Brandon J. Reeder

3.4k total citations
60 papers, 2.6k citations indexed

About

Brandon J. Reeder is a scholar working on Cell Biology, Molecular Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, Brandon J. Reeder has authored 60 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Cell Biology, 45 papers in Molecular Biology and 12 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in Brandon J. Reeder's work include Hemoglobin structure and function (52 papers), Heme Oxygenase-1 and Carbon Monoxide (40 papers) and Neonatal Health and Biochemistry (12 papers). Brandon J. Reeder is often cited by papers focused on Hemoglobin structure and function (52 papers), Heme Oxygenase-1 and Carbon Monoxide (40 papers) and Neonatal Health and Biochemistry (12 papers). Brandon J. Reeder collaborates with scholars based in United Kingdom, Italy and Sweden. Brandon J. Reeder's co-authors include Michael T. Wilson, Dimitri A. Svistunenko, Chris E. Cooper, Leif Bülow, Robert C. Hider, Peter Nicholls, Radu Silaghi‐Dumitrescu, Martyn A. Sharpe, M.T. Wilson and Gary Silkstone and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Brandon J. Reeder

58 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Brandon J. Reeder United Kingdom	30	1.4k	1.3k	569	386	260	60	2.6k
Jesús Tejero United States	31	1.6k 1.2×	1.0k 0.7×	1.4k 2.5×	466 1.2×	125 0.5×	87	3.8k
Enika Nagababu United States	34	1.1k 0.8×	969 0.7×	1.6k 2.9×	387 1.0×	164 0.6×	59	3.8k
Jack H. Crawford United States	20	500 0.4×	727 0.5×	1.8k 3.2×	158 0.4×	312 1.2×	34	3.1k
Miriam M. Cortese‐Krott Germany	33	1.1k 0.8×	353 0.3×	1.3k 2.3×	149 0.4×	262 1.0×	84	3.9k
J.F. Koster Netherlands	36	1.3k 0.9×	523 0.4×	1.0k 1.8×	174 0.5×	438 1.7×	102	4.1k
Laura Castro Uruguay	23	1.9k 1.4×	306 0.2×	1.9k 3.3×	93 0.2×	190 0.7×	36	4.3k
C C Winterbourn New Zealand	24	970 0.7×	224 0.2×	570 1.0×	111 0.3×	127 0.5×	32	2.9k
Paolo Di Simplicio Italy	28	1.1k 0.8×	326 0.2×	431 0.8×	100 0.3×	156 0.6×	77	2.4k
Christopher D. Reiter United States	11	821 0.6×	957 0.7×	2.1k 3.7×	383 1.0×	171 0.7×	11	4.3k
C. Roger White United States	33	1.1k 0.8×	178 0.1×	1.4k 2.4×	92 0.2×	598 2.3×	73	4.0k

Countries citing papers authored by Brandon J. Reeder

Since Specialization

Citations

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

Fields of papers citing papers by Brandon J. Reeder

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Brandon J. Reeder. 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 Brandon J. Reeder. The network helps show where Brandon J. Reeder may publish in the future.

Co-authorship network of co-authors of Brandon J. Reeder

This figure shows the co-authorship network connecting the top 25 collaborators of Brandon J. Reeder. A scholar is included among the top collaborators of Brandon J. Reeder 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 Brandon J. Reeder. Brandon J. Reeder 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

Reeder, Brandon J.. (2023). Insights into the function of cytoglobin. Biochemical Society Transactions. 51(5). 1907–1919. 6 indexed citations

Rubio, María C., Carmen Pérez‐Rontomé, Estíbaliz Larrainzar, et al.. (2021). Three classes of hemoglobins are required for optimal vegetative and reproductive growth of Lotus japonicus: genetic and biochemical characterization of LjGlb2-1. Journal of Experimental Botany. 72(22). 7778–7791. 4 indexed citations

Cooper, Chris E., Gary Silkstone, Victoria Allen-Baume, et al.. (2020). Engineering hemoglobin to enable homogenous PEGylation without modifying protein functionality. Biomaterials Science. 8(14). 3896–3906. 16 indexed citations

