Richard E. Honkanen

4.2k total citations
76 papers, 3.4k citations indexed

About

Richard E. Honkanen is a scholar working on Molecular Biology, Cancer Research and Cell Biology. According to data from OpenAlex, Richard E. Honkanen has authored 76 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 60 papers in Molecular Biology, 14 papers in Cancer Research and 11 papers in Cell Biology. Recurrent topics in Richard E. Honkanen's work include Enzyme function and inhibition (12 papers), Biochemical and Molecular Research (10 papers) and Beetle Biology and Toxicology Studies (9 papers). Richard E. Honkanen is often cited by papers focused on Enzyme function and inhibition (12 papers), Biochemical and Molecular Research (10 papers) and Beetle Biology and Toxicology Studies (9 papers). Richard E. Honkanen collaborates with scholars based in United States, Sweden and France. Richard E. Honkanen's co-authors include Mark R. Swingle, Teresa Golden, Nicholas M. Dean, Aiyang Cheng, Ni Li, Ileana Aragon, Xizhong Huang, Zhuang Zuo, Gudrun Urban and Guofei Zhou and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Richard E. Honkanen

76 papers receiving 3.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Richard E. Honkanen United States	35	2.4k	497	396	376	273	76	3.4k
C. James Hastie United Kingdom	26	3.0k 1.3×	332 0.7×	650 1.6×	649 1.7×	231 0.8×	37	4.2k
Wilfried Merlevede Belgium	42	3.5k 1.5×	363 0.7×	1.0k 2.5×	427 1.1×	176 0.6×	146	5.2k
Susana Alemany Spain	29	1.6k 0.7×	263 0.5×	313 0.8×	267 0.7×	82 0.3×	66	2.7k
Masaru Miyagi United States	37	3.8k 1.6×	283 0.6×	339 0.9×	445 1.2×	117 0.4×	128	5.9k
Randall C. Schatzman United States	29	1.9k 0.8×	161 0.3×	327 0.8×	431 1.1×	228 0.8×	42	4.7k
Vladimir N. Ivanov United States	38	2.4k 1.0×	700 1.4×	222 0.6×	948 2.5×	80 0.3×	76	4.1k
Weiru Wang United States	32	2.9k 1.2×	169 0.3×	353 0.9×	705 1.9×	230 0.8×	67	3.9k
Yong Cai China	36	3.4k 1.4×	694 1.4×	327 0.8×	500 1.3×	151 0.6×	164	4.6k
Greg B. G. Moorhead Canada	39	4.6k 1.9×	273 0.5×	948 2.4×	526 1.4×	65 0.2×	107	5.8k
Solange Desagher France	18	4.0k 1.7×	447 0.9×	540 1.4×	672 1.8×	104 0.4×	23	5.1k

Countries citing papers authored by Richard E. Honkanen

Since Specialization

Citations

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

Fields of papers citing papers by Richard E. Honkanen

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Richard E. Honkanen

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

All Works

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20 of 20 papers shown

Swingle, Mark R., Alla Musiyenko, Chenchen Li, et al.. (2023). Quantitative proteomics and phosphoproteomics of PP2A-PPP2R5D variants reveal deregulation of RPS6 phosphorylation via converging signaling cascades. Journal of Biological Chemistry. 299(9). 105154–105154. 5 indexed citations

Salter, E. Alan, Andrzej Wierzbicki, Richard E. Honkanen, & Mark R. Swingle. (2023). Quantum-based modeling implies that bidentate Arg89-substrate binding enhances serine/threonine protein phosphatase-2A(PPP2R5D/PPP2R1A/PPP2CA)-mediated dephosphorylation. Frontiers in Cell and Developmental Biology. 11. 1141804–1141804. 2 indexed citations

Swingle, Mark R., Richard Heng, Mourad Toporsian, et al.. (2021). A disorder-related variant (E420K) of a PP2A-regulatory subunit (PPP2R5D) causes constitutively active AKT-mTOR signaling and uncoordinated cell growth. Journal of Biological Chemistry. 296. 100313–100313. 21 indexed citations

Swingle, Mark R., et al.. (2019). The Antitumor Drug LB-100 Is a Catalytic Inhibitor of Protein Phosphatase 2A (PPP2CA) and 5 (PPP5C) Coordinating with the Active-Site Catalytic Metals in PPP5C. Molecular Cancer Therapeutics. 18(3). 556–566. 47 indexed citations

