Mark P. Roach

3.1k total citations · 1 hit paper
15 papers, 2.7k citations indexed

About

Mark P. Roach is a scholar working on Molecular Biology, Cell Biology and Inorganic Chemistry. According to data from OpenAlex, Mark P. Roach has authored 15 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 12 papers in Cell Biology and 7 papers in Inorganic Chemistry. Recurrent topics in Mark P. Roach's work include Hemoglobin structure and function (12 papers), Heme Oxygenase-1 and Carbon Monoxide (11 papers) and Metal-Catalyzed Oxygenation Mechanisms (7 papers). Mark P. Roach is often cited by papers focused on Hemoglobin structure and function (12 papers), Heme Oxygenase-1 and Carbon Monoxide (11 papers) and Metal-Catalyzed Oxygenation Mechanisms (7 papers). Mark P. Roach collaborates with scholars based in United States and Japan. Mark P. Roach's co-authors include John H. Dawson, Masanori Sono, Eric D. Coulter, Yoshihito Watanabe, Toshitaka Matsui, Shin‐ichi Ozaki, Melissa Thomas, Steven G. Boxer, Shin-ichi Ozaki and Stefan Franzen and has published in prestigious journals such as Chemical Reviews, Journal of the American Chemical Society and Accounts of Chemical Research.

In The Last Decade

Mark P. Roach

15 papers receiving 2.6k citations

Hit Papers

Heme-Containing Oxygenases 1996 2026 2006 2016 1996 500 1000 1.5k 2.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark P. Roach United States 12 1.7k 1.2k 794 615 402 15 2.7k
Eric D. Coulter United States 17 2.0k 1.2× 1.4k 1.1× 799 1.0× 466 0.8× 386 1.0× 25 3.1k
Roman Davydov United States 34 1.9k 1.1× 1.4k 1.1× 745 0.9× 729 1.2× 254 0.6× 85 3.1k
Thomas M. Makris United States 31 2.8k 1.7× 2.0k 1.6× 1.2k 1.5× 477 0.8× 596 1.5× 65 4.6k
Tomasz Borowski Poland 29 1.6k 1.0× 1.6k 1.3× 602 0.8× 186 0.3× 504 1.3× 83 3.2k
Thomas C. Pochapsky United States 34 819 0.5× 1.6k 1.3× 560 0.7× 329 0.5× 468 1.2× 108 4.3k
Shimrit Cohen Israel 17 1.9k 1.1× 879 0.7× 793 1.0× 187 0.3× 629 1.6× 22 2.7k
Shingo Nagano Japan 28 764 0.5× 1.1k 0.9× 290 0.4× 406 0.7× 236 0.6× 55 2.3k
Michael T. Green United States 39 3.8k 2.3× 1.9k 1.5× 1.6k 2.1× 485 0.8× 995 2.5× 66 5.4k
François Ogliaro Israel 25 2.5k 1.5× 901 0.7× 1.1k 1.4× 212 0.3× 1.0k 2.5× 52 3.4k
Ryu Makino Japan 30 629 0.4× 1.3k 1.1× 283 0.4× 768 1.2× 102 0.3× 58 2.5k

Countries citing papers authored by Mark P. Roach

Since Specialization
Citations

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

Fields of papers citing papers by Mark P. Roach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark P. Roach

This figure shows the co-authorship network connecting the top 25 collaborators of Mark P. Roach. A scholar is included among the top collaborators of Mark P. Roach 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 P. Roach. Mark P. Roach 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
2.
Ogo, Seiji, Ryo Yamahara, Mark P. Roach, et al.. (2002). Structural and Spectroscopic Features of a cis (Hydroxo)-FeIII-(Carboxylato) Configuration as an Active Site Model for Lipoxygenases. Inorganic Chemistry. 41(21). 5513–5520. 51 indexed citations
3.
4.
Ozaki, Shin‐ichi, Mark P. Roach, Toshitaka Matsui, & Yoshihito Watanabe. (2001). Investigations of the Roles of the Distal Heme Environment and the Proximal Heme Iron Ligand in Peroxide Activation by Heme Enzymes via Molecular Engineering of Myoglobin. Accounts of Chemical Research. 34(10). 818–825. 130 indexed citations
6.
Ozaki, Shin-ichi, Toshitaka Matsui, Mark P. Roach, & Yoshihito Watanabe. (2000). Rational molecular design of a catalytic site: engineering of catalytic functions to the myoglobin active site framework. Coordination Chemistry Reviews. 198(1). 39–59. 72 indexed citations
8.
Roach, Mark P., Shin‐ichi Ozaki, & Yoshihito Watanabe. (2000). Investigations of the Myoglobin Cavity Mutant H93G with Unnatural Imidazole Proximal Ligands as a Modular Peroxide O−O Bond Cleavage Model System. Biochemistry. 39(6). 1446–1454. 20 indexed citations
9.
Roach, Mark P., Masanori Sono, Ann H. Rux, et al.. (1999). Assignment of the Heme Axial Ligand(s) for the Ferric Myoglobin (H93G) and Heme Oxygenase (H25A) Cavity Mutants as Oxygen Donors Using Magnetic Circular Dichroism. Biochemistry. 38(23). 7601–7608. 44 indexed citations
11.
Franzen, Stefan, Mark P. Roach, Yung-Pin Chen, et al.. (1998). The Unusual Reactivities ofAmphitrite ornataDehaloperoxidase andNotomastus lobatusChloroperoxidase Do Not Arise from a Histidine Imidazolate Proximal Heme Iron Ligand. Journal of the American Chemical Society. 120(19). 4658–4661. 64 indexed citations
12.
Roach, Mark P., Stefan Franzen, Phillip S. Pang, et al.. (1997). Thiolate adducts of cavity mutant myoglobin H93G as models for cytochrome P450. Journal of Inorganic Biochemistry. 67(1-4). 134–134. 1 indexed citations
13.
Roach, Mark P., Yung Pin Chen, Sarah A. Woodin, et al.. (1997). Notomastus lobatus Chloroperoxidase and Amphitrite ornata Dehaloperoxidase Both Contain Histidine as Their Proximal Heme Iron Ligand. Biochemistry. 36(8). 2197–2202. 50 indexed citations
14.
Sono, Masanori, Mark P. Roach, Eric D. Coulter, & John H. Dawson. (1996). Heme-Containing Oxygenases. Chemical Reviews. 96(7). 2841–2888. 2093 indexed citations breakdown →
15.
Roach, Mark P. & Hendrick C. Van Ness. (1984). Excess thermodynamic functions for ternary systems. 10. HE and SE for ethanol/chloroform/1,4-dioxane at 50.degree.C. Journal of Chemical & Engineering Data. 29(2). 181–183. 10 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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