Martin D. Rees

1.9k total citations
28 papers, 1.6k citations indexed

About

Martin D. Rees is a scholar working on Immunology, Physiology and Molecular Biology. According to data from OpenAlex, Martin D. Rees has authored 28 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Immunology, 18 papers in Physiology and 8 papers in Molecular Biology. Recurrent topics in Martin D. Rees's work include Neutrophil, Myeloperoxidase and Oxidative Mechanisms (19 papers), Nitric Oxide and Endothelin Effects (18 papers) and Proteoglycans and glycosaminoglycans research (5 papers). Martin D. Rees is often cited by papers focused on Neutrophil, Myeloperoxidase and Oxidative Mechanisms (19 papers), Nitric Oxide and Endothelin Effects (18 papers) and Proteoglycans and glycosaminoglycans research (5 papers). Martin D. Rees collaborates with scholars based in Australia, Austria and United States. Martin D. Rees's co-authors include Michael J. Davies, Clare L. Hawkins, David I. Pattison, John M. Whitelock, Eleanor C. Kennett, Shane R. Thomas, Ernst Malle, Anthony J. Kettle, Christine Y. Chuang and Renato V. Iozzo and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Martin D. Rees

28 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Martin D. Rees Australia	18	687	542	430	265	110	28	1.6k
Helga Reicher Austria	25	350 0.5×	751 1.4×	267 0.6×	117 0.4×	127 1.2×	37	1.6k
Silvia Borrello Italy	27	416 0.6×	1.5k 2.7×	361 0.8×	195 0.7×	186 1.7×	46	2.5k
Denise C. Fernandes Brazil	23	230 0.3×	553 1.0×	369 0.9×	242 0.9×	78 0.7×	40	1.5k
Klaus‐Dietrich Kröncke Germany	22	249 0.4×	559 1.0×	662 1.5×	135 0.5×	346 3.1×	31	2.1k
Renata Colavitti Italy	17	431 0.6×	1.3k 2.5×	418 1.0×	181 0.7×	93 0.8×	21	2.3k
Mohammad Mahfuzul Haque United States	24	174 0.3×	641 1.2×	545 1.3×	227 0.9×	29 0.3×	78	1.5k
Ashok K. Srivastava Canada	28	242 0.4×	1.4k 2.5×	571 1.3×	197 0.7×	268 2.4×	87	2.7k
Costanzo Costamagna Italy	30	286 0.4×	872 1.6×	552 1.3×	89 0.3×	93 0.8×	51	2.5k
Anna Caselli Italy	23	305 0.4×	1.2k 2.2×	282 0.7×	214 0.8×	69 0.6×	51	1.9k
Mirosław Soszyński Poland	18	169 0.2×	508 0.9×	346 0.8×	109 0.4×	84 0.8×	55	1.2k

Countries citing papers authored by Martin D. Rees

Since Specialization

Citations

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

Fields of papers citing papers by Martin D. Rees

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin D. Rees

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

All Works

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20 of 20 papers shown

1.

Morris, Jonathan C., et al.. (2017). Regulation of the nitric oxide oxidase activity of myeloperoxidase by pharmacological agents. Biochemical Pharmacology. 135. 90–115. 22 indexed citations

2.

Dang, Lei, Enoch Chan, Elias N. Glaros, et al.. (2016). Endothelial-Transcytosed Myeloperoxidase Promotes Endothelial Dysfunction in an Oxidant Specific Manner: Novel Protective Actions of Thiocyanate and Nitrite. Free Radical Biology and Medicine. 100. S152–S153. 1 indexed citations

3.

Rees, Martin D. & Shane R. Thomas. (2015). Using Cell-substrate Impedance and Live Cell Imaging to Measure Real-time Changes in Cellular Adhesion and De-adhesion Induced by Matrix Modification. Journal of Visualized Experiments. 4 indexed citations

4.

Rees, Martin D. & Shane R. Thomas. (2015). Using Cell-substrate Impedance and Live Cell Imaging to Measure Real-time Changes in Cellular Adhesion and De-adhesion Induced by Matrix Modification. Journal of Visualized Experiments. 1 indexed citations

5.

