Mark R. Harpel

2.0k total citations
38 papers, 1.5k citations indexed

About

Mark R. Harpel is a scholar working on Molecular Biology, Inorganic Chemistry and Biochemistry. According to data from OpenAlex, Mark R. Harpel has authored 38 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 10 papers in Inorganic Chemistry and 6 papers in Biochemistry. Recurrent topics in Mark R. Harpel's work include Metal-Catalyzed Oxygenation Mechanisms (10 papers), Photosynthetic Processes and Mechanisms (10 papers) and Microbial bioremediation and biosurfactants (5 papers). Mark R. Harpel is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (10 papers), Photosynthetic Processes and Mechanisms (10 papers) and Microbial bioremediation and biosurfactants (5 papers). Mark R. Harpel collaborates with scholars based in United States, Russia and India. Mark R. Harpel's co-authors include Fred C. Hartman, John D. Lipscomb, F.C. Hartman, Robert A. Copeland, Peter J. Tummino, Allen M. Orville, Eckard Münck, Frank W. Larimer, Robert N. Willette and Karpagam Aravindhan and has published in prestigious journals such as Journal of Biological Chemistry, Annual Review of Biochemistry and PLoS ONE.

In The Last Decade

Mark R. Harpel

38 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
Mark R. Harpel United States 22 891 334 193 157 126 38 1.5k
Robert A. Pufahl United States 16 1.2k 1.3× 202 0.6× 246 1.3× 14 0.1× 65 0.5× 16 3.3k
Kunio Tagawa Japan 25 1.4k 1.6× 160 0.5× 108 0.6× 70 0.4× 24 0.2× 80 2.4k
Rosemary Paschke United States 9 979 1.1× 126 0.4× 199 1.0× 53 0.3× 38 0.3× 10 1.5k
Eugene G. Hrycay Canada 21 716 0.8× 271 0.8× 79 0.4× 115 0.7× 84 0.7× 28 1.7k
N R Orme-Johnson United States 26 1.2k 1.4× 157 0.5× 91 0.5× 674 4.3× 33 0.3× 36 2.2k
J.E. Clark United States 19 636 0.7× 73 0.2× 58 0.3× 261 1.7× 48 0.4× 37 1.8k
Brenda Walker Griffin United States 26 806 0.9× 219 0.7× 63 0.3× 58 0.4× 16 0.1× 60 1.7k
Matthew D. Lloyd United Kingdom 31 1.9k 2.2× 458 1.4× 365 1.9× 32 0.2× 77 0.6× 89 2.9k
T Ohnishi United States 31 2.1k 2.3× 223 0.7× 187 1.0× 34 0.2× 13 0.1× 52 2.8k
Edmund Lengfelder Germany 29 877 1.0× 283 0.8× 80 0.4× 841 5.4× 58 0.5× 60 2.6k

Countries citing papers authored by Mark R. Harpel

Since Specialization
Citations

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

Fields of papers citing papers by Mark R. Harpel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mark R. Harpel. 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 Mark R. Harpel. The network helps show where Mark R. Harpel may publish in the future.

