John L. Nitiss

9.3k total citations · 3 hit papers
101 papers, 7.4k citations indexed

About

John L. Nitiss is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, John L. Nitiss has authored 101 papers receiving a total of 7.4k indexed citations (citations by other indexed papers that have themselves been cited), including 96 papers in Molecular Biology, 43 papers in Oncology and 20 papers in Organic Chemistry. Recurrent topics in John L. Nitiss's work include Cancer therapeutics and mechanisms (87 papers), DNA Repair Mechanisms (27 papers) and Lung Cancer Research Studies (20 papers). John L. Nitiss is often cited by papers focused on Cancer therapeutics and mechanisms (87 papers), DNA Repair Mechanisms (27 papers) and Lung Cancer Research Studies (20 papers). John L. Nitiss collaborates with scholars based in United States, Denmark and Canada. John L. Nitiss's co-authors include Yves Pommier, J C Wang, Yilun Sun, Karin C. Nitiss, Shar-yin N. Huang, Neil Osheroff, Yuchu Hsiung, William T. Beck, James C. Wang and Jerrylaine V. Walker and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

John L. Nitiss

101 papers receiving 7.3k citations

Hit Papers

Targeting DNA topoisomerase II in cancer chemotherapy 2009 2026 2014 2020 2009 2009 2016 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John L. Nitiss United States 41 6.5k 2.5k 1.3k 1.2k 511 101 7.4k
Giovanni Capranico Italy 47 4.9k 0.8× 2.0k 0.8× 1.0k 0.8× 948 0.8× 385 0.8× 144 6.2k
Caroline A. Austin United Kingdom 40 4.5k 0.7× 1.8k 0.7× 727 0.6× 664 0.5× 307 0.6× 135 5.4k
Michael R. Mattern United States 46 5.8k 0.9× 2.6k 1.0× 758 0.6× 653 0.5× 326 0.6× 107 7.0k
Glenda Kohlhagen United States 43 4.1k 0.6× 1.9k 0.8× 1.3k 1.0× 1.1k 0.9× 413 0.8× 70 5.3k
William T. Beck United States 50 5.3k 0.8× 4.2k 1.7× 560 0.4× 429 0.3× 367 0.7× 131 7.4k
Thomas C. Rowe United States 24 3.2k 0.5× 1.2k 0.5× 691 0.5× 593 0.5× 293 0.6× 44 4.2k
Philippe Pourquier France 37 3.2k 0.5× 1.5k 0.6× 502 0.4× 602 0.5× 289 0.6× 108 4.6k
Jeanne A. Stuckey United States 51 7.1k 1.1× 2.0k 0.8× 1.8k 1.4× 240 0.2× 235 0.5× 142 9.9k
Claudio Pisano Italy 48 4.0k 0.6× 1.3k 0.5× 1.3k 1.0× 270 0.2× 327 0.6× 169 6.0k
Olga I. Lavrik Russia 41 6.4k 1.0× 2.5k 1.0× 661 0.5× 269 0.2× 290 0.6× 407 7.6k

Countries citing papers authored by John L. Nitiss

Since Specialization
Citations

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

Fields of papers citing papers by John L. Nitiss

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John L. Nitiss. 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 John L. Nitiss. The network helps show where John L. Nitiss may publish in the future.