Swingle, Mark R., Claude‐Henry Volmar, S. Adrian Saldanha, et al.. (2016). An Ultra-High-Throughput Screen for Catalytic Inhibitors of Serine/Threonine Protein Phosphatases Types 1 and 5 (PP1C and PP5C). SLAS DISCOVERY. 22(1). 21–31. 8 indexed citations

Chattopadhyay, Debasish, Mark R. Swingle, E. Alan Salter, et al.. (2016). Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. Biochemical Pharmacology. 109. 14–26. 25 indexed citations

Swingle, Mark R. & Richard E. Honkanen. (2014). Development and Validation of a Robust and Sensitive Assay for the Discovery of Selective Inhibitors for Serine/Threonine Protein Phosphatases PP1α ( PPP1C ) and PP5 ( PPP5C ). Assay and Drug Development Technologies. 12(8). 481–496. 10 indexed citations

Musiyenko, Alla, Joel Andrews, Gudrun Urban, et al.. (2013). Suppression of Ser/Thr Phosphatase 4 (PP4C/ PPP4C ) Mimics a Novel Post-Mitotic Action of Fostriecin, Producing Mitotic Slippage Followed by Tetraploid Cell Death. Molecular Cancer Research. 11(8). 845–855. 12 indexed citations

Goudreault, Marilyn, Hyungwon Choi, Michael Mullin, et al.. (2011). Label‐free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. PROTEOMICS. 11(8). 1508–1516. 57 indexed citations

10.

Swingle, Mark R., Lauren Amable, Brian G. Lawhorn, et al.. (2009). Structure-Activity Relationship Studies of Fostriecin, Cytostatin, and Key Analogs, with PP1, PP2A, PP5, and (β12–β13)-Chimeras (PP1/PP2A and PP5/PP2A), Provide Further Insight into the Inhibitory Actions of Fostriecin Family Inhibitors. Journal of Pharmacology and Experimental Therapeutics. 331(1). 45–53. 48 indexed citations

11.

Li, Ni, et al.. (2007). High Yield Expression of Serine/Threonine Protein Phosphatase Type 5, and a Fluorescent Assay Suitable for Use in the Detection of Catalytic Inhibitors. Assay and Drug Development Technologies. 5(5). 645–654. 21 indexed citations

12.

Golden, Teresa, Ileana Aragon, Guofei Zhou, et al.. (2004). Constitutive over expression of serine/threonine protein phosphatase 5 (PP5) augments estrogen-dependent tumor growth in mice. Cancer Letters. 215(1). 95–100. 31 indexed citations

13.

Sjöholm, Åke, Per‐Olof Berggren, & Richard E. Honkanen. (2001). Effects of Second Messengers on Serine/Threonine Protein Phosphatases in Insulin-Secreting Cells. Biochemical and Biophysical Research Communications. 283(2). 364–368. 2 indexed citations

14.

Urban, Gudrun, Teresa Golden, Ileana Aragon, et al.. (2001). Identification of an Estrogen-inducible Phosphatase (PP5) That Converts MCF-7 Human Breast Carcinoma Cells into an Estrogen-independent Phenotype when Expressed Constitutively. Journal of Biological Chemistry. 276(29). 27638–27646. 47 indexed citations

15.

Cheng, Aiyang, Nicholas M. Dean, & Richard E. Honkanen. (2000). Serine/Threonine Protein Phosphatase Type 1γ1 Is Required for the Completion of Cytokinesis in Human A549 Lung Carcinoma Cells. Journal of Biological Chemistry. 275(3). 1846–1854. 53 indexed citations

16.

Connor, John H., et al.. (1999). Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors. Journal of Biological Chemistry. 274(32). 22366–22372. 69 indexed citations

17.

Cheng, Aiyang, et al.. (1997). Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Letters. 416(3). 230–234. 185 indexed citations

18.

Kao, Race L., et al.. (1997). Comparison ofIn VitroPreconditioning Responses of Isolated Pig and Rabbit Cardiomyocytes: Effects of a Protein Phosphatase Inhibitor, Fostriecin. Journal of Molecular and Cellular Cardiology. 29(11). 3009–3024. 34 indexed citations

19.

Honkanen, Richard E., et al.. (1991). Cyanobacterial Nodularin Is a Potent Inhibitor of Type 1 and Type 2A Protein Phosphatases. Molecular Pharmacology. 40(4). 577–583. 113 indexed citations

20.

Zwiller, Jean, et al.. (1990). Phosphorylation of an inositol phosphate-stimulated protein phosphatase by protein kinase C.. PubMed. 20(5). 967–77. 3 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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