Robert J. Kurzeja

1.2k total citations
13 papers, 566 citations indexed

About

Robert J. Kurzeja is a scholar working on Molecular Biology, Biochemistry and Cancer Research. According to data from OpenAlex, Robert J. Kurzeja has authored 13 papers receiving a total of 566 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 3 papers in Biochemistry and 3 papers in Cancer Research. Recurrent topics in Robert J. Kurzeja's work include Metabolomics and Mass Spectrometry Studies (3 papers), Cancer, Hypoxia, and Metabolism (3 papers) and Amino Acid Enzymes and Metabolism (2 papers). Robert J. Kurzeja is often cited by papers focused on Metabolomics and Mass Spectrometry Studies (3 papers), Cancer, Hypoxia, and Metabolism (3 papers) and Amino Acid Enzymes and Metabolism (2 papers). Robert J. Kurzeja collaborates with scholars based in United States and United Kingdom. Robert J. Kurzeja's co-authors include Evelyn Yang, James Zondlo, Vivian Li, Rashid Syed, Jeffrey Lewis, Christopher J. Schofield, Christopher Mohr, Steven R. Jordan, Neil J. Oldham and M.A. McDonough and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and PLoS ONE.

In The Last Decade

Robert J. Kurzeja

13 papers receiving 558 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Robert J. Kurzeja United States	9	401	278	70	68	63	13	566
Mun Chiang Chan United Kingdom	14	591 1.5×	372 1.3×	98 1.4×	56 0.8×	36 0.6×	22	850
Imre Schlemminger Germany	11	457 1.1×	356 1.3×	91 1.3×	53 0.8×	19 0.3×	12	764
Danica Butler United Kingdom	12	936 2.3×	286 1.0×	69 1.0×	55 0.8×	28 0.4×	12	1.1k
Nicholas D. Adams United States	8	416 1.0×	307 1.1×	18 0.3×	51 0.8×	22 0.3×	11	817
Dominick Mobilio United States	9	278 0.7×	85 0.3×	60 0.9×	22 0.3×	30 0.5×	13	544
Mary S. Kovacs United States	15	569 1.4×	359 1.3×	72 1.0×	83 1.2×	11 0.2×	19	896
Xin Lin Zu Australia	6	591 1.5×	373 1.3×	32 0.5×	23 0.3×	83 1.3×	7	738
Ayuna Hattori Japan	10	368 0.9×	163 0.6×	12 0.2×	29 0.4×	48 0.8×	17	496
Benjamin Schwartz United States	6	440 1.1×	301 1.1×	23 0.3×	37 0.5×	19 0.3×	6	576
Rachel E. Hayden United Kingdom	12	349 0.9×	108 0.4×	26 0.4×	32 0.5×	13 0.2×	14	579

Countries citing papers authored by Robert J. Kurzeja

Since Specialization

Citations

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

Fields of papers citing papers by Robert J. Kurzeja

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert J. Kurzeja

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

All Works

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13 of 13 papers shown

Sickmier, E. Allen, et al.. (2016). The Panitumumab EGFR Complex Reveals a Binding Mechanism That Overcomes Cetuximab Induced Resistance. PLoS ONE. 11(9). e0163366–e0163366. 55 indexed citations

Campuzano, Iain D. G., Huilin Li, Dhanashri Bagal, et al.. (2016). Native MS Analysis of Bacteriorhodopsin and an Empty Nanodisc by Orthogonal Acceleration Time-of-Flight, Orbitrap and Ion Cyclotron Resonance. Analytical Chemistry. 88(24). 12427–12436. 48 indexed citations

Xu, Han, John J. Hill, Klaus Michelsen, et al.. (2015). Characterization of the direct interaction between KcsA-Kv1.3 and its inhibitors. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1848(10). 1974–1980. 19 indexed citations

Chen, Kui, Klaus Michelsen, Robert J. Kurzeja, et al.. (2014). Discovery of Small-Molecule Glucokinase Regulatory Protein Modulators That Restore Glucokinase Activity. SLAS DISCOVERY. 19(7). 1014–1023. 5 indexed citations

Zhang, Yihong, Robert J. Kurzeja, James Zondlo, et al.. (2011). Abstract 253: Identification of STK33 kinase inhibitors for the validation of a synthetic lethal relationship between STK33 and mutant KRAS. Cancer Research. 71(8_Supplement). 253–253. 1 indexed citations

Annis, Douglas S., Cliff C. Cheng, Cheng‐Chi Chuang, et al.. (2009). Inhibitors of the Lipid Phosphatase SHIP2 Discovered by High Throughput Affinity Selection-Mass Spectrometry Screening of Combinatorial Libraries. Combinatorial Chemistry & High Throughput Screening. 12(8). 760–771. 24 indexed citations

Poppe, Leszek, Christopher M. Tegley, Vivian Li, et al.. (2009). Different Modes of Inhibitor Binding to Prolyl Hydroxylase by Combined Use of X-ray Crystallography and NMR Spectroscopy of Paramagnetic Complexes. Journal of the American Chemical Society. 131(46). 16654–16655. 19 indexed citations

Kurzeja, Robert J., et al.. (2008). Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology. Analytical Biochemistry. 384(2). 213–223. 63 indexed citations

Yu, Violeta, Yanyan Tudor, Clarence Hale, et al.. (2007). High Capacity Homogeneous Non-Radioactive Cortisol Detection Assays for Human 11 β -Hydroxysteroid Dehydrogenase Type 1. Assay and Drug Development Technologies. 5(1). 105–116. 1 indexed citations

10.

McDonough, M.A., Vivian Li, Emily Flashman, et al.. (2006). Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proceedings of the National Academy of Sciences. 103(26). 9814–9819. 295 indexed citations

11.

Hale, Clarence, et al.. (2006). A High-Throughput Microfluidic Assay for SH2 Domain-Containing Inositol 5-Phosphatase 2. Assay and Drug Development Technologies. 4(2). 175–183. 11 indexed citations

12.

Mitchell, John L.A., et al.. (1996). Overproduction of stable ornithine decarboxylase and antizyme in the difluoromethylornithine-resistant cell line DH23b. Biochemical Journal. 317(3). 811–816. 24 indexed citations

13.

Kurzeja, Robert J., et al.. (1992). Recovery of ornithine decarboxylase activity after inhibition with α-difluoromethylornithine. Biochemical and Biophysical Research Communications. 187(1). 443–447. 1 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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