David Carling

52.6k total citations · 22 hit papers
183 papers, 40.7k citations indexed

About

David Carling is a scholar working on Molecular Biology, Surgery and Physiology. According to data from OpenAlex, David Carling has authored 183 papers receiving a total of 40.7k indexed citations (citations by other indexed papers that have themselves been cited), including 154 papers in Molecular Biology, 79 papers in Surgery and 35 papers in Physiology. Recurrent topics in David Carling's work include Metabolism, Diabetes, and Cancer (127 papers), Pancreatic function and diabetes (78 papers) and Adipose Tissue and Metabolism (30 papers). David Carling is often cited by papers focused on Metabolism, Diabetes, and Cancer (127 papers), Pancreatic function and diabetes (78 papers) and Adipose Tissue and Metabolism (30 papers). David Carling collaborates with scholars based in United Kingdom, United States and France. David Carling's co-authors include D. Grahame Hardie, Angela Woods, Barbara B. Kahn, Lee G.D. Fryer, Marian Carlson, Thierry Alquier, Matthew J. Sanders, Stephen Davies, Yasuhiko Minokoshi and Fabienne Foufelle and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

David Carling

181 papers receiving 40.0k citations

Hit Papers

Adiponectin stimulates glucose utilization and fatty-aci... 1989 2026 2001 2013 2002 2005 2002 2003 2014 1000 2.0k 3.0k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    2002 3.4k citations Yasuhiko Minokoshi, Fabienne Foufelle et al. profile →
  2. AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    2005 2.3k citations Barbara B. Kahn, David Carling et al. profile →
  3. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    2002 1.6k citations Yasuhiko Minokoshi, Young‐Bum Kim et al. Nature profile →
  4. LKB1 Is the Upstream Kinase in the AMP-Activated Protein Kinase Cascade
    2003 1.4k citations Angela Woods, Fiona C. Leiper et al. profile →
  5. The short-chain fatty acid acetate reduces appetite via a central homeostatic mechanism
    2014 1.3k citations Gary Frost, Michelle Sleeth et al. Nature Communications profile →
  6. THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?
    1998 1.2k citations D. Grahame Hardie, David Carling et al. profile →
  7. Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-activated protein kinase in mammalian cells
    2005 1.2k citations Angela Woods, Seung Pyo Hong et al. profile →
  8. The AMP‐Activated Protein Kinase
    1997 1.1k citations D. Grahame Hardie, David Carling profile →
  9. Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase
    1996 1.0k citations Angela Woods, David Carling et al. profile →
  10. The AMP-activated protein kinase cascade – a unifying system for energy control
    2003 939 citations David Carling profile →
  11. The Anti-diabetic Drugs Rosiglitazone and Metformin Stimulate AMP-activated Protein Kinase through Distinct Signaling Pathways
    2002 877 citations Lee G.D. Fryer, David Carling et al. profile →
  12. Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
    1989 763 citations David Carling, D. Grahame Hardie et al. Nature profile →
  13. Structure of mammalian AMPK and its regulation by ADP
    2011 712 citations David Carling et al. Nature profile →
  14. AMPK, insulin resistance, and the metabolic syndrome
    2013 695 citations David Carling et al. profile →
  15. Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia
    2000 653 citations David Carling et al. profile →
  16. Adenosine 5′-Monophosphate-Activated Protein Kinase Promotes Macrophage Polarization to an Anti-Inflammatory Functional Phenotype
    2008 647 citations David Carling et al. profile →
  17. AMPK signalling in health and disease
    2017 611 citations David Carling profile →
  18. AMP-activated Protein Kinase Plays a Role in the Control of Food Intake
    2004 610 citations Angela Woods, Stephen R. Bloom et al. profile →
  19. Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    2007 525 citations David Carling et al. Biochemical Journal profile →
  20. AMP-activated protein kinase: the current landscape for drug development
    2019 517 citations David Carling et al. profile →
  21. Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding
    2000 512 citations Ian P. Salt, D. Grahame Hardie et al. Biochemical Journal profile →
  22. Structural basis of AMPK regulation by small molecule activators
    2013 428 citations David Carling et al. Nature Communications profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David Carling United Kingdom 85 28.9k 11.9k 11.6k 8.2k 5.3k 183 40.7k
Benoı̂t Viollet France 98 27.2k 0.9× 9.7k 0.8× 9.5k 0.8× 10.8k 1.3× 5.3k 1.0× 344 42.4k
Morris J. Birnbaum United States 102 27.6k 1.0× 8.3k 0.7× 9.9k 0.9× 5.7k 0.7× 5.0k 0.9× 243 41.3k
Christopher B. Newgard United States 106 24.1k 0.8× 11.2k 0.9× 17.5k 1.5× 7.4k 0.9× 7.1k 1.3× 397 44.6k
Morris F. White United States 121 32.8k 1.1× 12.4k 1.0× 11.5k 1.0× 6.5k 0.8× 10.6k 2.0× 346 51.4k
Alan R. Saltiel United States 93 25.3k 0.9× 5.8k 0.5× 11.2k 1.0× 9.4k 1.1× 4.9k 0.9× 280 45.5k
Mitchell A. Lazar United States 125 30.0k 1.0× 3.7k 0.3× 16.7k 1.4× 12.7k 1.5× 6.6k 1.2× 325 56.1k
Domenico Accili United States 92 18.8k 0.7× 10.0k 0.8× 7.8k 0.7× 4.7k 0.6× 6.8k 1.3× 271 31.5k
Walter Wahli Switzerland 96 28.5k 1.0× 3.7k 0.3× 11.9k 1.0× 6.2k 0.7× 3.2k 0.6× 325 42.0k
Gary W. Cline United States 88 15.2k 0.5× 5.3k 0.4× 13.5k 1.2× 7.3k 0.9× 6.2k 1.2× 215 31.3k
Peter Tontonoz United States 95 27.4k 0.9× 13.3k 1.1× 10.6k 0.9× 7.8k 0.9× 3.3k 0.6× 228 45.0k

