Eduardo Howard

1.7k total citations
41 papers, 1.4k citations indexed

About

Eduardo Howard is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Eduardo Howard has authored 41 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 13 papers in Materials Chemistry and 9 papers in Cell Biology. Recurrent topics in Eduardo Howard's work include Enzyme Structure and Function (12 papers), Protein Structure and Dynamics (9 papers) and Aldose Reductase and Taurine (9 papers). Eduardo Howard is often cited by papers focused on Enzyme Structure and Function (12 papers), Protein Structure and Dynamics (9 papers) and Aldose Reductase and Taurine (9 papers). Eduardo Howard collaborates with scholars based in France, Argentina and United States. Eduardo Howard's co-authors include A. Podjarny, J. Raúl Grigera, A. Mitschler, Patrick Barth, Bernard Chevrier, M. Van Zandt, Valérie Lamour, Raúl E. Cachau, Martha C. Bohn and Ursula Vielkind and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Angewandte Chemie International Edition and Scientific Reports.

In The Last Decade

Eduardo Howard

39 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Eduardo Howard France	19	676	408	222	220	184	41	1.4k
Christopher R. Pudney United Kingdom	21	969 1.4×	344 0.8×	166 0.7×	146 0.7×	135 0.7×	61	1.5k
Federico I. Rosell Canada	25	1.4k 2.1×	323 0.8×	394 1.8×	116 0.5×	177 1.0×	44	2.1k
B. Wieb van der Meer United States	19	1.4k 2.0×	298 0.7×	158 0.7×	193 0.9×	199 1.1×	30	2.2k
Spencer Anderson United States	17	984 1.5×	294 0.7×	182 0.8×	91 0.4×	103 0.6×	20	1.4k
Isabella Daidone Italy	27	1.4k 2.1×	499 1.2×	176 0.8×	247 1.1×	244 1.3×	106	2.1k
Gianantonio Battistuzzi Italy	32	1.7k 2.5×	330 0.8×	391 1.8×	123 0.6×	132 0.7×	143	3.2k
James A. McCray United States	18	943 1.4×	460 1.1×	226 1.0×	265 1.2×	128 0.7×	28	1.7k
Knut Teigen Norway	21	1.6k 2.3×	228 0.6×	158 0.7×	173 0.8×	144 0.8×	49	2.3k
Norma M. Allewell United States	30	2.0k 3.0×	910 2.2×	261 1.2×	109 0.5×	165 0.9×	104	2.8k
Marvin L. Hackert United States	26	1.8k 2.6×	715 1.8×	375 1.7×	188 0.9×	127 0.7×	74	2.7k

Countries citing papers authored by Eduardo Howard

Since Specialization

Citations

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

Fields of papers citing papers by Eduardo Howard

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eduardo Howard. 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 Eduardo Howard. The network helps show where Eduardo Howard may publish in the future.

Co-authorship network of co-authors of Eduardo Howard

This figure shows the co-authorship network connecting the top 25 collaborators of Eduardo Howard. A scholar is included among the top collaborators of Eduardo Howard 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 Eduardo Howard. Eduardo Howard 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

Alvarez, H. Ariel, et al.. (2020). Molecular dynamics simulation of the heart type fatty acid binding protein in a crystal environment. Journal of Biomolecular Structure and Dynamics. 39(10). 3459–3468. 2 indexed citations

Batisse, Claire, Arnaud Vanden Broeck, Roland H. Stote, et al.. (2018). Post-translational modifications in DNA topoisomerase 2α highlight the role of a eukaryote-specific residue in the ATPase domain. Scientific Reports. 8(1). 9272–9272. 26 indexed citations

Noguera, Martín E., Gerardo Ferrer‐Sueta, Eduardo Howard, et al.. (2017). Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants. Scientific Reports. 7(1). 42343–42343. 9 indexed citations

Howard, Eduardo, Benoı̂t Guillot, Matthew P. Blakeley, et al.. (2016). High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution. IUCrJ. 3(2). 115–126. 26 indexed citations

Zhao, Yuguang, Raúl E. Cachau, A. Cousido-Siah, et al.. (2015). New insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MM. Acta Crystallographica Section D Biological Crystallography. 71(7). 1455–1470. 26 indexed citations

