Johanna Deinum

2.8k total citations
76 papers, 2.4k citations indexed

About

Johanna Deinum is a scholar working on Molecular Biology, Hematology and Cancer Research. According to data from OpenAlex, Johanna Deinum has authored 76 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 26 papers in Hematology and 19 papers in Cancer Research. Recurrent topics in Johanna Deinum's work include Blood Coagulation and Thrombosis Mechanisms (26 papers), Protease and Inhibitor Mechanisms (19 papers) and Microtubule and mitosis dynamics (12 papers). Johanna Deinum is often cited by papers focused on Blood Coagulation and Thrombosis Mechanisms (26 papers), Protease and Inhibitor Mechanisms (19 papers) and Microtubule and mitosis dynamics (12 papers). Johanna Deinum collaborates with scholars based in Sweden, Australia and United States. Johanna Deinum's co-authors include Margareta Wallin, Margareta Elg, David Gustafsson, Petter Björquist, Erika Gyzander, Tord Inghardt, Beryl Hartley‐Asp, Christer Mattsson, Carin Briving and Jacques Baudier and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Experimental Medicine and PLoS ONE.

In The Last Decade

Johanna Deinum

76 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
Johanna Deinum Sweden 29 1.1k 582 534 343 343 76 2.4k
David R. Light United States 31 1.4k 1.2× 751 1.3× 220 0.4× 275 0.8× 145 0.4× 84 3.0k
Mamoru Shoji United States 30 1.8k 1.7× 377 0.6× 360 0.7× 100 0.3× 137 0.4× 63 3.0k
Sidney D. Lewis United States 31 1.2k 1.1× 733 1.3× 233 0.4× 131 0.4× 141 0.4× 71 2.5k
Joseph D. Shore United States 36 1.6k 1.4× 1.7k 3.0× 1.7k 3.2× 185 0.5× 935 2.7× 81 4.0k
Michael Dockal Austria 24 1.1k 1.0× 796 1.4× 72 0.1× 93 0.3× 188 0.5× 64 2.5k
D P Via United States 25 1.4k 1.2× 159 0.3× 612 1.1× 335 1.0× 261 0.8× 46 3.2k
Andrew M. Stern United States 32 1.6k 1.4× 258 0.4× 359 0.7× 78 0.2× 212 0.6× 89 3.3k
Małgorzata Czyż Poland 32 2.0k 1.8× 121 0.2× 697 1.3× 155 0.5× 334 1.0× 112 3.2k
Richard Hill United States 28 1.3k 1.2× 326 0.6× 436 0.8× 72 0.2× 155 0.5× 48 2.6k
Cody J. Peer United States 33 1.8k 1.6× 172 0.3× 351 0.7× 288 0.8× 70 0.2× 156 4.0k