Countries citing papers authored by David Carling

Since Specialization
Citations

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

Fields of papers citing papers by David Carling

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Carling

This figure shows the co-authorship network connecting the top 25 collaborators of David Carling. A scholar is included among the top collaborators of David Carling 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 Carling. David Carling 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.
Adriaenssens, Alice E., William R. Scott, David Carling, et al.. (2025). Chronic GIPR agonism results in pancreatic islet GIPR functional desensitisation. Molecular Metabolism. 92. 102094–102094. 5 indexed citations
2.
Zhang, Jiping, Ewan R. Pearson, David Carling, et al.. (2024). Hypoglycaemic stimulation of macrophage cytokine release is suppressed by AMP‐activated protein kinase activation. Diabetic Medicine. 42(3). e15456–e15456. 1 indexed citations
3.
Sweeney, Mark, Michael S. Lee, Henrike Maatz, et al.. (2024). Interleukin 11 therapy causes acute left ventricular dysfunction. Cardiovascular Research. 120(17). 2220–2235. 1 indexed citations
4.
McGlone, Emma Rose, David C. D. Hope, Bryn M. Owen, et al.. (2023). Sleeve gastrectomy causes weight‐loss independent improvements in hepatic steatosis. Liver International. 43(9). 1890–1900. 8 indexed citations
5.
Bonnard, Carine, Naveenan Navaratnam, Thong Teck Tan, et al.. (2020). A loss-of-function NUAK2 mutation in humans causes anencephaly due to impaired Hippo-YAP signaling. The Journal of Experimental Medicine. 217(12). 35 indexed citations
6.
Woods, Angela, Phillip Muckett, Alexander Yu. Nikitin, et al.. (2018). CAMKK2 Promotes Prostate Cancer Independently of AMPK via Increased Lipogenesis. Cancer Research. 78(24). 6747–6761. 53 indexed citations
7.
Navaratnam, Naveenan, et al.. (2017). Effect of different γ-subunit isoforms on the regulation of AMPK. Biochemical Journal. 474(10). 1741–1754. 49 indexed citations
8.
Warren, Sean, et al.. (2016). Imaging of Metabolic Status in 3D Cultures with an Improved AMPK FRET Biosensor for FLIM. Sensors. 16(8). 1312–1312. 14 indexed citations
9.
Frost, Gary, Michelle Sleeth, Meliz Sahuri-Arisoylu, et al.. (2014). The short-chain fatty acid acetate reduces appetite via a central homeostatic mechanism. Nature Communications. 5(1). 3611–3611. 1301 indexed citations breakdown →
10.
Lallet-Daher, Hélène, Clotilde Wiel, Delphine Gitenay, et al.. (2013). Potassium Channel KCNA1 Modulates Oncogene-Induced Senescence and Transformation. Cancer Research. 73(16). 5253–5265. 42 indexed citations
11.
Bungard, David, Ping-Yao Zeng, Brandon Faubert, et al.. (2010). Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation. Science. 329(5996). 1201–1205. 290 indexed citations
12.
Martin, Matthew J., David Carling, & Richard Marais. (2009). Taking the Stress out of Melanoma. Cancer Cell. 15(3). 163–164. 10 indexed citations
13.
Carling, David. (2007). The Role of the AMP‐Activated Protein Kinase in the Regulation of Energy Homeostasis. Novartis Foundation symposium. 286. 72–85. 41 indexed citations
14.
Oliveira, Sandra Marisa, et al.. (2007). Cardiac troponin I is a potential novel substrate for AMP-activated protein kinase. Biophysical Journal. 3 indexed citations
15.
Hong, Seung Pyo, Fiona C. Leiper, Angela Woods, David Carling, & Marian Carlson. (2003). Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases. Proceedings of the National Academy of Sciences. 100(15). 8839–8843. 480 indexed citations
16.
Ernandes, José Roberto, Maria C. Loureiro‐Dias, Joris Winderickx, et al.. (2002). Evidence for involvement ofSaccharomyces cerevisiaeprotein kinase C in glucose induction ofHXTgenes and derepression ofSUC2. FEMS Yeast Research. 2(2). 93–102. 9 indexed citations
17.
Minokoshi, Yasuhiko, Young‐Bum Kim, Odile D. Peroni, et al.. (2002). Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature. 415(6869). 339–343. 1632 indexed citations breakdown →
18.
Woods, Angela, Dalila Azzout‐Marniche, Marc Foretz, et al.. (2000). Characterization of the Role of AMP-Activated Protein Kinase in the Regulation of Glucose-Activated Gene Expression Using Constitutively Active and Dominant Negative Forms of the Kinase. Molecular and Cellular Biology. 20(18). 6704–6711. 351 indexed citations
19.
20.
Hardie, D. Grahame, David Carling, & Nigel G. Halford. (1994). Roles of the Snf1/Rkin1/AMP-activated protein kinase family in the response to environmental and nutritional stress. PubMed. 5(6). 409–416. 77 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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