Vesna de Serrano

693 total citations
23 papers, 578 citations indexed

About

Vesna de Serrano is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Vesna de Serrano has authored 23 papers receiving a total of 578 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 18 papers in Cell Biology and 5 papers in Physiology. Recurrent topics in Vesna de Serrano's work include Hemoglobin structure and function (18 papers), Heme Oxygenase-1 and Carbon Monoxide (16 papers) and Porphyrin Metabolism and Disorders (5 papers). Vesna de Serrano is often cited by papers focused on Hemoglobin structure and function (18 papers), Heme Oxygenase-1 and Carbon Monoxide (16 papers) and Porphyrin Metabolism and Disorders (5 papers). Vesna de Serrano collaborates with scholars based in United States, Italy and Nepal. Vesna de Serrano's co-authors include Stefan Franzen, Reza A. Ghiladi, M.F. Davis, Carla Mattos, Junjie Zhao, Lirong Chen, Aimin Liu, Fange Liu, Rong Fu and Greg Buhrman and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Physical Chemistry B and Biochemistry.

In The Last Decade

Vesna de Serrano

23 papers receiving 568 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vesna de Serrano United States 15 445 344 142 59 51 23 578
Laurence A. Fishel United States 10 577 1.3× 222 0.6× 122 0.9× 26 0.4× 73 1.4× 12 908
Latesh Lad United States 17 776 1.7× 467 1.4× 102 0.7× 23 0.4× 60 1.2× 26 1.0k
K S Eble United States 12 400 0.9× 110 0.3× 227 1.6× 47 0.8× 134 2.6× 15 717
Phillip S. Brereton United States 13 222 0.5× 62 0.2× 87 0.6× 25 0.4× 84 1.6× 21 572
Terry Mincey United States 9 270 0.6× 129 0.4× 74 0.5× 52 0.9× 100 2.0× 10 450
M. Soltis United States 11 315 0.7× 81 0.2× 24 0.2× 44 0.7× 71 1.4× 16 557
Jing Du United States 12 273 0.6× 212 0.6× 83 0.6× 40 0.7× 39 0.8× 17 431
William N. Poillon United States 15 212 0.5× 232 0.7× 24 0.2× 142 2.4× 31 0.6× 25 633
Zongxiang Xia China 8 524 1.2× 66 0.2× 152 1.1× 9 0.2× 107 2.1× 11 613
Nicholas D. Lanz United States 13 453 1.0× 50 0.1× 186 1.3× 10 0.2× 95 1.9× 16 806

Countries citing papers authored by Vesna de Serrano

Since Specialization
Citations

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

Fields of papers citing papers by Vesna de Serrano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Vesna de Serrano. 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 Vesna de Serrano. The network helps show where Vesna de Serrano may publish in the future.

Co-authorship network of co-authors of Vesna de Serrano

This figure shows the co-authorship network connecting the top 25 collaborators of Vesna de Serrano. A scholar is included among the top collaborators of Vesna de Serrano 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 Vesna de Serrano. Vesna de Serrano 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.
Serrano, Vesna de, et al.. (2024). Structural Comparison of Substrate Binding Sites in Dehaloperoxidase A and B. Biochemistry. 63(14). 1761–1773. 2 indexed citations
2.
Serrano, Vesna de, et al.. (2023). Comparative study of the binding and activation of 2,4-dichlorophenol by dehaloperoxidase A and B. Journal of Inorganic Biochemistry. 247. 112332–112332. 5 indexed citations
3.
4.
Yun, Dongju, Vesna de Serrano, & Reza A. Ghiladi. (2022). Oxidation of bisphenol A (BPA) and related compounds by the multifunctional catalytic globin dehaloperoxidase. Journal of Inorganic Biochemistry. 238. 112020–112020. 9 indexed citations
5.
Serrano, Vesna de, et al.. (2019). The multifunctional globin dehaloperoxidase strikes again: Simultaneous peroxidase and peroxygenase mechanisms in the oxidation of EPA pollutants. Archives of Biochemistry and Biophysics. 673. 108079–108079. 14 indexed citations
6.
Zhao, Junjie, Vesna de Serrano, & Stefan Franzen. (2014). A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct. Biochemistry. 53(15). 2474–2482. 12 indexed citations
7.
Liu, Fange, et al.. (2013). Pirin is an iron-dependent redox regulator of NF-κB. Proceedings of the National Academy of Sciences. 110(24). 9722–9727. 92 indexed citations
8.
Zhao, Jing, et al.. (2013). Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata. Biochemistry. 52(14). 2427–2439. 31 indexed citations
9.
Zhao, Junjie, et al.. (2012). The Role of the Distal Histidine in H2O2 Activation and Heme Protection in both Peroxidase and Globin Functions. The Journal of Physical Chemistry B. 116(40). 12065–12077. 23 indexed citations
10.
Serrano, Vesna de & Stefan Franzen. (2011). Structural evidence for stabilization of inhibitor binding by a protein cavity in the dehaloperoxidase‐hemoglobin from Amphitrite ornata. Biopolymers. 98(1). 27–35. 28 indexed citations
11.
Zhao, Junjie, et al.. (2011). Effect of H55D Mutation on Kinetics and Structure of Dehaloperoxidase-Hemoglobin A. Biophysical Journal. 100(3). 221a–221a. 1 indexed citations
12.
D'Antonio, E.L., Vesna de Serrano, Hanna Gracz, et al.. (2011). Functional Consequences of the Creation of an Asp-His-Fe Triad in a 3/3 Globin. Biochemistry. 50(44). 9664–9680. 20 indexed citations
13.
Thompson, Matthew K., M.F. Davis, Vesna de Serrano, et al.. (2010). Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function. Biophysical Journal. 99(5). 1586–1595. 51 indexed citations
14.
Serrano, Vesna de, et al.. (2010). Structure of dehaloperoxidase B at 1.58 Å resolution and structural characterization of the AB dimer fromAmphitrite ornata. Acta Crystallographica Section D Biological Crystallography. 66(5). 529–538. 35 indexed citations
15.
Davis, M.F., Hanna Gracz, Franck A. P. Vendeix, et al.. (2009). Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata. Biochemistry. 48(10). 2164–2172. 45 indexed citations
16.
Serrano, Vesna de, et al.. (2008). Distal histidine conformational flexibility in dehaloperoxidase fromAmphitrite ornata. Acta Crystallographica Section D Biological Crystallography. 65(1). 34–40. 38 indexed citations
17.
Serrano, Vesna de, et al.. (2007). X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned fromAmphitrite ornata. Acta Crystallographica Section D Biological Crystallography. 63(10). 1094–1101. 40 indexed citations
18.
Nicely, Nathan I., et al.. (2004). Crystal Structures of Ral-GppNHp and Ral-GDP Reveal Two Binding Sites that Are Also Present in Ras and Rap. Structure. 12(11). 2025–2036. 33 indexed citations
19.
Buhrman, Greg, Vesna de Serrano, & Carla Mattos. (2003). Organic Solvents Order the Dynamic Switch II in Ras Crystals. Structure. 11(7). 747–751. 34 indexed citations
20.
Castellino, F.J., Tetsumei Urano, Vesna de Serrano, Joseph P. Morris, & B A Chibber. (1988). Control of Human Plasminogen Activation. Pathophysiology of Haemostasis and Thrombosis. 18(Suppl. 1). 15–23. 9 indexed citations

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