E. Ugochukwu

718 total citations
6 papers, 528 citations indexed

About

E. Ugochukwu is a scholar working on Molecular Biology, Genetics and Oncology. According to data from OpenAlex, E. Ugochukwu has authored 6 papers receiving a total of 528 indexed citations (citations by other indexed papers that have themselves been cited), including 3 papers in Molecular Biology, 3 papers in Genetics and 2 papers in Oncology. Recurrent topics in E. Ugochukwu's work include Coagulation, Bradykinin, Polyphosphates, and Angioedema (2 papers), Protein Tyrosine Phosphatases (2 papers) and Galectins and Cancer Biology (2 papers). E. Ugochukwu is often cited by papers focused on Coagulation, Bradykinin, Polyphosphates, and Angioedema (2 papers), Protein Tyrosine Phosphatases (2 papers) and Galectins and Cancer Biology (2 papers). E. Ugochukwu collaborates with scholars based in United Kingdom, Germany and Finland. E. Ugochukwu's co-authors include Stefan Knapp, A. Barr, Wen‐Hwa Lee, P. Savitsky, I. Alfano, Oliver N. F. King, N. Burgess-Brown, Susanne Müller, P. Filippakopoulos and Scott A. White and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

E. Ugochukwu

6 papers receiving 522 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
E. Ugochukwu United Kingdom	6	455	221	74	40	38	6	528
S C Lucas United Kingdom	10	359 0.8×	340 1.5×	154 2.1×	38 0.9×	26 0.7×	11	622
Daisy Lio Australia	10	365 0.8×	85 0.4×	111 1.5×	42 1.1×	55 1.4×	16	541
Behnaz Ahangarian Abhari Germany	15	555 1.2×	144 0.7×	152 2.1×	42 1.1×	33 0.9×	26	699
David Critton United States	9	448 1.0×	136 0.6×	71 1.0×	64 1.6×	7 0.2×	12	543
Sabina Keen Canada	6	385 0.8×	127 0.6×	96 1.3×	47 1.2×	7 0.2×	6	478
Peter Gildsig Jansen Denmark	5	781 1.7×	481 2.2×	106 1.4×	48 1.2×	8 0.2×	5	863
Deborah Moshinsky United States	11	270 0.6×	54 0.2×	166 2.2×	31 0.8×	32 0.8×	14	431
Yingdai Gao China	13	301 0.7×	91 0.4×	86 1.2×	12 0.3×	73 1.9×	42	536
Ahmed S.A. Mady United States	9	341 0.7×	52 0.2×	114 1.5×	25 0.6×	14 0.4×	13	444
Franziska Wachter United States	13	369 0.8×	53 0.2×	157 2.1×	42 1.1×	18 0.5×	28	521

Countries citing papers authored by E. Ugochukwu

Since Specialization

Citations

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

Fields of papers citing papers by E. Ugochukwu

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of E. Ugochukwu

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

All Works

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6 of 6 papers shown

1.

Salah, E., E. Ugochukwu, A. Barr, et al.. (2011). Crystal Structures of ABL-Related Gene (ABL2) in Complex with Imatinib, Tozasertib (VX-680), and a Type I Inhibitor of the Triazole Carbothioamide Class. Journal of Medicinal Chemistry. 54(7). 2359–2367. 35 indexed citations

2.

Barr, A., E. Ugochukwu, Wen‐Hwa Lee, et al.. (2009). Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome. Cell. 136(2). 352–363. 376 indexed citations

3.

Lee, Wen‐Hwa, Petra Lukacik, Kunde Guo, et al.. (2008). Structure–activity relationships of human AKR-type oxidoreductases involved in bile acid synthesis: AKR1D1 and AKR1C4. Molecular and Cellular Endocrinology. 301(1-2). 199–204. 15 indexed citations

4.

Ugochukwu, E., Andrew L. Lovering, O.C. Mather, Thomas W. Young, & Scott A. White. (2007). The Crystal Structure of the Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae Reveals the Basis for Substrate Specificity. Journal of Molecular Biology. 371(4). 1007–1021. 31 indexed citations

5.

Ugochukwu, E., et al.. (2007). Kinetic and Mutational Analyses of the Major Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae. Journal of Biological Chemistry. 282(13). 9302–9311. 20 indexed citations

6.

Eswaran, Jeyanthy, Brian D. Marsden, J.E. Debreczeni, et al.. (2006). Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases. Biochemical Journal. 395(3). 483–491. 51 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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