Moshe Finel

7.2k total citations
156 papers, 6.0k citations indexed

About

Moshe Finel is a scholar working on Molecular Biology, Pharmacology and Oncology. According to data from OpenAlex, Moshe Finel has authored 156 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 90 papers in Molecular Biology, 87 papers in Pharmacology and 44 papers in Oncology. Recurrent topics in Moshe Finel's work include Pharmacogenetics and Drug Metabolism (84 papers), Drug Transport and Resistance Mechanisms (42 papers) and Photosynthetic Processes and Mechanisms (26 papers). Moshe Finel is often cited by papers focused on Pharmacogenetics and Drug Metabolism (84 papers), Drug Transport and Resistance Mechanisms (42 papers) and Photosynthetic Processes and Mechanisms (26 papers). Moshe Finel collaborates with scholars based in Finland, United States and China. Moshe Finel's co-authors include Mårten Wikström, Anne Puustinen, Mika Kurkela, Risto Kostiainen, Michael H. Court, Anna Majander, Tuomas Haltia, Jari Yli‐Kauhaluoma, Jouni Hirvonen and Anna Radomińska‐Pandya and has published in prestigious journals such as Journal of Biological Chemistry, The EMBO Journal and PLoS ONE.

In The Last Decade

Moshe Finel

155 papers receiving 5.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Moshe Finel Finland 45 3.5k 1.9k 1.0k 502 483 156 6.0k
Bettie Sue Siler Masters United States 52 4.1k 1.2× 2.8k 1.5× 1.2k 1.2× 477 1.0× 473 1.0× 131 11.0k
Takashi Iyanagi Japan 39 3.0k 0.8× 2.2k 1.2× 1.2k 1.1× 908 1.8× 338 0.7× 85 6.2k
Marilyn E. Morris United States 45 3.4k 1.0× 1.1k 0.6× 2.2k 2.1× 715 1.4× 729 1.5× 189 7.8k
Jürgen Borlak Germany 49 3.8k 1.1× 1.6k 0.9× 1.0k 1.0× 361 0.7× 301 0.6× 201 8.7k
Michael W.H. Coughtrie United Kingdom 42 2.6k 0.7× 2.1k 1.1× 871 0.9× 783 1.6× 347 0.7× 139 6.2k
Henry W. Strobel United States 42 2.3k 0.7× 3.4k 1.8× 1.5k 1.5× 350 0.7× 491 1.0× 159 6.0k
Xinxin Ding United States 46 2.6k 0.7× 3.1k 1.7× 1.5k 1.5× 262 0.5× 411 0.9× 210 6.7k
Peter Moldéus Sweden 53 3.4k 1.0× 2.5k 1.4× 1.1k 1.1× 292 0.6× 527 1.1× 221 9.7k
M.W. Anders United States 45 4.3k 1.2× 1.7k 0.9× 815 0.8× 311 0.6× 451 0.9× 173 8.9k
Howard G. Shertzer United States 46 3.5k 1.0× 864 0.5× 497 0.5× 256 0.5× 307 0.6× 128 8.1k

Countries citing papers authored by Moshe Finel

Since Specialization
Citations

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

Fields of papers citing papers by Moshe Finel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Moshe Finel

