M.L. Dodson

2.0k total citations
30 papers, 1.7k citations indexed

About

M.L. Dodson is a scholar working on Molecular Biology, Genetics and Ecology. According to data from OpenAlex, M.L. Dodson has authored 30 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 11 papers in Genetics and 5 papers in Ecology. Recurrent topics in M.L. Dodson's work include DNA Repair Mechanisms (14 papers), DNA and Nucleic Acid Chemistry (14 papers) and Bacterial Genetics and Biotechnology (9 papers). M.L. Dodson is often cited by papers focused on DNA Repair Mechanisms (14 papers), DNA and Nucleic Acid Chemistry (14 papers) and Bacterial Genetics and Biotechnology (9 papers). M.L. Dodson collaborates with scholars based in United States, Russia and Iran. M.L. Dodson's co-authors include R. Stephen Lloyd, Amanda K. McCullough, Mark L. Michaels, M. Mandel, Janet Bergendahl, Robert D. Schrock, Katherine Atkins Latham, Bin Sun, Andrew Kurtz and Orlando D. Schärer and has published in prestigious journals such as Journal of Biological Chemistry, Annual Review of Biochemistry and Journal of Molecular Biology.

In The Last Decade

M.L. Dodson

29 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.L. Dodson United States 18 1.5k 329 234 154 141 30 1.7k
Elizabeth J. Grayhack United States 28 2.9k 1.9× 330 1.0× 187 0.8× 139 0.9× 187 1.3× 43 3.2k
Dale W. Mosbaugh United States 29 2.0k 1.3× 480 1.5× 363 1.6× 179 1.2× 104 0.7× 48 2.2k
Alessandra M. Albertini Italy 22 1.5k 1.0× 569 1.7× 241 1.0× 80 0.5× 273 1.9× 32 1.9k
Mary Edmonds United States 23 2.1k 1.4× 232 0.7× 174 0.7× 76 0.5× 251 1.8× 48 2.5k
Hosahalli S. Subramanya India 12 1.6k 1.0× 500 1.5× 199 0.9× 73 0.5× 174 1.2× 19 1.8k
Alexey A. Bogdanov Russia 31 2.4k 1.6× 562 1.7× 297 1.3× 94 0.6× 132 0.9× 132 2.7k
David Kowalski United States 29 2.3k 1.5× 525 1.6× 193 0.8× 113 0.7× 381 2.7× 50 2.5k
Fumiaki Yamao Japan 29 1.7k 1.1× 390 1.2× 410 1.8× 43 0.3× 215 1.5× 60 2.1k
Mukund J. Modak United States 27 1.3k 0.8× 288 0.9× 111 0.5× 46 0.3× 78 0.6× 85 1.9k
Akira Wada Japan 28 2.0k 1.3× 1.1k 3.4× 514 2.2× 97 0.6× 102 0.7× 62 2.6k

Countries citing papers authored by M.L. Dodson

Since Specialization
Citations

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

Fields of papers citing papers by M.L. Dodson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M.L. Dodson