Zandt, M.C. Van, Darren L. Whitehouse, Adam Gołȩbiowski, et al.. (2013). Discovery of (R)-2-Amino-6-borono-2-(2-(piperidin-1-yl)ethyl)hexanoic Acid and Congeners As Highly Potent Inhibitors of Human Arginases I and II for Treatment of Myocardial Reperfusion Injury. Journal of Medicinal Chemistry. 56(6). 2568–2580. 67 indexed citations

Howard, Eduardo, Matthew P. Blakeley, Michael Haertlein, et al.. (2011). Neutron structure of type‐III antifreeze protein allows the reconstruction of AFP–ice interface. Journal of Molecular Recognition. 24(4). 724–732. 59 indexed citations

Salvay, Andrés G., Frank Gabel, Bernard Pucci, et al.. (2010). Structure and Interactions of Fish Type III Antifreeze Protein in Solution. Biophysical Journal. 99(2). 609–618. 18 indexed citations

Blakeley, Matthew P., Susana C. M. Teixeira, Isabelle Hazemann, et al.. (2010). Neutron macromolecular crystallography with LADI-III. Acta Crystallographica Section D Biological Crystallography. 66(11). 1198–1205. 71 indexed citations

10.

Blakeley, Matthew P., Eduardo Howard, Isabelle Hazemann, et al.. (2010). Incorporation of methyl-protonated valine and leucine residues into deuterated ocean pout type III antifreeze protein: expression, crystallization and preliminary neutron diffraction studies. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(6). 665–669. 8 indexed citations

11.

Blakeley, Matthew P., Eduardo Howard, Isabelle Hazemann, et al.. (2009). Perdeuteration, purification, crystallization and preliminary neutron diffraction of an ocean pout type III antifreeze protein. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(4). 406–409. 18 indexed citations

12.

Salvay, Andrés G., Javier Santos, & Eduardo Howard. (2007). Electro-Optical Properties Characterization of Fish Type III Antifreeze Protein. Journal of Biological Physics. 33(5-6). 389–397. 9 indexed citations

13.

Zandt, M.C. Van, E. Sibley, Brenda R. Flam, et al.. (2004). Design and synthesis of highly potent and selective (2-arylcarbamoyl-phenoxy)-acetic acid inhibitors of aldose reductase for treatment of chronic diabetic complications. Bioorganic & Medicinal Chemistry. 12(21). 5661–5675. 44 indexed citations

14.

Howard, Eduardo, Ruslan Sanishvili, Raúl E. Cachau, et al.. (2004). Ultrahigh resolution drug design I: Details of interactions in human aldose reductase–inhibitor complex at 0.66 Å. Proteins Structure Function and Bioinformatics. 55(4). 792–804. 270 indexed citations

15.

Calderone, V., Bernard Chevrier, M. Van Zandt, et al.. (2000). The structure of human aldose reductase bound to the inhibitor IDD384. Acta Crystallographica Section D Biological Crystallography. 56(5). 536–540. 33 indexed citations

16.

Cachau, Raúl E., Eduardo Howard, Patrick Barth, et al.. (2000). Model of the catalytic mechanism of human aldose reductase based on quantum chemical calculations. Journal de Physique IV (Proceedings). 10(PR10). Pr10–3. 14 indexed citations

17.

Lamour, Valérie, Patrick Barth, Hélène Rogniaux, et al.. (1999). Production of crystals of human aldose reductase with very high resolution diffraction. Acta Crystallographica Section D Biological Crystallography. 55(3). 721–723. 29 indexed citations

18.

Marañón, Julio, et al.. (1996). The Influence of Charge Calculation on Molecular Dynamics Simulation of Adenine in Water. Molecular Simulation. 18(1-2). 101–113. 9 indexed citations

19.

Bohn, Martha C., Eduardo Howard, Ursula Vielkind, & Zygmunt S. Krozowski. (1991). Glial cells express both mineralocorticoid and glucocorticoid receptors. The Journal of Steroid Biochemistry and Molecular Biology. 40(1-3). 105–111. 103 indexed citations

20.

Lorenzo, Cristina de, Eduardo Howard, & Rosa Nagel. (1990). Studies on Tn10 transposition and excision in DNA-repair mutants of Salmonella typhimurium. Mutation research. Fundamental and molecular mechanisms of mutagenesis. 232(1). 99–104. 10 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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