Co-authorship network of co-authors of John L. Nitiss

This figure shows the co-authorship network connecting the top 25 collaborators of John L. Nitiss. A scholar is included among the top collaborators of John L. Nitiss 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 John L. Nitiss. John L. Nitiss 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.
Blower, Tim R., et al.. (2023). Using energy to go downhill—a genoprotective role for ATPase activity in DNA topoisomerase II. Nucleic Acids Research. 52(3). 1313–1324. 8 indexed citations
2.
Boot, Arnoud, Mo Liu, Willie Yu, et al.. (2022). Recurrent mutations in topoisomerase IIα cause a previously undescribed mutator phenotype in human cancers. Proceedings of the National Academy of Sciences. 119(4). 27 indexed citations
3.
Sun, Yilun, Lisa M. Jenkins, Yijun Su, et al.. (2020). A conserved SUMO pathway repairs topoisomerase DNA-protein cross-links by engaging ubiquitin-mediated proteasomal degradation. Science Advances. 6(46). 94 indexed citations
4.
Rogojina, Anna, Yilun Sun, James M. Berger, et al.. (2020). Trapped topoisomerase II initiates formation of de novo duplications via the nonhomologous end-joining pathway in yeast. Proceedings of the National Academy of Sciences. 117(43). 26876–26884. 20 indexed citations
5.
Sun, Yilun, et al.. (2017). Detection of Topoisomerase Covalent Complexes in Eukaryotic Cells. Methods in molecular biology. 1703. 283–299. 22 indexed citations
6.
Pommier, Yves, Yilun Sun, Shar-yin N. Huang, & John L. Nitiss. (2016). Roles of eukaryotic topoisomerases in transcription, replication and genomic stability. Nature Reviews Molecular Cell Biology. 17(11). 703–721. 654 indexed citations breakdown →
7.
Heo, Jinho, Jing Li, Sachin Katyal, et al.. (2015). TDP1 promotes assembly of non-homologous end joining protein complexes on DNA. DNA repair. 30. 28–37. 36 indexed citations
8.
Bhattarai, Bharat Raj, et al.. (2012). Chemical reactivity and microbicidal action of bethoxazin. Bioorganic & Medicinal Chemistry. 20(4). 1494–1501. 6 indexed citations
9.
Bahmed, Karim, Aman Seth, Karin C. Nitiss, & John L. Nitiss. (2010). End-processing during non-homologous end-joining: a role for exonuclease 1. Nucleic Acids Research. 39(3). 970–978. 18 indexed citations
10.
Walker, Jerrylaine V., Karin C. Nitiss, Lars H. Jensen, et al.. (2004). A Mutation in Human Topoisomerase II α Whose Expression Is Lethal in DNA Repair-deficient Yeast Cells. Journal of Biological Chemistry. 279(25). 25947–25954. 16 indexed citations
11.
Renodon‐Cornière, Axelle, et al.. (2003). Probing the Role of Linker Substituents in Bisdioxopiperazine Analogs for Activity against Wild-Type and Mutant Human Topoisomerase IIα. Molecular Pharmacology. 63(5). 1159–1168. 4 indexed citations
12.
Walker, Jerrylaine V., et al.. (2000). A Mutation in Yeast Topoisomerase II That Confers Hypersensitivity to Multiple Classes of Topoisomerase II Poisons. Journal of Biological Chemistry. 275(11). 7980–7987. 26 indexed citations
13.
Strumberg, Dirk, et al.. (1999). Mutation of a Conserved Serine Residue in a Quinolone-resistant Type II Topoisomerase Alters the Enzyme-DNA and Drug Interactions. Journal of Biological Chemistry. 274(11). 7292–7301. 20 indexed citations
14.
Nitiss, John L., et al.. (1996). Using Yeast to Understand Drugs that Target Topoisomerasesa. Annals of the New York Academy of Sciences. 803(1). 32–43. 25 indexed citations
15.
Chang, Yu‐Chen, Muraleedharan G. Nair, & John L. Nitiss. (1995). Metabolites of Daidzein and Genistein and Their Biological Activities. Journal of Natural Products. 58(12). 1901–1905. 68 indexed citations
16.
Elsea, Sarah H., Yuchu Hsiung, John L. Nitiss, & Neil Osheroff. (1995). A Yeast Type II Topoisomerase Selected for Resistance to Quinolones. Journal of Biological Chemistry. 270(4). 1913–1920. 75 indexed citations
17.
Nitiss, John L.. (1994). Roles of DNA Topoisomerases in Chromosomal Replication and Segregation. Advances in pharmacology. 29A. 103–134. 39 indexed citations
18.
Nitiss, John L.. (1994). Using yeast to study resistance to topoisomerase II-targeting drugs. Cancer Chemotherapy and Pharmacology. 34(S1). S6–S13. 41 indexed citations
19.
Nitiss, John L., et al.. (1994). Mutations in the gyrB domain of eukaryotic topoisomerase II can lead to partially dominant resistance to etoposide and amsacrine.. Molecular Pharmacology. 46(4). 773–777. 13 indexed citations
20.
Nitiss, John L., et al.. (1993). A temperature sensitive topoisomerase II allele confers temperature dependent drug resistance on amsacrine and etoposide: a genetic system for determining the targets of topoisomerase II inhibitors.. PubMed. 53(1). 89–93. 73 indexed citations

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