Martin T. Tuck

409 total citations
19 papers, 340 citations indexed

About

Martin T. Tuck is a scholar working on Molecular Biology, Biotechnology and Materials Chemistry. According to data from OpenAlex, Martin T. Tuck has authored 19 papers receiving a total of 340 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 2 papers in Biotechnology and 2 papers in Materials Chemistry. Recurrent topics in Martin T. Tuck's work include Cancer-related gene regulation (12 papers), RNA modifications and cancer (8 papers) and Epigenetics and DNA Methylation (6 papers). Martin T. Tuck is often cited by papers focused on Cancer-related gene regulation (12 papers), RNA modifications and cancer (8 papers) and Epigenetics and DNA Methylation (6 papers). Martin T. Tuck collaborates with scholars based in United States. Martin T. Tuck's co-authors include Woon Ki Paik, Richard A. Leach, Jamal Farooqui, Ray Cox, Tao Pan, Bruce Kelder, John J. Kopchick, Calvin James, Anthony T. Campagnoni and Myung‐Hee Kim and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Biochemical Journal.

In The Last Decade

Martin T. Tuck

19 papers receiving 335 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Martin T. Tuck United States 11 308 81 23 19 16 19 340
Francesca Meschi Italy 6 186 0.6× 107 1.3× 10 0.4× 2 0.1× 9 0.6× 7 212
Liangliang Li China 12 192 0.6× 54 0.7× 11 0.5× 6 0.3× 8 0.5× 18 304
Dongqin Xu China 7 221 0.7× 157 1.9× 15 0.7× 2 0.1× 12 0.8× 13 323
Huili Xia China 5 155 0.5× 17 0.2× 4 0.2× 5 0.3× 6 0.4× 8 267
Fanni Molnár United States 5 57 0.2× 31 0.4× 7 0.3× 9 0.5× 7 0.4× 13 143
Brendan J. Floyd United States 5 171 0.6× 11 0.1× 23 1.0× 8 0.4× 22 1.4× 7 219
Min‐Seok Kwon South Korea 7 169 0.5× 29 0.4× 3 0.1× 5 0.3× 10 0.6× 13 277
Kathy Fange Liu United States 11 428 1.4× 171 2.1× 15 0.7× 2 0.1× 5 0.3× 25 470
Qais Al‐Hadid United States 10 474 1.5× 27 0.3× 5 0.2× 5 0.3× 8 0.5× 11 504
María Teresa Borrello United Kingdom 11 196 0.6× 27 0.3× 9 0.4× 2 0.1× 24 1.5× 16 300

Countries citing papers authored by Martin T. Tuck

Since Specialization
Citations

This map shows the geographic impact of Martin T. Tuck'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 Martin T. Tuck with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Martin T. Tuck more than expected).

Fields of papers citing papers by Martin T. Tuck

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Martin T. Tuck. 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 Martin T. Tuck. The network helps show where Martin T. Tuck may publish in the future.

Co-authorship network of co-authors of Martin T. Tuck

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

All Works

19 of 19 papers shown
1.
Leach, Richard A. & Martin T. Tuck. (2001). Methionine depletion induces transcription of the mRNA (N6-adenosine)methyltransferase. The International Journal of Biochemistry & Cell Biology. 33(11). 1116–1128. 10 indexed citations
2.
Tuck, Martin T., et al.. (1999). Inhibition of 6-methyladenine formation decreases the translation efficiency of dihydrofolate reductase transcripts. The International Journal of Biochemistry & Cell Biology. 31(8). 837–851. 34 indexed citations
3.
Leach, Richard A., et al.. (1996). Internal 6-methyladenine residues increase the in vitro translation efficiency of dihydrofolate reductase messenger RNA. The International Journal of Biochemistry & Cell Biology. 28(7). 823–829. 29 indexed citations
4.
Tuck, Martin T., Calvin James, Bruce Kelder, & John J. Kopchick. (1996). Elevation of internal 6-methyladenine mRNA methyltransferase activity after cellular transformation. Cancer Letters. 103(1). 107–113. 18 indexed citations
5.
Rider, Lisa G., et al.. (1994). The relationship between the trimethylation of lysine 77 and cytochrome c metabolism in Saccharomyces cerevisiae. International Journal of Biochemistry. 26(5). 721–734. 7 indexed citations
6.
Tuck, Martin T.. (1992). The formation of internal 6-methyladenine residues in eucaryotic messenger rna. International Journal of Biochemistry. 24(3). 379–386. 45 indexed citations
7.
Tuck, Martin T.. (1992). Partial purification of a 6-methyladenine mRNA methyltransferase which modifies internal adenine residues. Biochemical Journal. 288(1). 233–240. 43 indexed citations
8.
Tuck, Martin T., et al.. (1991). Further investigations regarding the role of trimethyllysine for cytochrome c uptake into mitochondria. International Journal of Biochemistry. 23(7-8). 761–768. 8 indexed citations
9.
Tuck, Martin T., et al.. (1990). Analysis andin vitrolocalization of internal methylated adenine residues in dihydrofolate reductase mRNA. Nucleic Acids Research. 18(16). 4803–4808. 19 indexed citations
10.
Park, Kwang Sook, et al.. (1989). Site-specificity of histone HL methylation by two H1-specific protein-lysine N-methyltransferases from Euglena gracilis. International Journal of Biochemistry. 21(9). 1061–1070. 1 indexed citations
11.
Tuck, Martin T., et al.. (1987). Enzymatic methylation of in vitro synthesized apocytochrome c enhances its transport into mitochondria.. Journal of Biological Chemistry. 262(30). 14702–14708. 37 indexed citations
12.
Kim, S., Martin T. Tuck, Lap Ho, et al.. (1986). Myelin basic protein‐specific protein methylase I activity in shiverer mutant mouse brain. Journal of Neuroscience Research. 16(2). 357–365. 3 indexed citations
13.
Tuck, Martin T., Jamal Farooqui, & Woon Ki Paik. (1985). Two histone H1-specific protein-lysine N-methyltransferases from Euglena gracilis. Purification and characterization.. Journal of Biological Chemistry. 260(11). 7114–7121. 13 indexed citations
14.
Farooqui, Jamal, Martin T. Tuck, & Woon Ki Paik. (1985). Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c.. Journal of Biological Chemistry. 260(1). 537–545. 24 indexed citations
15.
Tuck, Martin T. & Woon Ki Paik. (1984). [25] S-adenosylmethionine: Protein (arginine) N-methyltransferase (protein methylase I) (wheat germ). Methods in enzymology on CD-ROM/Methods in enzymology. 106. 268–274. 4 indexed citations
16.
Kim, Sangduk, Martin T. Tuck, Myung‐Hee Kim, Anthony T. Campagnoni, & Woon Ki Paik. (1984). Studies on myelin basic protein-specific protein methylase I in various dysmyelinating mutant mice. Biochemical and Biophysical Research Communications. 123(2). 468–474. 21 indexed citations
17.
Tuck, Martin T. & Ray Cox. (1982). Ethionine inhibits in vivo methylation of nuclear proteins. Carcinogenesis. 3(4). 431–434. 7 indexed citations
18.
Tuck, Martin T. & Ray Cox. (1982). Ethionine causes the formation of NG-monoethylarginine in nuclear proteins from regenerating rat liver. Carcinogenesis. 3(12). 1477–1480. 4 indexed citations
19.
Cox, Ray & Martin T. Tuck. (1981). Alteration of methylation patterns in rat liver histones following administration of ethionine, a liver carcinogen.. PubMed. 41(4). 1253–6. 13 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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