Co-authorship network of co-authors of Mark R. Harpel

This figure shows the co-authorship network connecting the top 25 collaborators of Mark R. Harpel. A scholar is included among the top collaborators of Mark R. Harpel 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 Mark R. Harpel. Mark R. Harpel 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.
Wong, Pancras C., Mimi L. Quan, Carol A. Watson, et al.. (2015). In vitro, antithrombotic and bleeding time studies of BMS-654457, a small-molecule, reversible and direct inhibitor of factor XIa. Journal of Thrombosis and Thrombolysis. 40(4). 416–423. 32 indexed citations
2.
Aravindhan, Karpagam, Weike Bao, Mark R. Harpel, et al.. (2015). Cardioprotection Resulting from Glucagon-Like Peptide-1 Administration Involves Shifting Metabolic Substrate Utilization to Increase Energy Efficiency in the Rat Heart. PLoS ONE. 10(6). e0130894–e0130894. 51 indexed citations
3.
Glunz, Peter W., Xiaojun Zhang, Yan Zou, et al.. (2013). Nonbenzamidine acylsulfonamide tissue factor–factor VIIa inhibitors. Bioorganic & Medicinal Chemistry Letters. 23(18). 5244–5248. 13 indexed citations
4.
Gatto, Gregory J., Zhaohui Ao, Michael G. Kearse, et al.. (2011). NADPH oxidase-dependent and -independent mechanisms of reported inhibitors of reactive oxygen generation. Journal of Enzyme Inhibition and Medicinal Chemistry. 28(1). 95–104. 64 indexed citations
5.
Bao, Weike, Karpagam Aravindhan, Hasan Alsaid, et al.. (2011). Albiglutide, a Long Lasting Glucagon-Like Peptide-1 Analog, Protects the Rat Heart against Ischemia/Reperfusion Injury: Evidence for Improving Cardiac Metabolic Efficiency. PLoS ONE. 6(8). e23570–e23570. 94 indexed citations
6.
Pullen, Mark, Mark R. Harpel, Theodore M. Danoff, & David P. Brooks. (2008). Comparison of non-digitalis binding properties of digoxin-specific Fabs using direct binding methods. Journal of Immunological Methods. 336(2). 235–241. 12 indexed citations
7.
Copeland, Robert A., Mark R. Harpel, & Peter J. Tummino. (2007). Targeting enzyme inhibitors in drug discovery. Expert Opinion on Therapeutic Targets. 11(7). 967–978. 98 indexed citations
8.
Cheng, Dongmei, Ching-Hsuen Chu, Luping Chen, et al.. (2006). Expression, purification, and characterization of human and rat acetyl cfenzyme A carboxylase (ACC) isozymes. Protein Expression and Purification. 51(1). 11–21. 36 indexed citations
9.
Harpel, Mark R., Kurumi Y. Horiuchi, Ying Luo, et al.. (2002). Mutagenesis and Mechanism-Based Inhibition of Streptococcus pyogenes Glu-tRNAGln Amidotransferase Implicate a Serine-Based Glutaminase Site. Biochemistry. 41(20). 6398–6407. 25 indexed citations
10.
Decicco, Carl P., David J. Nelson, Ying Luo, et al.. (2001). Glutamyl-γ-boronate Inhibitors of Bacterial Glu-tRNAGln Amidotransferase. Bioorganic & Medicinal Chemistry Letters. 11(18). 2561–2564. 19 indexed citations
11.
Harpel, Mark R., Kurumi Y. Horiuchi, Kelley C. Rogers, et al.. (2000). Implementation of a Continuous, Enzyme-Coupled Fluorescence Assay for High-Throughput Analysis of Glutamate-Producing Enzymes. Analytical Biochemistry. 284(2). 382–387. 14 indexed citations
12.
Harpel, Mark R., Frank W. Larimer, & Fred C. Hartman. (1998). Multiple catalytic roles of His 287 of Rhodospirillum rubrum ribulose 1,5‐bisphosphate carboxylase/oxygenase. Protein Science. 7(3). 730–738. 11 indexed citations
13.
Harpel, Mark R., et al.. (1995). The nature and alternate rates of the ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) oxygenation intermediate. University of North Texas Digital Library (University of North Texas). 2 indexed citations
15.
Hartman, Fred C. & Mark R. Harpel. (1994). STRUCTURE, FUNCTION, REGULATION, AND ASSEMBLY OF D-RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE. Annual Review of Biochemistry. 63(1). 197–232. 274 indexed citations
16.
Harpel, Mark R. & Fred C. Hartman. (1994). Chemical Rescue by Exogenous Amines of a Site-Directed Mutant of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase That Lacks a Key Lysyl Residue. Biochemistry. 33(18). 5553–5561. 25 indexed citations
17.
Harpel, Mark R., E.H. Lee, & F.C. Hartman. (1993). Anion-Exchange Analysis of Ribulose-Bisphosphate Carboxylase/Oxygenase Reactions: CO2/O2 Specificity Determination and Identification of Side Products. Analytical Biochemistry. 209(2). 367–374. 30 indexed citations
18.
Harpel, Mark R., et al.. (1993). Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.. Journal of Biological Chemistry. 268(35). 26583–26591. 30 indexed citations
20.
Harpel, Mark R. & John D. Lipscomb. (1990). [17] Gentisate 1,2-dioxygenase from Pseudomonas acidovorans. Methods in enzymology on CD-ROM/Methods in enzymology. 188. 101–107. 8 indexed citations

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