M.F. Davis

666 total citations
17 papers, 550 citations indexed

About

M.F. Davis is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, M.F. Davis has authored 17 papers receiving a total of 550 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 10 papers in Cell Biology and 4 papers in Physiology. Recurrent topics in M.F. Davis's work include Heme Oxygenase-1 and Carbon Monoxide (10 papers), Hemoglobin structure and function (10 papers) and Porphyrin Metabolism and Disorders (4 papers). M.F. Davis is often cited by papers focused on Heme Oxygenase-1 and Carbon Monoxide (10 papers), Hemoglobin structure and function (10 papers) and Porphyrin Metabolism and Disorders (4 papers). M.F. Davis collaborates with scholars based in United States, Italy and Germany. M.F. Davis's co-authors include Stefan Franzen, Vesna de Serrano, Steven A. Lommel, Jennifer Belyea, Tim L. Sit, Matthew K. Thompson, Benjamin G. Bobay, Sharon L. Campbell, Barry D. Howes and Francesco Nicoletti and has published in prestigious journals such as The Journal of Physical Chemistry B, Biochemistry and Free Radical Biology and Medicine.

In The Last Decade

M.F. Davis

15 papers receiving 529 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M.F. Davis United States	11	302	282	160	151	91	17	550
Di Qiu China	9	88 0.3×	7 0.0×	57 0.4×	31 0.2×	18 0.2×	23	311
N. H. Jensen Denmark	10	32 0.1×	11 0.0×	219 1.4×	206 1.4×	5 0.1×	15	501
Hirosato Kikuchi Japan	13	156 0.5×	17 0.1×	83 0.5×	69 0.5×		46	448
Yong Liang China	11	139 0.5×	7 0.0×	139 0.9×	77 0.5×	7 0.1×	26	406
Philip Tillman United States	8	228 0.8×	112 0.4×	12 0.1×	52 0.3×		11	395
George Barlow United States	12	80 0.3×	19 0.1×	8 0.1×	29 0.2×	23 0.3×	43	436
William L. Paul United States	9	70 0.2×	13 0.0×	45 0.3×	35 0.2×	3 0.0×	19	298
Helen Feilden United Kingdom	9	196 0.6×	3 0.0×	406 2.5×	176 1.2×	13 0.1×	11	829
Andrea N. Steward United Kingdom	10	83 0.3×	16 0.1×	123 0.8×	60 0.4×	1 0.0×	16	451
Robert Kruszyna United States	16	107 0.4×	108 0.4×	5 0.0×	34 0.2×	3 0.0×	27	925

Countries citing papers authored by M.F. Davis

Since Specialization

Citations

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

Fields of papers citing papers by M.F. Davis

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M.F. Davis

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

All Works

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17 of 17 papers shown

Davis, M.F., et al.. (2018). Wilde’s Other Worlds. 1–15.

Davis, M.F., Marilyn Ehrenshaft, Kalina Ranguelova, et al.. (2012). Detection of Ras GTPase protein radicals through immuno-spin trapping. Free Radical Biology and Medicine. 53(6). 1339–1345. 9 indexed citations

Davis, M.F., et al.. (2011). Regulation of Ras proteins by reactive nitrogen species. Free Radical Biology and Medicine. 51(3). 565–575. 20 indexed citations

Thompson, Matthew K., Stefan Franzen, M.F. Davis, Ryan C. Oliver, & Joanna K. Krueger. (2011). Dehaloperoxidase-Hemoglobin from Amphitrite ornata Is Primarily a Monomer in Solution. The Journal of Physical Chemistry B. 115(14). 4266–4272. 14 indexed citations

Thompson, Matthew K., M.F. Davis, Vesna de Serrano, et al.. (2010). Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function. Biophysical Journal. 99(5). 1586–1595. 51 indexed citations

Serrano, V.S. de, M.F. Davis, Qi Zhang, et al.. (2010). X-ray structure of the metcyano form of dehaloperoxidase fromAmphitrite ornata: evidence for photoreductive dissociation of the iron–cyanide bond. Acta Crystallographica Section D Biological Crystallography. 66(7). 770–782. 15 indexed citations

Davis, M.F., Benjamin G. Bobay, & Stefan Franzen. (2010). Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase−Hemoglobin from Amphitrite ornata^,. Biochemistry. 49(6). 1199–1206. 25 indexed citations

Davis, M.F., Hanna Gracz, Franck A. P. Vendeix, et al.. (2009). Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata. Biochemistry. 48(10). 2164–2172. 45 indexed citations

Nienhaus, Karin, et al.. (2008). Determinants of Substrate Internalization in the Distal Pocket of Dehaloperoxidase Hemoglobin of Amphitrite ornata. Biochemistry. 47(49). 12985–12994. 29 indexed citations

10.

Mikšovská, Jaroslava, et al.. (2008). Conformational Dynamics Associated with Photodissociation of CO from Dehaloperoxidase Studied Using Photoacoustic Calorimetry. Biochemistry. 47(44). 11510–11517. 8 indexed citations

11.

Serrano, Vesna de, et al.. (2007). X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned fromAmphitrite ornata. Acta Crystallographica Section D Biological Crystallography. 63(10). 1094–1101. 40 indexed citations

12.

Franzen, Stefan, et al.. (2006). Proximal Cavity, Distal Histidine, and Substrate Hydrogen-Bonding Mutations Modulate the Activity of Amphitrite ornata Dehaloperoxidase. Biochemistry. 45(30). 9085–9094. 42 indexed citations

13.

Belyea, Jennifer, et al.. (2005). Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding. Biochemistry. 44(48). 15637–15644. 65 indexed citations

14.

Davis, M.F., et al.. (1995). <title>Estimation of VOC emission rates from FTIR measurements and whole-air canister data</title>. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 2365. 230–242. 3 indexed citations

15.

Davis, M.F., et al.. (1995). <title>Evaluation of emissions from remedial activity at a former manufactured gas plant by open-path Fourier transform infrared spectroscopy</title>. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 2365. 253–261. 3 indexed citations

16.

Davis, M.F.. (1993). Writing the Mother inThe Notebooks of Malte Laurids Brigge:The Rhetoric of Abjection. The Germanic Review Literature Culture Theory. 68(4). 156–166. 2 indexed citations

17.

Davis, M.F., et al.. (1992). Lidocaine for the Prevention of Pain Due to Injection of Propofol. Anesthesia & Analgesia. 74(2). 246–249. 179 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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