David Stapleton

10.6k total citations · 2 hit papers
94 papers, 8.9k citations indexed

About

David Stapleton is a scholar working on Molecular Biology, Surgery and Rheumatology. According to data from OpenAlex, David Stapleton has authored 94 papers receiving a total of 8.9k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 38 papers in Surgery and 18 papers in Rheumatology. Recurrent topics in David Stapleton's work include Metabolism, Diabetes, and Cancer (44 papers), Pancreatic function and diabetes (36 papers) and Glycogen Storage Diseases and Myoclonus (18 papers). David Stapleton is often cited by papers focused on Metabolism, Diabetes, and Cancer (44 papers), Pancreatic function and diabetes (36 papers) and Glycogen Storage Diseases and Myoclonus (18 papers). David Stapleton collaborates with scholars based in Australia, United States and China. David Stapleton's co-authors include Bruce E. Kemp, Lee A. Witters, Belinda J. Michell, Ken I. Mitchelhill, David A. Power, Frosa Katsis, Guang Gao, Colin M. House, Jane Widmer and Carolina Fernández and has published in prestigious journals such as Science, Journal of Biological Chemistry and Circulation.

In The Last Decade

David Stapleton

94 papers receiving 8.8k citations

Hit Papers

AMP‐activated protein kin... 1996 2026 2006 2016 1999 1996 200 400 600

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
David Stapleton 6.4k 2.7k 2.1k 1.1k 876 94 8.9k
Grant A. Mitchell 5.8k 0.9× 1.5k 0.5× 3.7k 1.8× 886 0.8× 2.0k 2.3× 206 11.8k
Donald A. McClain 6.4k 1.0× 2.3k 0.9× 2.7k 1.3× 1.5k 1.4× 1.1k 1.3× 166 11.5k
Lawrence Chan 4.0k 0.6× 1.8k 0.7× 1.9k 0.9× 1.1k 1.1× 2.1k 2.4× 125 9.5k
Angela Woods 8.8k 1.4× 3.4k 1.3× 2.0k 1.0× 1.2k 1.1× 1.7k 2.0× 60 11.2k
James Mu 6.9k 1.1× 3.1k 1.1× 3.0k 1.4× 1.6k 1.5× 1.3k 1.5× 42 10.1k
Geoffrey D. Holman 6.8k 1.1× 3.1k 1.1× 2.9k 1.4× 1.2k 1.1× 584 0.7× 158 9.9k
James A. Thomas 4.1k 0.6× 995 0.4× 1.0k 0.5× 697 0.6× 1.2k 1.4× 103 8.2k
Fátima Bosch 3.8k 0.6× 1.9k 0.7× 2.4k 1.2× 1.1k 1.1× 1.1k 1.2× 167 7.8k
Seung‐Hoi Koo 6.2k 1.0× 2.6k 1.0× 2.0k 1.0× 1.7k 1.6× 1.8k 2.0× 96 9.6k
Terry G. Unterman 7.3k 1.1× 1.7k 0.6× 2.5k 1.2× 2.6k 2.4× 1.0k 1.2× 157 12.6k

