Robert W. Henkens

1.9k total citations
50 papers, 1.6k citations indexed

About

Robert W. Henkens is a scholar working on Molecular Biology, Cell Biology and Electrical and Electronic Engineering. According to data from OpenAlex, Robert W. Henkens has authored 50 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 16 papers in Cell Biology and 12 papers in Electrical and Electronic Engineering. Recurrent topics in Robert W. Henkens's work include Hemoglobin structure and function (14 papers), Electrochemical sensors and biosensors (12 papers) and Enzyme function and inhibition (12 papers). Robert W. Henkens is often cited by papers focused on Hemoglobin structure and function (14 papers), Electrochemical sensors and biosensors (12 papers) and Enzyme function and inhibition (12 papers). Robert W. Henkens collaborates with scholars based in United States, Denmark and Hungary. Robert W. Henkens's co-authors include Alvin L. Crumbliss, John P. O'Daly, Junguo Zhao, J. Stonehuerner, Julian M. Sturtevant, Taffy J. Williams, Celia Bonaventura, Mary C. Rose, Barbara B. Kitchell and Jinping Zhao 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

Robert W. Henkens

50 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert W. Henkens United States 23 955 620 403 233 211 50 1.6k
Susan A. Rotenberg United States 28 1.1k 1.2× 360 0.6× 803 2.0× 134 0.6× 181 0.9× 54 2.3k
Paul D. Barker United Kingdom 28 1.7k 1.7× 348 0.6× 245 0.6× 427 1.8× 566 2.7× 74 2.4k
Elizabeth M. Boon United States 29 2.5k 2.6× 546 0.9× 311 0.8× 298 1.3× 664 3.1× 63 3.4k
Garfield P. Royer United States 21 795 0.8× 246 0.4× 145 0.4× 168 0.7× 67 0.3× 44 1.5k
Alexander Kotlyar Israel 34 2.7k 2.8× 1000 1.6× 312 0.8× 540 2.3× 69 0.3× 117 3.8k
S. Rappoport Israel 11 668 0.7× 354 0.6× 106 0.3× 263 1.1× 53 0.3× 18 1.3k
Artur Sucheta United States 20 411 0.4× 430 0.7× 364 0.9× 146 0.6× 77 0.4× 29 1.1k
D. G. Davis United States 19 418 0.4× 241 0.4× 287 0.7× 417 1.8× 44 0.2× 49 1.3k
Walther R. Ellis United States 16 552 0.6× 215 0.3× 160 0.4× 162 0.7× 154 0.7× 30 1.1k
Marián Antalı́k Slovakia 21 1.0k 1.1× 199 0.3× 124 0.3× 306 1.3× 168 0.8× 102 1.7k

Countries citing papers authored by Robert W. Henkens

Since Specialization
Citations

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

Fields of papers citing papers by Robert W. Henkens

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert W. Henkens. 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 Robert W. Henkens. The network helps show where Robert W. Henkens may publish in the future.