This figure shows the co-authorship network connecting the top 25 collaborators of M.L. Dodson. A scholar is included among the top collaborators of M.L. Dodson 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 M.L. Dodson. M.L. Dodson 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.
Golan, G., Dmitry O. Zharkov, Arthur P. Grollman, et al.. (2006). Structure of T4 Pyrimidine Dimer Glycosylase in a Reduced Imine Covalent Complex with Abasic Site-containing DNA. Journal of Molecular Biology. 362(2). 241–258. 24 indexed citations
2.
Rajagopalan, Lavanya, et al.. (2004). Role of His-16 in Turnover of T4 Pyrimidine Dimer Glycosylase. Journal of Biological Chemistry. 279(5). 3348–3353. 4 indexed citations
3.
Manuel, Raymond C., Kenichi Hitomi, A.S. Arvai, et al.. (2004). Reaction Intermediates in the Catalytic Mechanism of Escherichia coli MutY DNA Glycosylase. Journal of Biological Chemistry. 279(45). 46930–46939. 46 indexed citations
4.
5.
Dodson, M.L., Andrew Kurtz, & R. Stephen Lloyd. (2002). T4 Endonuclease V: Use of NMR and Borohydride Trapping to Provide Evidence for Covalent Enzyme–Substrate Imine Intermediate. Methods in enzymology on CD-ROM/Methods in enzymology. 354. 202–207. 6 indexed citations
6.
Jaruga, Paweł, et al.. (2002). Determination of Active Site Residues in Escherichia coli Endonuclease VIII. Journal of Biological Chemistry. 277(4). 2938–2944. 42 indexed citations
7.
Dodson, M.L. & R. Stephen Lloyd. (2001). Backbone dynamics of DNA containing 8-oxoguanine: importance for substrate recognition by base excision repair glycosylases. Mutation Research/DNA Repair. 487(3-4). 93–108. 7 indexed citations
8.
McCullough, Amanda K., et al.. (2000). The Reaction Mechanism of DNA Glycosylase/AP Lyases at Abasic Sites. Biochemistry. 40(2). 561–568. 54 indexed citations
9.
McCullough, Amanda K., Simon G. Nyaga, Thomas G. Wood, et al.. (1998). Characterization of a Novel cis-synandtrans-syn-IIPyrimidine Dimer Glycosylase/AP Lyase from a Eukaryotic Algal Virus, Paramecium bursaria chlorellaVirus-1. Journal of Biological Chemistry. 273(21). 13136–13142. 45 indexed citations
10.
McCullough, Amanda K., M.L. Dodson, Orlando D. Schärer, & R. Stephen Lloyd. (1997). The Role of Base Flipping in Damage Recognition and Catalysis by T4 Endonuclease V. Journal of Biological Chemistry. 272(43). 27210–27217. 61 indexed citations
11.
Sun, Bin, Katherine Atkins Latham, M.L. Dodson, & R. Stephen Lloyd. (1995). Studies on the Catalytic Mechanism of Five DNA Glycosylases. Journal of Biological Chemistry. 270(33). 19501–19508. 130 indexed citations
12.
Manuel, Raymond C., Katherine Atkins Latham, M.L. Dodson, & R. Stephen Lloyd. (1995). Involvement of Glutamic Acid 23 in the Catalytic Mechanism of T4 Endonuclease V. Journal of Biological Chemistry. 270(6). 2652–2661. 33 indexed citations
13.
Piersen, C E, Melissa Prince, Mary Lou Augustine, M.L. Dodson, & R. Stephen Lloyd. (1995). Purification and Cloning of Micrococcus luteus Ultraviolet Endonuclease, an N-Glycosylase/Abasic Lyase That Proceeds via an Imino Enzyme-DNA Intermediate. Journal of Biological Chemistry. 270(40). 23475–23484. 55 indexed citations
14.
Dodson, M.L., Robert D. Schrock, & R. Stephen Lloyd. (1993). Evidence for an imino intermediate in the T4 endonuclease V reaction. Biochemistry. 32(32). 8284–8290. 129 indexed citations
15.
Augustine, Mary Lou, Robert W. Hamilton, M.L. Dodson, & R. Stephen Lloyd. (1991). Oligonucleotide site directed mutagenesis of all histidine residues within the T4 endonuclease V gene: role in enzyme nontarget DNA binding. Biochemistry. 30(32). 8052–8059. 13 indexed citations
16.
Dodson, M.L., Melissa Prince, W.F. Anderson, & R. Stephen Lloyd. (1991). Site-directed deletion mutagenesis within the T4 endonuclease V gene: dispensable sequences within putative loop regions. Mutation Research/DNA Repair. 255(1). 19–29. 2 indexed citations
17.
Dodson, M.L. & R. Stephen Lloyd. (1989). Structure-function studies of the T4 endonuclease V repair enzyme. Mutation Research/DNA Repair. 218(2). 49–65. 62 indexed citations
18.
19.
Bowen, James M., et al.. (1976). Implications of humoral antibody in mice and humans to breast tumor and mouse mammary tumor virus-associated antigens.. PubMed. 36(2 pt 2). 759–64. 24 indexed citations
20.
Dodson, M.L., Roger R. Hewitt, & M. Mandel. (1972). THE NATURE OF ULTRAVIOLET LIGHT‐INDUCED STRAND BREAKAGE IN DNA CONTAINING BROMOURACIL. Photochemistry and Photobiology. 16(1). 15–25. 16 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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