(3). 688–688. 14 indexed citations
10.
Saaranen, Mirva J. & Lloyd W. Ruddock. (2019). Applications of catalyzed cytoplasmic disulfide bond formation. Biochemical Society Transactions. 47(5). 1223–1231. 14 indexed citations
11.
Saaranen, Mirva J., et al.. (2018). Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding. Life Science Alliance. 1(3). e201800090–e201800090. 27 indexed citations
12.
Biterova, Ekaterina, et al.. (2018). Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease. Scientific Reports. 8(1). 6752–6752. 43 indexed citations
13.
14.
Veijola, Johanna, et al.. (2016). Systematic screening of soluble expression of antibody fragments in the cytoplasm of E. coli. Microbial Cell Factories. 15(1). 22–22. 84 indexed citations
15.
Saaranen, Mirva J. & Lloyd W. Ruddock. (2012). Disulfide Bond Formation in the Cytoplasm. Antioxidants and Redox Signaling. 19(1). 46–53. 28 indexed citations
16.
Nguyen, Van Dat, Mirva J. Saaranen, Anna‐Riikka Karala, et al.. (2011). Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation. Journal of Molecular Biology. 406(3). 503–515. 217 indexed citations
17.
Saaranen, Mirva J., et al.. (2009). The C-Terminal Active Site Cysteine of Escherichia coli Glutaredoxin 1 Determines the Glutathione Specificity of the Second Step of Peptide Deglutathionylation. Antioxidants and Redox Signaling. 11(8). 1819–1828. 20 indexed citations
18.
Saaranen, Mirva J., Anna‐Riikka Karala, Anna–Kaisa Lappi, & Lloyd W. Ruddock. (2009). The Role of Dehydroascorbate in Disulfide Bond Formation. Antioxidants and Redox Signaling. 12(1). 15–25. 52 indexed citations
19.
Nguyen, Van Dat, Mark J. Howard, Antti M. Haapalainen, et al.. (2008). Alternative Conformations of the x Region of Human Protein Disulphide-Isomerase Modulate Exposure of the Substrate Binding b’ Domain. Journal of Molecular Biology. 383(5). 1144–1155. 89 indexed citations
20.
Karala, Anna‐Riikka, Anna–Kaisa Lappi, Mirva J. Saaranen, & Lloyd W. Ruddock. (2008). Efficient Peroxide-Mediated Oxidative Refolding of a Protein at Physiological pH and Implications for Oxidative Folding in the Endoplasmic Reticulum. Antioxidants and Redox Signaling. 11(5). 963–970. 73 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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