Mark T. Martin

604 total citations
21 papers, 490 citations indexed

About

Mark T. Martin is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Oncology. According to data from OpenAlex, Mark T. Martin has authored 21 papers receiving a total of 490 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 5 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Oncology. Recurrent topics in Mark T. Martin's work include Monoclonal and Polyclonal Antibodies Research (5 papers), Advanced biosensing and bioanalysis techniques (4 papers) and Protein purification and stability (4 papers). Mark T. Martin is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (5 papers), Advanced biosensing and bioanalysis techniques (4 papers) and Protein purification and stability (4 papers). Mark T. Martin collaborates with scholars based in United States and United Kingdom. Mark T. Martin's co-authors include Rosa I. Sánchez, John G. Brushmiller, Francis A. Jacobs, Andrew D. Napper, Jonathan K. Leland, David A. Yost, James Riordan, Anthony R. Rees, Robert H. Shapiro and Peter G. Schultz and has published in prestigious journals such as Journal of the American Chemical Society, Analytical Chemistry and Biochemistry.

In The Last Decade

Mark T. Martin

21 papers receiving 462 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark T. Martin United States 12 307 89 87 86 77 21 490
Lutz Haalck Germany 14 494 1.6× 16 0.2× 31 0.4× 74 0.9× 58 0.8× 24 662
Magnus Glad Sweden 10 328 1.1× 31 0.3× 80 0.9× 73 0.8× 294 3.8× 11 920
Mats‐Olle Månsson Sweden 12 308 1.0× 24 0.3× 24 0.3× 70 0.8× 80 1.0× 15 481
Aaron Watts United Kingdom 4 261 0.9× 15 0.2× 20 0.2× 17 0.2× 26 0.3× 7 493
Hana Pivoňková Czechia 19 795 2.6× 155 1.7× 14 0.2× 131 1.5× 105 1.4× 37 932
Nahum Lee South Korea 12 302 1.0× 14 0.2× 10 0.1× 83 1.0× 109 1.4× 16 482
David M. Charbonneau Canada 10 601 2.0× 16 0.2× 19 0.2× 52 0.6× 118 1.5× 14 740
Junlin He China 18 709 2.3× 31 0.3× 8 0.1× 60 0.7× 107 1.4× 59 863
Jean-François Neault Canada 7 405 1.3× 21 0.2× 13 0.1× 19 0.2× 58 0.8× 7 577

Countries citing papers authored by Mark T. Martin

Since Specialization
Citations

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

Fields of papers citing papers by Mark T. Martin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Mark T. Martin. A scholar is included among the top collaborators of Mark T. Martin 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 Mark T. Martin. Mark T. Martin 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.
Martin, Mark T.. (1996). Commercially valuable catalytic antibodies: the life to come. Drug Discovery Today. 1(6). 239–247. 6 indexed citations
2.
Martin, Mark T., et al.. (1996). Enzyme-Triggered Formation of Electrochemiluminescent Ruthenium Complexes. Analytical Biochemistry. 236(2). 344–347. 14 indexed citations
3.
Sánchez, Rosa I., et al.. (1996). Electrochemiluminescence-Based Quantitation of Classical Clinical Chemistry Analytes. Analytical Chemistry. 68(8). 1298–1302. 94 indexed citations
4.
Fischer, Alan B., et al.. (1996). Reversible and irreversible immobilization of enzymes on graphite fibrilsTM. Journal of Molecular Recognition. 9(5-6). 383–388. 10 indexed citations
5.
Martin, Mark T., et al.. (1996). Light Emission from Ruthenium-Labeled Penicillins Signaling Their Hydrolysis by β-Lactamase. Journal of the American Chemical Society. 118(38). 9198–9199. 22 indexed citations
6.
Titmas, Richard C., Thelma S. Angeles, Renee Sugasawara, et al.. (1994). Aspects of antibody-catalyzed primary amide hydrolysis. Applied Biochemistry and Biotechnology. 47(2-3). 277–292. 5 indexed citations
7.
Martin, Mark T., Thelma S. Angeles, Renee Sugasawara, et al.. (1994). Antibody-Catalyzed Hydrolysis of an Unsubstituted Amide. Journal of the American Chemical Society. 116(15). 6508–6512. 53 indexed citations
8.
Angeles, Thelma S., Rodger Smith, Michael J. Darsley, et al.. (1993). Isoabzymes: Structurally and mechanistically similar catalytic antibodies from the same immunization. Biochemistry. 32(45). 12128–12135. 30 indexed citations
9.
Martin, Mark T., Andrew D. Napper, Peter G. Schultz, & Anthony R. Rees. (1991). Mechanistic studies of a tyrosine-dependent catalytic antibody. Biochemistry. 30(40). 9757–9761. 30 indexed citations
10.
Blackburn, Gary F., David B. Talley, Charles N. Durfor, et al.. (1990). Potentiometric biosensor employing catalytic antibodies as the molecular recognition element. Analytical Chemistry. 62(20). 2211–2216. 33 indexed citations
11.
Martin, Mark T., Barton Holmquist, & James Riordan. (1989). An angiotensin converting enzyme inhibitor is a tight-binding slow substrate of carboxypeptidase A. Journal of Inorganic Biochemistry. 36(1). 39–50. 11 indexed citations
12.
Martin, Mark T., Barton Holmquist, & James Riordan. (1989). Effects of mechanism-based reversible inhibitors on the metal environment of cobalt(II)carboxypeptidase A: An electronic spectral study. Journal of Inorganic Biochemistry. 36(1). 27–37. 1 indexed citations
13.
Martin, Mark T. & Robert H. Shapiro. (1988). [28] Atomic absorption spectrometry of magnesium. Methods in enzymology on CD-ROM/Methods in enzymology. 158. 365–370. 17 indexed citations
14.
Shapiro, Robert H. & Mark T. Martin. (1988). [25] Determination of cobalt by atomic absorption spectrometry. Methods in enzymology on CD-ROM/Methods in enzymology. 158. 344–351. 4 indexed citations
15.
Martin, Mark T.. (1988). [4] Metal-free chromatographic media. Methods in enzymology on CD-ROM/Methods in enzymology. 158. 15–21. 6 indexed citations
16.
Bicknell, Roy, Barton Holmquist, Frank S. Lee, Mark T. Martin, & James Riordan. (1987). Electronic spectroscopy of cobalt angiotensin converting enzyme and its inhibitor complexes. Biochemistry. 26(23). 7291–7297. 30 indexed citations
17.
Martin, Mark T., Bert L. Vallée, & James Riordan. (1987). Fluorescent inhibitor probes of enzyme active site conformation: Anion binding to angiotensin-converting enzyme. Analytical Biochemistry. 161(2). 341–347. 3 indexed citations
18.
Riordan, James, J. Wade Harper, & Mark T. Martin. (1986). The Catalytic Mechanism of Angiotensin Converting Enzyme and Related Zinc Enzymes. Journal of Cardiovascular Pharmacology. 8. S29–34. 5 indexed citations
19.
Martin, Mark T., Francis A. Jacobs, & John G. Brushmiller. (1984). Identification of Copper- and Zinc-Binding Ligands in Human and Bovine Milk. Journal of Nutrition. 114(5). 869–879. 29 indexed citations
20.
Martin, Mark T., et al.. (1981). Detection of low molecular weight copper(II) and zinc(II) binding ligands in ultrafiltered milks—the citrate connection. Journal of Inorganic Biochemistry. 15(1). 55–65. 36 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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