Rees, Martin D., et al.. (2014). Mechanism and regulation of peroxidase-catalyzed nitric oxide consumption in physiological fluids: Critical protective actions of ascorbate and thiocyanate. Free Radical Biology and Medicine. 72. 91–103. 16 indexed citations

6.

Rees, Martin D., et al.. (2012). Targeted subendothelial matrix oxidation by myeloperoxidase triggers myosin II-dependent de-adhesion and alters signaling in endothelial cells. Free Radical Biology and Medicine. 53(12). 2344–2356. 31 indexed citations

7.

Rees, Martin D., Elias N. Glaros, Xiaosuo Wang, et al.. (2012). Human Indoleamine 2,3-Dioxygenase Is a Catalyst of Physiological Heme Peroxidase Reactions. Journal of Biological Chemistry. 288(3). 1548–1567. 46 indexed citations

8.

Meotti, Flávia Carla, Guy N. L. Jameson, Rufus Turner, et al.. (2011). Urate as a Physiological Substrate for Myeloperoxidase. Journal of Biological Chemistry. 286(15). 12901–12911. 105 indexed citations

9.

Kennett, Eleanor C., Martin D. Rees, Ernst Malle, et al.. (2010). Peroxynitrite modifies the structure and function of the extracellular matrix proteoglycan perlecan by reaction with both the protein core and the heparan sulfate chains. Free Radical Biology and Medicine. 49(2). 282–293. 41 indexed citations

10.

Chuang, Christine Y., Megan S. Lord, James Melrose, et al.. (2010). Heparan Sulfate-Dependent Signaling of Fibroblast Growth Factor 18 by Chondrocyte-Derived Perlecan. Biochemistry. 49(26). 5524–5532. 89 indexed citations

11.

Rees, Martin D., John M. Whitelock, Ernst Malle, et al.. (2009). Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan. Matrix Biology. 29(1). 63–73. 56 indexed citations

12.

Graham, Garry G., Anthony J. Kettle, Kieran F. Scott, et al.. (2009). Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations. Biochemical Pharmacology. 79(8). 1156–1164. 60 indexed citations

13.

Rees, Martin D., Eleanor C. Kennett, John M. Whitelock, & Michael J. Davies. (2008). Oxidative damage to extracellular matrix and its role in human pathologies. Free Radical Biology and Medicine. 44(12). 1973–2001. 178 indexed citations

14.

Davies, Michael J., Clare L. Hawkins, David I. Pattison, & Martin D. Rees. (2008). Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications. Antioxidants and Redox Signaling. 10(7). 1199–1234. 462 indexed citations

15.

Rees, Martin D., et al.. (2006). Degradation of extracellular matrix and its components by hypobromous acid. Biochemical Journal. 401(2). 587–596. 36 indexed citations

16.

Rees, Martin D. & Michael J. Davies. (2006). Heparan Sulfate Degradation via Reductive Homolysis of Its N-Chloro Derivatives. Journal of the American Chemical Society. 128(9). 3085–3097. 39 indexed citations

17.

Rees, Martin D., David I. Pattison, & Michael J. Davies. (2005). Oxidation of heparan sulphate by hypochlorite: role of N-chloro derivatives and dichloramine-dependent fragmentation. Biochemical Journal. 391(1). 125–134. 51 indexed citations

18.

Rees, Martin D., Clare L. Hawkins, & Michael J. Davies. (2004). Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates. Biochemical Journal. 381(1). 175–184. 85 indexed citations

19.

Rees, Martin D., Clare L. Hawkins, & Michael J. Davies. (2003). Hypochlorite-Mediated Fragmentation of Hyaluronan, Chondroitin Sulfates, and RelatedN-Acetyl Glycosamines: Evidence for Chloramide Intermediates, Free Radical Transfer Reactions, and Site-Specific Fragmentation. Journal of the American Chemical Society. 125(45). 13719–13733. 82 indexed citations

20.

Hawkins, Clare L., Martin D. Rees, & Michael J. Davies. (2001). Superoxide radicals can act synergistically with hypochlorite to induce damage to proteins. FEBS Letters. 510(1-2). 41–44. 38 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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