Cooper, Chris E., Gary Silkstone, Natalie Syrett, et al.. (2018). Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute. Free Radical Biology and Medicine. 134. 106–118. 20 indexed citations

Vos, Marten H., Brandon J. Reeder, Fevzi Daldal, & Ursula Liebl. (2017). Ultrafast photochemistry of the bc₁complex. Physical Chemistry Chemical Physics. 19(9). 6807–6813. 3 indexed citations

Reeder, Brandon J., et al.. (2017). Effect of Enzymatic pre-treatment of microalgae extracts on their anti-tumor activity. Biomedical Journal. 40(6). 339–346. 16 indexed citations

Reeder, Brandon J.. (2016). Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease. Antioxidants and Redox Signaling. 26(14). 763–776. 32 indexed citations

Silkstone, Gary, Jenny Arnling Bååth, Peter Nicholls, et al.. (2016). The βLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute. Advances in experimental medicine and biology. 876. 455–460. 7 indexed citations

Silkstone, Gary, Michael T. Wilson, Leif Bülow, et al.. (2016). Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design. Biochemical Journal. 473(19). 3371–3383. 23 indexed citations

10.

Reeder, Brandon J., et al.. (2015). Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding. FEBS Letters. 589(4). 507–512. 31 indexed citations

11.

Battah, Sinan, et al.. (2014). Design, synthesis and biological evaluation of 5-aminolaevulinic acid/3-hydroxypyridinone conjugates as potential photodynamic therapeutical agents. Bioorganic & Medicinal Chemistry Letters. 25(3). 558–561. 16 indexed citations

12.

Reeder, Brandon J. & Michael A. Hough. (2014). The structure of a class 3 nonsymbiotic plant haemoglobin fromArabidopsis thalianareveals a novel N-terminal helical extension. Acta Crystallographica Section D Biological Crystallography. 70(5). 1411–1418. 10 indexed citations

13.

Franzen, Stefan, et al.. (2011). Decay of Compound ES in Dehaloperoxidase-Hemoglobin. Biophysical Journal. 100(3). 194a–194a.

14.

Reeder, Brandon J., Marie Grey, Radu Silaghi‐Dumitrescu, et al.. (2008). Tyrosine Residues as Redox Cofactors in Human Hemoglobin. Journal of Biological Chemistry. 283(45). 30780–30787. 107 indexed citations

15.

Reeder, Brandon J., Francesca Cutruzzolà, Maria Giulia Bigotti, Nicholas J. Watmough, & Michael T. Wilson. (2007). Histidine and not tyrosine is required for the Peroxide‐induced formation of haem to protein cross‐linked myoglobin. IUBMB Life. 59(8-9). 477–489. 20 indexed citations

16.

Wilson, Michael T. & Brandon J. Reeder. (2007). Oxygen‐binding haem proteins. Experimental Physiology. 93(1). 128–132. 76 indexed citations

17.

Reeder, Brandon J., Francesca Cutruzzolà, Maria Giulia Bigotti, Robert C. Hider, & Michael T. Wilson. (2007). Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology and Medicine. 44(3). 274–283. 59 indexed citations

18.

Silaghi‐Dumitrescu, Radu, Brandon J. Reeder, Peter Nicholls, Chris E. Cooper, & M.T. Wilson. (2007). Ferryl haem protonation gates peroxidatic reactivity in globins. Biochemical Journal. 403(3). 391–395. 69 indexed citations

19.

Svistunenko, Dimitri A., Michael J. Fryer, Peter Nicholls, et al.. (2002). Comparative Study of Tyrosine Radicals in Hemoglobin and Myoglobins Treated with Hydrogen Peroxide. Biophysical Journal. 83(5). 2845–2855. 79 indexed citations

20.

Reeder, Brandon J. & Michael T. Wilson. (2001). The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Free Radical Biology and Medicine. 30(11). 1311–1318. 88 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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