Cynthia L. Williamson

605 total citations
15 papers, 521 citations indexed

About

Cynthia L. Williamson is a scholar working on Molecular Biology, Plant Science and Materials Chemistry. According to data from OpenAlex, Cynthia L. Williamson has authored 15 papers receiving a total of 521 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 4 papers in Plant Science and 3 papers in Materials Chemistry. Recurrent topics in Cynthia L. Williamson's work include RNA modifications and cancer (3 papers), Polyamine Metabolism and Applications (3 papers) and Biochemical and Molecular Research (3 papers). Cynthia L. Williamson is often cited by papers focused on RNA modifications and cancer (3 papers), Polyamine Metabolism and Applications (3 papers) and Biochemical and Molecular Research (3 papers). Cynthia L. Williamson collaborates with scholars based in United States. Cynthia L. Williamson's co-authors include Robert D. Slocum, John M. Burke, William M. Tierney, František Kalousek, Kenneth R. Williams, Jan P. Kraus, Niraj M. Desai, Hao Yan, Stephen E. Alway and Erinne R. Dabkowski and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Cynthia L. Williamson

15 papers receiving 502 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Cynthia L. Williamson United States 12 393 103 83 67 56 15 521
Joachim M. Gerhold Estonia 13 624 1.6× 113 1.1× 130 1.6× 28 0.4× 60 1.1× 16 814
Rachel Navet Belgium 16 386 1.0× 52 0.5× 78 0.9× 48 0.7× 206 3.7× 21 654
Catherine E. Minogue United States 5 245 0.6× 72 0.7× 14 0.2× 29 0.4× 104 1.9× 5 388
Hasmukh V. Patel Canada 14 368 0.9× 14 0.1× 65 0.8× 72 1.1× 333 5.9× 26 585
Tara L. Archuleta United States 8 150 0.4× 17 0.2× 27 0.3× 20 0.3× 99 1.8× 9 387
Megan Morgan United Kingdom 7 488 1.2× 319 3.1× 20 0.2× 59 0.9× 33 0.6× 7 683
RoseAnn L. Shorey United States 14 399 1.0× 57 0.6× 13 0.2× 18 0.3× 56 1.0× 21 646
Anne-Cécile V. Bayne United States 7 260 0.7× 15 0.1× 42 0.5× 28 0.4× 77 1.4× 7 392
Tom Bender Switzerland 8 477 1.2× 26 0.3× 80 1.0× 39 0.6× 59 1.1× 8 573
Carlos Mújica‐Jiménez Mexico 11 234 0.6× 86 0.8× 59 0.7× 78 1.2× 12 0.2× 25 379

Countries citing papers authored by Cynthia L. Williamson

Since Specialization
Citations

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

Fields of papers citing papers by Cynthia L. Williamson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Cynthia L. Williamson

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

All Works

15 of 15 papers shown
1.
Ryan, Michael J., John R. Jackson, Hao Yan, et al.. (2010). Suppression of Oxidative Stress by Resveratrol After Isometric Contractions in Gastrocnemius Muscles of Aged Mice. The Journals of Gerontology Series A. 65A(8). 815–831. 92 indexed citations
2.
Hewitt, Matthew M., et al.. (2005). Effects of phosphate limitation on expression of genes involved in pyrimidine synthesis and salvaging in Arabidopsis. Plant Physiology and Biochemistry. 43(2). 91–99. 23 indexed citations
3.
Williamson, Cynthia L., et al.. (2003). PALA-mediated pyrimidine starvation increases expression of aspartate transcarbamoylase (pyrB) in Arabidopsis seedlings. Plant Physiology and Biochemistry. 41(8). 695–703. 11 indexed citations
4.
Slocum, Robert D., et al.. (2000). Purification and characterization of Arabidopsis ornithine transcarbamoylase (OTCase), a member of a distinct and evolutionarily-conserved group of plant OTCases. Plant Physiology and Biochemistry. 38(4). 279–288. 7 indexed citations
5.
Lake, Marc, Cynthia L. Williamson, & Robert D. Slocum. (1998). Molecular cloning and characterization of a UDP-glucose-4-epimerase gene (galE) and its expression in pea tissues. Plant Physiology and Biochemistry. 36(8). 555–562. 12 indexed citations
6.
Williamson, Cynthia L., Marc Lake, & Robert D. Slocum. (1996). Isolation and characterization of a cDNA encoding a pea ornithine transcarbamoylase (argF) and comparison with other transcarbamoylases. Plant Molecular Biology. 31(6). 1087–1092. 11 indexed citations
7.
Williamson, Cynthia L. & Robert D. Slocum. (1994). Molecular Cloning and Characterization of the pyrB1 and pyrB2 Genes Encoding Aspartate Transcarbamoylase in Pea (Pisum sativum L.). PLANT PHYSIOLOGY. 105(1). 377–384. 27 indexed citations
8.
Williamson, Cynthia L. & Robert D. Slocum. (1993). Characterization of an Aspartate Transcarbamoylase cDNA from Pea (Pisum sativum L.). PLANT PHYSIOLOGY. 102(3). 1055–1056. 5 indexed citations
9.
Williamson, Cynthia L. & Robert D. Slocum. (1992). Molecular Cloning and Evidence for Osmoregulation of the Δ1-Pyrroline-5-Carboxylate Reductase (proC) Gene in Pea (Pisum sativum L.). PLANT PHYSIOLOGY. 100(3). 1464–1470. 53 indexed citations
10.
Slocum, Robert D., et al.. (1990). Immunological Characterization of Plant Ornithine Transcarbamylases. PLANT PHYSIOLOGY. 92(4). 1205–1210. 10 indexed citations
11.
Williamson, Cynthia L., Niraj M. Desai, & John M. Burke. (1989). Compensatory mutations demonstrate that P8 and P6 are RNA secondary structure elements important for processing of a group I intron. Nucleic Acids Research. 17(2). 675–689. 42 indexed citations
12.
Williamson, Cynthia L., et al.. (1987). Site-directed mutagenesis of core sequence elements 9R', 9L, 9R, and 2 in self-splicing Tetrahymena pre-rRNA.. Journal of Biological Chemistry. 262(30). 14672–14682. 38 indexed citations
13.
Burke, John M., Kenneth D. Irvine, Kotaro Kaneko, et al.. (1986). Role of conserved sequence elements 9L and 2 in self-splicing of the Tetrahymena ribosomal RNA precursor. Cell. 45(2). 167–176. 73 indexed citations
14.
Kraus, Jan P., F A Firgaira, Jiří Novotný, et al.. (1986). Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.. Proceedings of the National Academy of Sciences. 83(21). 8049–8053. 53 indexed citations
15.
Kraus, Jan P., Peter E. Hodges, Cynthia L. Williamson, et al.. (1985). A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research. 13(3). 943–952. 64 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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