Countries citing papers authored by David Stapleton

Since Specialization
Citations

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

Fields of papers citing papers by David Stapleton

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Stapleton

This figure shows the co-authorship network connecting the top 25 collaborators of David Stapleton. A scholar is included among the top collaborators of David Stapleton 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 David Stapleton. David Stapleton 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.
Flores‐Opazo, Marcelo, Jennifer Trieu, Timur Naim, et al.. (2019). Defective fasting-induced PKA activation impairs adipose tissue glycogen degradation in obese Zucker rats. International Journal of Obesity. 44(2). 500–509. 7 indexed citations
2.
Murphy, Kate T., Mohammed Iqbal Hossain, Kristy Swiderski, et al.. (2018). Mas Receptor Activation Slows Tumor Growth and Attenuates Muscle Wasting in Cancer. Cancer Research. 79(4). 706–719. 33 indexed citations
3.
Murphy, Robyn M., et al.. (2018). No evidence of direct association between GLUT4 and glycogen in human skeletal muscle. Physiological Reports. 6(22). e13917–e13917. 3 indexed citations
4.
Mobbs, Jesse I., et al.. (2017). Unravelling the Carbohydrate‐Binding Preferences of the Carbohydrate‐Binding Modules of AMP‐Activated Protein Kinase. ChemBioChem. 19(3). 229–238. 3 indexed citations
5.
Deliyanti, Devy, et al.. (2015). FT011, a Novel Cardiorenal Protective Drug, Reduces Inflammation, Gliosis and Vascular Injury in Rats with Diabetic Retinopathy. PLoS ONE. 10(7). e0134392–e0134392. 15 indexed citations
6.
Reichelt, Melissa E., Kimberley M. Mellor, Claire L. Curl, David Stapleton, & Lea M.D. Delbridge. (2013). Myocardial glycophagy — A specific glycogen handling response to metabolic stress is accentuated in the female heart. Journal of Molecular and Cellular Cardiology. 65. 67–75. 72 indexed citations
7.
Zhang, Yuan, Amanda J. Edgley, Alison J. Cox, et al.. (2012). FT011, a New Anti-Fibrotic Drug, Attenuates Fibrosis and Chronic Heart Failure in Experimental Diabetic Cardiomyopathy. European Journal of Heart Failure. 14(5). 549–562. 41 indexed citations
8.
Bieri, Michael, Jesse I. Mobbs, Ann Koay, et al.. (2012). AMP-Activated Protein Kinase β-Subunit Requires Internal Motion for Optimal Carbohydrate Binding. Biophysical Journal. 102(2). 305–314. 18 indexed citations
9.
Scott, John W., Bryce J. W. van Denderen, Sebastian B. Jørgensen, et al.. (2008). Thienopyridone Drugs Are Selective Activators of AMP-Activated Protein Kinase β1-Containing Complexes. Chemistry & Biology. 15(11). 1220–1230. 209 indexed citations
10.
Iseli, Tristan J., Jonathan S. Oakhill, Michael F. Bailey, et al.. (2007). AMP-activated Protein Kinase Subunit Interactions. Journal of Biological Chemistry. 283(8). 4799–4807. 25 indexed citations
11.
Steinberg, Gregory R., Matthew J. Watt, Sean L. McGee, et al.. (2006). Reduced glycogen availability is associated with increased AMPKα2 activity, nuclear AMPKα2 protein abundance, and GLUT4 mRNA expression in contracting human skeletal muscle. Applied Physiology Nutrition and Metabolism. 31(3). 302–312. 87 indexed citations
12.
Polekhina, Galina, et al.. (2005). Structural Basis for Glycogen Recognition by AMP-Activated Protein Kinase. Structure. 13(10). 1453–1462. 160 indexed citations
13.
Park, Eui Kyun, Neil Warner, Yong‐Sik Bong, et al.. (2004). Ectopic EphA4 Receptor Induces Posterior Protrusions via FGF Signaling inXenopusEmbryos. Molecular Biology of the Cell. 15(4). 1647–1655. 34 indexed citations
14.
Polekhina, Galina, et al.. (2004). Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 39–42. 12 indexed citations
15.
Steiler, Tatiana L., Valérie Amarger, Margit Mahlapuu, et al.. (2004). The 5′-AMP-activated Protein Kinase γ3 Isoform Has a Key Role in Carbohydrate and Lipid Metabolism in Glycolytic Skeletal Muscle. Journal of Biological Chemistry. 279(37). 38441–38447. 252 indexed citations
16.
Hill, Richard L., et al.. (2003). Inhibition of the Na-K-2Cl co-transporter by novel interaction with the metabolic sensor AMP-activated protein kinase.. Journal of the American Society of Nephrology. 14. 1 indexed citations
17.
Polekhina, Galina, Belinda J. Michell, Bryce van Denderen, et al.. (2003). AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen. Current Biology. 13(10). 867–871. 353 indexed citations
18.
Hamilton, Stephen R., David Stapleton, John B. O'Donnell, et al.. (2001). An activating mutation in the γ1 subunit of the AMP‐activated protein kinase. FEBS Letters. 500(3). 163–168. 93 indexed citations
19.
Sicheri, Frank, et al.. (1999). The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.. Nature Structural Biology. 6(1). 44–49. 206 indexed citations
20.
Michell, Belinda J., David Stapleton, Ken I. Mitchelhill, et al.. (1996). Isoform-specific Purification and Substrate Specificity of the 5′-AMP-activated Protein Kinase. Journal of Biological Chemistry. 271(45). 28445–28450. 114 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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