Co-authorship network of co-authors of Robert W. Henkens

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

All Works

20 of 20 papers shown
1.
Abdellaoui, Sofiène, Alexandre Noiriel, Robert W. Henkens, et al.. (2013). A 96-Well Electrochemical Method for the Screening of Enzymatic Activities. Analytical Chemistry. 85(7). 3690–3697. 28 indexed citations
2.
Banerjee, Sambuddha, Yiping Jia, Bindu Abraham, et al.. (2012). Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions. Free Radical Biology and Medicine. 53(6). 1317–1326. 31 indexed citations
3.
Bonaventura, Celia, et al.. (2011). Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(10). 1261–1268. 2 indexed citations
4.
Bonaventura, Celia, Robert W. Henkens, Juan López‐Garriga, et al.. (2010). Extreme differences between Hemoglobins I and II of the Clam Lucina pectinalis in their reactions with nitrite. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804(10). 1988–1995. 7 indexed citations
5.
Bonaventura, Celia, Robert W. Henkens, Abdu I. Alayash, & Alvin L. Crumbliss. (2007). Allosteric effects on oxidative and nitrosative reactions of cell‐free hemoglobins. IUBMB Life. 59(8-9). 498–505. 20 indexed citations
6.
Stevens, Robert D., Randall S. Wells, Suraj Dhungana, et al.. (2007). Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins. Gene. 398(1-2). 123–131. 8 indexed citations
7.
Bonaventura, Celia, et al.. (2005). Overproduction of α Chains Provides a Proton-insensitive Component to the Bluefish Hemoglobin System. Journal of Biological Chemistry. 280(49). 40509–40514. 3 indexed citations
8.
Henkens, Robert W., et al.. (2004). Detection of Staphylococcus aureus enterotoxin A and B genes with PCR-EIA and a hand-held electrochemical sensor. Molecular and Cellular Probes. 18(6). 373–377. 22 indexed citations
9.
Bonaventura, Celia, Angela Fago, Robert W. Henkens, & Alvin L. Crumbliss. (2004). Critical Redox and Allosteric Aspects of Nitric Oxide Interactions with Hemoglobin. Antioxidants and Redox Signaling. 6(6). 979–991. 10 indexed citations
10.
Bonaventura, Celia, et al.. (2002). Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease. Biophysical Chemistry. 98(1-2). 165–181. 11 indexed citations
11.
Zhao, Jinping, Robert W. Henkens, & Alvin L. Crumbliss. (1996). Mediator-Free Amperometric Determination of Toxic Substances Based on Their Inhibition of Immobilized Horseradish Peroxidase. Biotechnology Progress. 12(5). 703–708. 30 indexed citations
12.
Zhao, Junguo, John P. O'Daly, Robert W. Henkens, J. Stonehuerner, & Alvin L. Crumbliss. (1996). A xanthine oxidase/colloidal gold enzyme electrode for amperometric biosensor applications. Biosensors and Bioelectronics. 11(5). 493–502. 103 indexed citations
13.
Crumbliss, Alvin L., J. Stonehuerner, Robert W. Henkens, Jinping Zhao, & John P. O'Daly. (1993). A carrageenan hydrogel stabilized colloidal gold multi-enzyme biosensor electrode utilizing immobilized horseradish peroxidase and cholesterol oxidase/cholesterol esterase to detect cholesterol in serum and whole blood. Biosensors and Bioelectronics. 8(6). 331–337. 65 indexed citations
14.
Stonehuerner, J., et al.. (1992). Comparison of colloidal gold electrode fabrication methods: the preparation of a horseradish peroxidase enzyme electrode. Biosensors and Bioelectronics. 7(6). 421–428. 38 indexed citations
15.
O'Daly, John P., Junguo Zhao, Philip A. Brown, & Robert W. Henkens. (1992). Electrochemical enzyme immunoassay for detection of toxic substances. Enzyme and Microbial Technology. 14(4). 299–302. 14 indexed citations
16.
Zhao, Junguo, et al.. (1992). Direct electron transfer at horseradish peroxidase—colloidal gold modified electrodes. Journal of Electroanalytical Chemistry. 327(1-2). 109–119. 270 indexed citations
17.
Williams, Taffy J., et al.. (1989). Mussel glue protein has an open conformation. Archives of Biochemistry and Biophysics. 269(2). 415–422. 54 indexed citations
18.
Crumbliss, Alvin L., et al.. (1988). Preparation and activity of carbonic anhydrase immobilized on porous silica beads and graphite rods. Biotechnology and Bioengineering. 31(8). 796–801. 32 indexed citations
19.
20.
Rose, Mary C. & Robert W. Henkens. (1974). Stability of sodium and potassium complexes of valinomycin. Biochimica et Biophysica Acta (BBA) - General Subjects. 372(2). 426–435. 49 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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