Matthew O. Ross

2.3k total citations
31 papers, 1.2k citations indexed

About

Matthew O. Ross is a scholar working on Inorganic Chemistry, Molecular Biology and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Matthew O. Ross has authored 31 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Inorganic Chemistry, 11 papers in Molecular Biology and 5 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Matthew O. Ross's work include Metal-Catalyzed Oxygenation Mechanisms (12 papers), Microbial metabolism and enzyme function (5 papers) and Trace Elements in Health (4 papers). Matthew O. Ross is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (12 papers), Microbial metabolism and enzyme function (5 papers) and Trace Elements in Health (4 papers). Matthew O. Ross collaborates with scholars based in United States, United Kingdom and India. Matthew O. Ross's co-authors include Amy C. Rosenzweig, Brian M. Hoffman, Thomas J. Lawton, Barry D. Olafson, Fraser MacMillan, Alex Nisthal, Stephen L. Mayo, Robert G. Miller, Mark B. Bromberg and Timothy L. Stemmler and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Matthew O. Ross

30 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Matthew O. Ross United States 19 390 357 294 203 156 31 1.2k
Jing Huang China 21 280 0.7× 602 1.7× 372 1.3× 18 0.1× 164 1.1× 96 1.7k
Junyi Chen China 23 161 0.4× 271 0.8× 242 0.8× 47 0.2× 64 0.4× 100 2.0k
Mrinmoy Chakrabarti United States 19 625 1.6× 431 1.2× 290 1.0× 19 0.1× 344 2.2× 30 1.2k
Xiaoying Luo China 18 149 0.4× 340 1.0× 49 0.2× 115 0.6× 83 0.5× 32 994
Paloma Navarro Spain 20 87 0.2× 549 1.5× 416 1.4× 33 0.2× 94 0.6× 54 1.6k
Yuexiang Wang China 28 91 0.2× 959 2.7× 1.1k 3.7× 56 0.3× 304 1.9× 72 2.8k
Yanling Han China 21 25 0.1× 380 1.1× 424 1.4× 149 0.7× 400 2.6× 68 1.4k
Andong Zhao China 23 37 0.1× 922 2.6× 1.4k 4.7× 47 0.2× 103 0.7× 60 2.3k

Countries citing papers authored by Matthew O. Ross

Since Specialization
Citations

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

Fields of papers citing papers by Matthew O. Ross

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Matthew O. Ross. 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 Matthew O. Ross. The network helps show where Matthew O. Ross may publish in the future.

Co-authorship network of co-authors of Matthew O. Ross

This figure shows the co-authorship network connecting the top 25 collaborators of Matthew O. Ross. A scholar is included among the top collaborators of Matthew O. Ross 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 Matthew O. Ross. Matthew O. Ross 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.
Ross, Matthew O., et al.. (2025). Hydralazine Strikes Again-Anti-Neutrophil Cytoplasmic Antibody Positive Vasculitis With Hemorrhagic Bullae. American Journal of Respiratory and Critical Care Medicine. 211(Supplement_1). A3848–A3848.
2.
Stoian, Sebastian A., Nicholas S. Lees, Bryan T. Cronin, et al.. (2024). The Active-Site [4Fe-4S] Cluster in the Isoprenoid Biosynthesis Enzyme IspH Adopts Unexpected Redox States during Ligand Binding and Catalysis. Journal of the American Chemical Society. 146(6). 3926–3942. 3 indexed citations
3.
Ross, Matthew O., Yuan Xie, Chang Ye, et al.. (2024). PTPN2 copper-sensing relays copper level fluctuations into EGFR/CREB activation and associated CTR1 transcriptional repression. Nature Communications. 15(1). 6947–6947. 3 indexed citations
4.
Jodts, Richard J., et al.. (2021). Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuCSite by EPR and ENDOR Spectroscopies. Journal of the American Chemical Society. 143(37). 15358–15368. 35 indexed citations
5.
Kung, Mayfair C., et al.. (2020). Noncontact catalysis: Initiation of selective ethylbenzene oxidation by Au cluster-facilitated cyclooctene epoxidation. Science Advances. 6(5). eaax6637–eaax6637. 13 indexed citations
6.
Ross, Matthew O., Fraser MacMillan, Alex Nisthal, et al.. (2019). Particulate methane monooxygenase contains only mononuclear copper centers. Science. 364(6440). 566–570. 234 indexed citations
7.
Ross, Matthew O., Oriana S. Fisher, Matthew D. Krzyaniak, et al.. (2019). Formation and Electronic Structure of an Atypical CuA Site. Journal of the American Chemical Society. 141(11). 4678–4686. 17 indexed citations
8.
Fisher, Oriana S., et al.. (2019). PCuAC domains from methane-oxidizing bacteria use a histidine brace to bind copper. Journal of Biological Chemistry. 294(44). 16351–16363. 12 indexed citations
9.
Fisher, Oriana S., Grace E. Kenney, Matthew O. Ross, et al.. (2018). Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nature Communications. 9(1). 4276–4276. 50 indexed citations
10.
Purohit, Rahul, et al.. (2018). Cu + -specific CopB transporter: Revising P 1B -type ATPase classification. Proceedings of the National Academy of Sciences. 115(9). 2108–2113. 30 indexed citations
11.
Ro, Soo Y., Matthew O. Ross, Thomas J. Lawton, et al.. (2018). From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity. Journal of Biological Chemistry. 293(27). 10457–10465. 49 indexed citations
12.
Reed, Julian H., Qianhong Zhu, Saumen Chakraborty, et al.. (2017). Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism. Journal of the American Chemical Society. 139(35). 12209–12218. 32 indexed citations
13.
Smith, Aaron T., Matthew O. Ross, Brian M. Hoffman, & Amy C. Rosenzweig. (2016). Metal Selectivity of a Cd-, Co-, and Zn-Transporting P1B-type ATPase. Biochemistry. 56(1). 85–95. 18 indexed citations
14.
Ross, Matthew O. & Amy C. Rosenzweig. (2016). A tale of two methane monooxygenases. JBIC Journal of Biological Inorganic Chemistry. 22(2-3). 307–319. 204 indexed citations
15.
Petrik, Igor D., Roman Davydov, Matthew O. Ross, et al.. (2015). Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin. Journal of the American Chemical Society. 138(4). 1134–1137. 27 indexed citations
16.
Chakraborty, Saumen, Julian H. Reed, Matthew O. Ross, et al.. (2014). Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase. Angewandte Chemie International Edition. 53(9). 2417–2421. 34 indexed citations
17.
Magnusson, Marianne, Malcolm H. Pope, Leif Hasselquist, et al.. (1999). Cervical electromyographic activity during low-speed rear impact. European Spine Journal. 8(2). 118–125. 93 indexed citations
18.
McGuire, Dawn, Louis P. Garrison, Carmel Armon, et al.. (1996). Relationship of the Tufts Quantitative Neuromuscular Exam (TQNE) and the Sickness Impact Profile (SIP) in measuring progression of ALS. Neurology. 46(5). 1442–1442. 53 indexed citations
19.
Onishi, Hiroaki, Thoru Yamada, Takanori Saito, et al.. (1991). The effect of stimulus rate upon common peroneal, posterior tibial, and sural nerve somatosensory evoked potentials. Neurology. 41(12). 1972–1972. 23 indexed citations
20.
Machida, Masafumi, Thoru Yamada, Matthew O. Ross, Jun Kimura, & Patrick W. Hitchon. (1990). Effect of spinal cord ischemia on compound muscle action potentials and spinal evoked potentials following spinal cord stimulation in the dog.. PubMed. 3(4). 345–52. 15 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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