Kathryn Perez

989 total citations
11 papers, 667 citations indexed

About

Kathryn Perez is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Inorganic Chemistry. According to data from OpenAlex, Kathryn Perez has authored 11 papers receiving a total of 667 indexed citations (citations by other indexed papers that have themselves been cited), including 5 papers in Molecular Biology, 5 papers in Renewable Energy, Sustainability and the Environment and 3 papers in Inorganic Chemistry. Recurrent topics in Kathryn Perez's work include Metalloenzymes and iron-sulfur proteins (5 papers), Electrocatalysts for Energy Conversion (3 papers) and Organometallic Complex Synthesis and Catalysis (2 papers). Kathryn Perez is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (5 papers), Electrocatalysts for Energy Conversion (3 papers) and Organometallic Complex Synthesis and Catalysis (2 papers). Kathryn Perez collaborates with scholars based in Germany, United States and France. Kathryn Perez's co-authors include Thomas Spatzal, Douglas C. Rees, James B. Howard, Oliver Einsle, Ailiena O. Maggiolo, Trixia M. Buscagan, Thomas Colby, Juán José Bonfiglio, Pablo San Segundo‐Acosta and Ivan Matić and has published in prestigious journals such as Science, Cell and Nucleic Acids Research.

In The Last Decade

Kathryn Perez

11 papers receiving 666 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Kathryn Perez Germany	7	471	297	172	166	119	11	667
Matthew I. Radle United States	8	253 0.5×	56 0.2×	44 0.3×	80 0.5×	290 2.4×	9	454
Aubrey D. Scott United States	7	221 0.5×	75 0.3×	86 0.5×	65 0.4×	82 0.7×	10	329
Richard C. Conover United States	18	410 0.9×	14 0.0×	130 0.8×	233 1.4×	259 2.2×	26	750
Truc Chi T. Pham United States	7	333 0.7×	25 0.1×	54 0.3×	41 0.2×	144 1.2×	7	504
Joyce P. Whitehead United States	11	187 0.4×	25 0.1×	101 0.6×	109 0.7×	177 1.5×	11	478
Brian R. Crouse United States	11	337 0.7×	11 0.0×	52 0.3×	237 1.4×	230 1.9×	13	544
David W. Kastner United States	12	30 0.1×	13 0.0×	129 0.8×	119 0.7×	191 1.6×	22	411
Rangam Gopinath India	12	25 0.1×	41 0.1×	126 0.7×	283 1.7×	274 2.3×	20	970
Richard J. Jodts United States	11	137 0.3×	23 0.1×	60 0.3×	141 0.8×	124 1.0×	14	304
Anne K. Hickey United States	13	45 0.1×	30 0.1×	68 0.4×	223 1.3×	48 0.4×	15	475

Countries citing papers authored by Kathryn Perez

Since Specialization

Citations

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

Fields of papers citing papers by Kathryn Perez

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kathryn Perez

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

All Works

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11 of 11 papers shown

1.

Perez, Kathryn, et al.. (2024). Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra. Nature Communications. 15(1). 4041–4041. 1 indexed citations

2.

Aresta‐Branco, Francisco, Gianna Triller, Monique van Straaten, et al.. (2023). Immunodominant surface epitopes power immune evasion in the African trypanosome. Cell Reports. 42(3). 112262–112262. 4 indexed citations

3.

Simon, Bernd, Pravin Kumar Ankush Jagtap, Sophie L. Winter, et al.. (2021). Structure and dynamics of the quaternary hunchback mRNA translation repression complex. Nucleic Acids Research. 49(15). 8866–8885. 6 indexed citations

4.

Dimitrova-Paternoga, Lyudmila, Pravin Kumar Ankush Jagtap, Karine Lapouge, et al.. (2021). Molecular basis of mRNA transport by a kinesin-1–atypical tropomyosin complex. Genes & Development. 35(13-14). 976–991. 23 indexed citations

5.

Zeelen, Johan, Monique van Straaten, A. Hempelmann, et al.. (2021). Structure of trypanosome coat protein VSGsur and function in suramin resistance. Nature Microbiology. 6(3). 392–400. 22 indexed citations

6.

Bonfiglio, Juán José, Orsolya Leidecker, Helen Dauben, et al.. (2020). An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell. 183(4). 1086–1102.e23. 72 indexed citations

7.

Chen, Po‐Chia, et al.. (2020). Structure-based screening of binding affinities via small-angle X-ray scattering. IUCrJ. 7(4). 644–655. 11 indexed citations

8.

Buscagan, Trixia M., Kathryn Perez, Ailiena O. Maggiolo, Douglas C. Rees, & Thomas Spatzal. (2020). Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site. Angewandte Chemie International Edition. 60(11). 5704–5707. 59 indexed citations

9.

Buscagan, Trixia M., Kathryn Perez, Ailiena O. Maggiolo, Douglas C. Rees, & Thomas Spatzal. (2020). Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site. Angewandte Chemie. 133(11). 5768–5771. 6 indexed citations

10.

Spatzal, Thomas, Kathryn Perez, James B. Howard, & Douglas C. Rees. (2015). Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. eLife. 4. e11620–e11620. 120 indexed citations

11.

Spatzal, Thomas, Kathryn Perez, Oliver Einsle, James B. Howard, & Douglas C. Rees. (2014). Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science. 345(6204). 1620–1623. 343 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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