Barry D. Howes

2.7k total citations
82 papers, 2.3k citations indexed

About

Barry D. Howes is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Barry D. Howes has authored 82 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 29 papers in Cell Biology and 11 papers in Materials Chemistry. Recurrent topics in Barry D. Howes's work include Hemoglobin structure and function (29 papers), Photosynthetic Processes and Mechanisms (24 papers) and Porphyrin Metabolism and Disorders (15 papers). Barry D. Howes is often cited by papers focused on Hemoglobin structure and function (29 papers), Photosynthetic Processes and Mechanisms (24 papers) and Porphyrin Metabolism and Disorders (15 papers). Barry D. Howes collaborates with scholars based in Italy, United Kingdom and Australia. Barry D. Howes's co-authors include Giulietta Smulevich, Alessandro Feis, Federica Sinibaldi, Roberto Santucci, Chiara Indiani, Massimo Coletta, Andrew Smith, Francesco Nicoletti, Mario P. Marzocchi and David Lowe and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Accounts of Chemical Research.

In The Last Decade

Barry D. Howes

82 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Barry D. Howes Italy	28	1.4k	645	340	326	297	82	2.3k
Shigetoshi Aono Japan	29	1.6k 1.1×	1.1k 1.8×	604 1.8×	554 1.7×	370 1.2×	129	2.7k
Alessandro Coda Italy	32	2.1k 1.5×	896 1.4×	592 1.7×	122 0.4×	361 1.2×	80	3.2k
Kenton R. Rodgers United States	34	1.5k 1.1×	1.1k 1.7×	651 1.9×	372 1.1×	853 2.9×	92	3.5k
Sue A. Roberts United States	22	641 0.5×	359 0.6×	378 1.1×	216 0.7×	373 1.3×	53	1.8k
Charles P. Scholes United States	35	1.6k 1.2×	438 0.7×	836 2.5×	370 1.1×	709 2.4×	89	3.2k
Toshitaka Matsui Japan	34	1.8k 1.3×	1.3k 2.0×	530 1.6×	174 0.5×	821 2.8×	77	3.0k
Fred C. Hartman United States	28	2.1k 1.5×	427 0.7×	413 1.2×	266 0.8×	310 1.0×	80	2.7k
Alain Desbois France	21	605 0.4×	464 0.7×	253 0.7×	86 0.3×	199 0.7×	46	1.1k
Tsunenori Nozawa Japan	31	2.2k 1.6×	426 0.7×	673 2.0×	384 1.2×	235 0.8×	148	3.0k
Michael A. Hough United Kingdom	29	1.3k 0.9×	241 0.4×	678 2.0×	279 0.9×	495 1.7×	93	2.6k

Countries citing papers authored by Barry D. Howes

Since Specialization

Citations

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

Fields of papers citing papers by Barry D. Howes

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Barry D. Howes

This figure shows the co-authorship network connecting the top 25 collaborators of Barry D. Howes. A scholar is included among the top collaborators of Barry D. Howes 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 Barry D. Howes. Barry D. Howes 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

Howes, Barry D., et al.. (2019). Addition of sodium ascorbate to extend the shelf-life of tuna meat fish: A risk or a benefit for consumers?. Journal of Inorganic Biochemistry. 200. 110813–110813. 10 indexed citations

Ardini, Matteo, Barry D. Howes, Annarita Fiorillo, et al.. (2018). Study of manganese binding to the ferroxidase centre of human H-type ferritin. Journal of Inorganic Biochemistry. 182. 103–112. 15 indexed citations

Ciaccio, Chiara, Theo Battista, Manuela Cervelli, et al.. (2017). The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket. Journal of Inorganic Biochemistry. 169. 86–96. 21 indexed citations

Sinibaldi, Federica, Lisa Milazzo, Barry D. Howes, et al.. (2016). The key role played by charge in the interaction of cytochrome c with cardiolipin. JBIC Journal of Biological Inorganic Chemistry. 22(1). 19–29. 40 indexed citations

Cutone, Antimo, Barry D. Howes, A.E. Miele, et al.. (2016). Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding. Scientific Reports. 6(1). 31872–31872. 17 indexed citations

Howes, Barry D., Leonardo Boechi, Alberto Boffi, Darío A. Estrı́n, & Giulietta Smulevich. (2015). Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins. Advances in microbial physiology. 67. 85–126. 5 indexed citations

Adrover, Miquel, Barry D. Howes, Clara Iannuzzi, Giulietta Smulevich, & Annalisa Pastore. (2014). Anatomy of an iron-sulfur cluster scaffold protein: Understanding the determinants of [2Fe–2S] cluster stability on IscU. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853(6). 1448–1456. 27 indexed citations

Gow, Andrew J., et al.. (2014). Oxygen-Linked S-Nitrosation in Fish Myoglobins: A Cysteine-Specific Tertiary Allosteric Effect. PLoS ONE. 9(5). e97012–e97012. 8 indexed citations

Coppola, Daniela, Stefania Abbruzzetti, Francesco Nicoletti, et al.. (2012). ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. Molecular BioSystems. 8(12). 3295–3304. 10 indexed citations

10.

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

11.

Bonente, Giulia, Barry D. Howes, Stefano Caffarri, Giulietta Smulevich, & Roberto Bassi. (2007). Interactions between the Photosystem II Subunit PsbS and Xanthophylls Studied in Vivo and in Vitro. Journal of Biological Chemistry. 283(13). 8434–8445. 107 indexed citations

12.

Sinibaldi, Federica, Barry D. Howes, Giampiero Mei, et al.. (2005). Insights into the role of the histidines in the structure and stability of cytochrome c. JBIC Journal of Biological Inorganic Chemistry. 11(1). 52–62. 20 indexed citations

13.

Verde, Cinzia, Barry D. Howes, Maria Cristina De Rosa, et al.. (2004). Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes. Protein Science. 13(10). 2766–2781. 27 indexed citations

14.

Sinibaldi, Federica, Barry D. Howes, Laura Fiorucci, et al.. (2004). The 40s ?-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c. JBIC Journal of Biological Inorganic Chemistry. 9(8). 997–1006. 16 indexed citations

15.

Howes, Barry D., Nigel C. Veitch, Andrew Smith, Christopher White, & Giulietta Smulevich. (2001). Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221→Met mutant. Biochemical Journal. 353(2). 181–181. 16 indexed citations

16.

Howes, Barry D., et al.. (2001). Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme C. Biopolymers. 62(5). 261–267. 9 indexed citations

17.

Howes, Barry D., Alessandro Feis, Chiara Indiani, M.P. Marzocchi, & Giulietta Smulevich. (2000). Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature. JBIC Journal of Biological Inorganic Chemistry. 5(2). 227–235. 33 indexed citations

18.

Indiani, Chiara, Alessandro Feis, Barry D. Howes, Mario P. Marzocchi, & Giulietta Smulevich. (2000). Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state. Journal of Inorganic Biochemistry. 79(1-4). 269–274. 21 indexed citations

19.

Howes, Barry D., Christine Bruun Schiødt, Karen G. Welinder, et al.. (1999). The Quantum Mixed-Spin Heme State of Barley Peroxidase:A Paradigm for Class III Peroxidases. Biophysical Journal. 77(1). 478–492. 68 indexed citations

20.

Bray, Robert C., Brian Bennett, J. F. Burke, et al.. (1996). Recent studies on xanthine oxidase and related enzymes. Biochemical Society Transactions. 24(1). 99–105. 21 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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