Countries citing papers authored by Johanna Deinum

Since Specialization
Citations

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

Fields of papers citing papers by Johanna Deinum

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Johanna Deinum

This figure shows the co-authorship network connecting the top 25 collaborators of Johanna Deinum. A scholar is included among the top collaborators of Johanna Deinum 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 Johanna Deinum. Johanna Deinum 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.
Lindgren, A., Johanna Deinum, Göran Bergström, et al.. (2017). Fibrinolysis inhibitors in plaque stability: a morphological association of PAI‐1 and TAFI in advanced carotid plaque. Journal of Thrombosis and Haemostasis. 15(4). 758–769. 13 indexed citations
2.
Lövgren, Ann, et al.. (2015). Characterization of thrombin derived from human recombinant prothrombin. Blood Coagulation & Fibrinolysis. 26(5). 545–555. 3 indexed citations
3.
Hansson, Kenny M., Søren B. Nielsen, Margareta Elg, & Johanna Deinum. (2014). The effect of corn trypsin inhibitor and inhibiting antibodies for FXIa and FXIIa on coagulation of plasma and whole blood. Journal of Thrombosis and Haemostasis. 12(10). 1678–1686. 33 indexed citations
4.
Hansson, Kenny M., Jenny Björkqvist, & Johanna Deinum. (2014). Addition of prothrombin to plasma can result in a paradoxical increase in activated partial thromboplastin time. Blood Coagulation & Fibrinolysis. 25(8). 851–855. 5 indexed citations
5.
Geschwindner, Stefan, et al.. (2013). Identification of Structural–Kinetic and Structural–Thermodynamic Relationships for Thrombin Inhibitors. Biochemistry. 52(4). 613–626. 22 indexed citations
6.
Bucha, Elke, et al.. (2012). Expression and Characterization of Recombinant Ecarin. The Protein Journal. 31(5). 353–358. 12 indexed citations
7.
Fjellström, Ola, Johanna Deinum, Tove Sjögren, et al.. (2012). Characterization of a Small Molecule Inhibitor of Plasminogen Activator Inhibitor Type 1 That Accelerates the Transition into the Latent Conformation. Journal of Biological Chemistry. 288(2). 873–885. 26 indexed citations
8.
Deinum, Johanna, et al.. (2011). Monitoring of Protein Conformational Changes Upon Interaction with Low Molecular Weight Compounds by QCM-D and its Application to Drug Discovery. Biophysical Journal. 100(3). 375a–375a. 1 indexed citations
9.
Deinum, Johanna, et al.. (2010). Viscoelastic Sensing of Conformational Changes in Plasminogen Induced upon Binding of Low Molecular Weight Compounds. Analytical Chemistry. 82(20). 8374–8376. 13 indexed citations
10.
Brogren, Helén, Carina Sihlbom, Malin Lönn, et al.. (2008). Heterogeneous glycosylation patterns of human PAI-1 may reveal its cellular origin. Thrombosis Research. 122(2). 271–281. 37 indexed citations
11.
Svedhem, Sofia, et al.. (2008). A Novel Surface Modification Using Tissue Factor Reconstituted in Phospholipid Vesicles for the Activation of Blood Coagulation. Journal of Biomaterials Science Polymer Edition. 20(1). 133–140. 1 indexed citations
12.
Buchanan, Malcolm S., Anthony R. Carroll, Michael F. Jobling, et al.. (2008). Clavatadine A, A Natural Product with Selective Recognition and Irreversible Inhibition of Factor XIa. Journal of Medicinal Chemistry. 51(12). 3583–3587. 60 indexed citations
13.
Karlsson, Robert, Markku Hämäläinen, Karl Andersson, et al.. (2001). Biosensor Analysis of Drug–Target Interactions: Direct and Competitive Binding Assays for Investigation of Interactions between Thrombin and Thrombin Inhibitors. Analytical Biochemistry. 291(2). 306–306. 1 indexed citations
14.
Björquist, Petter, et al.. (1997). Epitopes on plasminogen activator inhibitor type-1 important for binding to tissue plasminogen activator. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1341(1). 87–98. 23 indexed citations
15.
Elg, Margareta, David Gustafsson, & Johanna Deinum. (1997). The Importance of Enzyme Inhibition Kinetics for the Effect of Thrombin Inhibitors in a Rat Model of Arterial Thrombosis. Thrombosis and Haemostasis. 78(4). 1286–1292. 102 indexed citations
16.
Strömqvist, Mats, et al.. (1996). Characterisation of the complex of plasminogen activator inhibitor type 1 with tissue-type plasminogen activator by mass spectrometry and size-exclusion chromatography. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1295(1). 103–109. 18 indexed citations
17.
Nilsson, Ingemar, et al.. (1990). Cis-trans isomerization of an angiotensin I-converting enzyme inhibitor. An enzyme kinetic and nuclear magnetic resonance study. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1041(1). 22–30. 12 indexed citations
18.
Wallin, Margareta, et al.. (1988). Effects of proteolysis of the extending parts of the high-molecular-weight microtubule-associated proteins on interactions between microtubules. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 955(2). 135–142. 11 indexed citations
19.
Wallin, Margareta, et al.. (1986). Changes in the hydrodynamic properties of microtubules induced by taxol. Biochimica et Biophysica Acta (BBA) - General Subjects. 880(2-3). 189–196. 20 indexed citations
20.
Deinum, Johanna, Jacques Baudier, Carin Briving, et al.. (1983). The effect of S‐100a and S‐100b proteins and Zn2+ on the assembly of brain microtubule proteins in vitro. FEBS Letters. 163(2). 287–291. 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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