This figure shows the co-authorship network connecting the top 25 collaborators of Moshe Finel. A scholar is included among the top collaborators of Moshe Finel 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 Moshe Finel. Moshe Finel 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.
Liu, Peiqi, Guanghao Zhu, Hairong Zeng, et al.. (2024). Human UDP-glucuronosyltransferase 1As catalyze aristolochic acid D O-glucuronidation to form a lesser nephrotoxic glucuronide. Journal of Ethnopharmacology. 328. 118116–118116. 3 indexed citations
2.
Juvonen, Risto O., et al.. (2024). Anthraquinone biocolourant dermocybin is metabolized whereas dermorubin is not in in vitro liver fractions and recombinant metabolic enzymes. Basic & Clinical Pharmacology & Toxicology. 134(6). 846–857.
3.
He, Rong-Jing, Ziru Dai, Moshe Finel, et al.. (2023). Fluorescence-Based High-Throughput Assays for Investigating Cytochrome P450 Enzyme-Mediated Drug–Drug Interactions. Drug Metabolism and Disposition. 51(10). 1254–1272. 8 indexed citations
4.
Kidron, Heidi, et al.. (2019). Human efflux transport of testosterone, epitestosterone and other androgen glucuronides. The Journal of Steroid Biochemistry and Molecular Biology. 197. 105518–105518. 17 indexed citations
5.
Juvonen, Risto O., Sanna Niinivehmas, Aleksanteri Petsalo, et al.. (2018). Molecular Docking-Based Design and Development of a Highly Selective Probe Substrate for UDP-glucuronosyltransferase 1A10. Molecular Pharmaceutics. 15(3). 923–933. 18 indexed citations
6.
7.
Ge, Guang‐Bo, et al.. (2016). UGT1A10 Is a High Activity and Important Extrahepatic Enzyme: Why Has Its Role in Intestinal Glucuronidation Been Frequently Underestimated?. Molecular Pharmaceutics. 14(9). 2875–2883. 24 indexed citations
8.
Starlard‐Davenport, Athena, Vineetha Koroth Edavana, Stacie M. Bratton, et al.. (2014). A Potential Role for Human UDP-Glucuronosyltransferase 1A4 Promoter Single Nucleotide Polymorphisms in the Pharmacogenomics of Tamoxifen and Its Derivatives. Drug Metabolism and Disposition. 42(9). 1392–1400. 11 indexed citations
9.
Waart, Dirk R. de, Lysbeth ten Bloemendaal, Suzanne Duijst, et al.. (2012). Ezetimibe: A biomarker for efficacy of liver directed UGT1A1 gene therapy for inherited hyperbilirubinemia. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1822(8). 1223–1229. 6 indexed citations
10.
Kidron, Heidi, Nenad Manevski, Marika Häkli, et al.. (2012). Impact of probe compound in MRP2 vesicular transport assays. European Journal of Pharmaceutical Sciences. 46(1-2). 100–105. 29 indexed citations
11.
Kurkela, Mika, et al.. (2011). Fluorescence-Based High-Throughput Screening Assay for Drug Interactions with UGT1A6. Assay and Drug Development Technologies. 9(5). 496–502. 7 indexed citations
12.
Zhang, Hongbo, et al.. (2010). Effects of Cell Differentiation and Assay Conditions on the UDP-Glucuronosyltransferase Activity in Caco-2 Cells. Drug Metabolism and Disposition. 39(3). 456–464. 18 indexed citations
13.
Mackenzie, Peter I., et al.. (2008). The Configuration of the 17-Hydroxy Group Variably Influences the Glucuronidation of β-Estradiol and Epiestradiol by Human UDP-Glucuronosyltransferases. Drug Metabolism and Disposition. 36(11). 2307–2315. 91 indexed citations
14.
Trubetskoy, Olga V., et al.. (2007). High Throughput Screening Assay for UDP-Glucuronosyltransferase 1A1 Glucuronidation Profiling. Assay and Drug Development Technologies. 5(3). 343–354. 17 indexed citations
15.
Galkin, Anna, Moshe Finel, Kaija H. Valkonen, et al.. (2007). Transport properties of bovine and reindeer β-lactoglobulin in the Caco-2 cell model. International Journal of Pharmaceutics. 347(1-2). 1–8. 12 indexed citations
16.
Starlard‐Davenport, Athena, et al.. (2006). Phenylalanine90 and phenylalanine93 are crucial amino acids within the estrogen binding site of the human UDP-glucuronosyltransferase 1A10. Steroids. 72(1). 85–94. 33 indexed citations
17.
Uutela, Päivi, et al.. (2006). Prominent but Reverse Stereoselectivity in Propranolol Glucuronidation by Human UDP-Glucuronosyltransferases 1A9 and 1A10. Drug Metabolism and Disposition. 34(9). 1488–1494. 42 indexed citations
18.
Anderka, Oliver, Kathy Pfeiffer, Takao Yagi, et al.. (2004). Assembly of Respiratory Complexes I, III, and IV into NADH Oxidase Supercomplex Stabilizes Complex I in Paracoccus denitrificans. Journal of Biological Chemistry. 279(6). 5000–5007. 193 indexed citations
19.
Majander, Anna, Moshe Finel, Marja‐Liisa Savontaus, Eeva Nikoskelainen, & Mårten Wikström. (1996). Catalytic Activity of Complex I in Cell Lines that Possess Replacement Mutations in the ND Genes in Leber's Hereditary Optic Neuropathy. European Journal of Biochemistry. 239(1). 201–207. 61 indexed citations
20.
Finel, Moshe. (1988). Proteolysis of Paracoccus denitrificans cytochrome oxidase by trypsin and chymotrypsin. FEBS Letters. 236(2). 415–419. 11 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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