The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2C α and native bovine protein phosphatase‐2A c
Abstract
Human protein phosphatase-2C alpha (PP2C alpha) was purified to homogeneity after expression in Escherichia coli. AMP inhibited the dephosphorylation of AMP-activated protein kinase (AMPK), but not phosphocasein, by PP2C alpha. The concentration dependence and the effects of other nucleotides (ATP and formycin A-5'-monophosphate) suggest that AMP acts by binding to the same site which causes direct allosteric activation of AMPK. A similar, although less pronounced, effect was observed with another protein phosphatase (PP2AC). We have now shown that AMPK activates the AMPK cascade by four mechanisms, which should make the system exquisitely sensitive to changes in AMP concentration.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Activation loop phosphorylation increases AMPK activity by about 100-fold, while allosteric regulation changes AMPK activity up to tenfold in mammalian cells and about twofold in recombinant, bacterially produced AMPK [26,28,38,39].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [39]
Citations
Cites
Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232
Serine/threonine protein phosphatases
Wera, S., & Hemmings, B. A. (1995) · Biochemical Journal · doi:10.1042/bj3110017 · Cited by 638
Muchmore, D. C., McIntosh, L. P., Russell, C., Anderson, D. E., & Dahlquist, F. W. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)77005-1 · Cited by 454
Hawley, S. A., Selbert, M. A., Goldstein, E. G., Edelman, A. M., Carling, D., & Hardie, D. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27186 · Cited by 441
DAVIES, S. P., Carling, D., & Hardie, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15185.x · Cited by 431
Role of the AMP-activated protein kinase in the cellular stress response
Corton, J. M., Gillespie, J. G., & Hardie, D. G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00070-1 · Cited by 423
Purification and characterization of the AMP‐activated protein kinase
Carling, D., Clarke, P. R., Zammit, V. A., & Hardie, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15186.x · Cited by 418
[37] Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle
Cohen, P., Alemany, S., Therese, B. A., Resink, J., Strålfors, P., & Tung, H. Y. L. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)59039-0 · Cited by 411
Woods, A., Munday, M. R., Scott, J., Yang, X., Carlson, M., & Carling, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32198-1 · Cited by 409
Mitchelhill, K. I., Stapleton, D., Gao, G., House, C. M., Michell, B. J., Katsis, F., Witters, L. A., & Kemp, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41951-x · Cited by 338
Research works printed but not linked: 3
- 10.1111/j.1432-1033.1995.0558k.x · DOI
- Clarke P.R., 1991, Adv. Protein Phosphatases, 6, 187
- MacKintosh C. (1993) in: (Hardie D.G. eds.) pp. 214–216. Oxford University Press Oxford.
Cited by
Sorted by citations
Items 501–600 of 606
Can food factors provide Us with the similar beneficial effects of physical exercise?
Miyamoto, L. (2016) · Food Science and Biotechnology · doi:10.1007/s10068-016-0092-9 · Cited by 3
Urine levels of 5-aminoimidazole-4-carboxamide riboside (AICAR) in patients with type 2 diabetes
Mendler, M., Kopf, S., Groener, J. B., Riedinger, C., Fleming, T. H., Nawroth, P. P., & Okun, J. G. (2018) · Acta Diabetologica · doi:10.1007/s00592-018-1130-2 · Cited by 3
Nandi, N., Zaidi, Z., Tracy, C., & Krämer, H. (2022) · eLife · doi:10.7554/elife.72169 · Cited by 3
“…a pivotal role in different physiological or pathological processes that are responsive to cellular stress signaling, including regulation of AMPK ( Davies et al., 1995 ), Tak1 ( Hanada et al., 2001 ), or other mitogen-activated protein (MAP) kinases ( Hanada et al., 1998 ; Maeda et al., 1994 ;…”
Maintaining Energy Balance in Health and Disease: Role of the AMP-Activated Protein Kinase
Scott, J. W. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_9 · Cited by 2
Glucose-free conditions induce the expression of AMPK in dental pulp cells
Muramatsu, T., Yuasa, K., Ebihara, K., Shibukawa, Y., Ohta, K., Furusawa, M., & Shimono, M. (2013) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2013.08.009 · Cited by 2
ATIC as a link between antirheumatic drugs and regulation of energy metabolism in skeletal muscle
Dolinar, K. (2020) · Periodicum Biologorum · doi:10.18054/pb.v121-122i3-4.10802 · Cited by 2
An Inducible System to Study the Growth Arrest Properties of Protein Phosphatase 2C
Ofek, P., Ben‐Meir, D., & Lavi, S. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)66025-8 · Cited by 2
Reichling, L. J., Riddle, S. M., Mei, B., Bruinsma, R., Goossens, T. A., Huwiler, K. G., Maffitt, M., Newport, A. M. G., Qian, X.-D., Rüttimann-Johnson, C., et al. (2008) · Current Chemical Genomics · doi:10.2174/1875397300801010034 · Cited by 2
“AMPK is a heterotrimeric complex consisting of , , and subunits [3, 4], and is directly regulated by at least three processes: activation through phosphorylation of Thr-172 in the activation loop of the catalytic subunit by LKB1 [5-9] or CaMKK or [10, 11], deactivation via dephosphorylation at this site by PP2 [12], a…”
BackgroundmTOR and its Physiological Impacts-Part I: An Overview
Kwan, P., & Tse, T. M. (2013) · Cited by 2
Venugopal, A., & Bishu, S. (2021) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000709 · Cited by 2
“Binding of AMP at sites 1 and 3 causes a conformal change and exposes a threonine (Thr172) residue to phosphorylation (by upstream kinases), thereby activating AMPK [2,5] (Fig.”
BackgroundTHE EFFECTS OF METFORMIN ON PANCREATIC CANCER METABOLISM
Cantoria, M. J. (2014) · UA Campus Repository (The University of Arizona) · Cited by 2
Smiles, W. J., Ovens, A. J., Yu, D., Ling, N. X. Y., Morrison, K. R., Hoque, A., Scott, J. W., Galić, S., Langendorf, C. G., Kemp, B. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.20.462995 · Cited by 2
“The presence of nucleotides bound at the g -subunit is sensed by the a -RIM, where binding of AMP sequesters the AID from the a -KD to allosterically activate AMPK, whereas AMP or ADP binding also promote a T172 phosphorylation (p-a T172 ) and protect it from dephosphorylation [18,19].”
BackgroundThe Lysosome Signaling Platform: Adapting With the Times
Inpanathan, S., & Botelho, R. (2023) · doi:10.32920/21982901 · Cited by 2
Kircheva, N., Petkova, V., Angelova, S., & Dudev, T. (2026) · Biomolecules · doi:10.3390/biom16060860 · Cited by 1
“The function of the metal cofactor in the binuclear active site is to capture one water molecule to subsequently attack the phosphate groups of the diverse substrates—AMP-activated protein kinase (AMPK), mitogen-activated protein kinase (MAPK), cyclin-dependent kinases (CDK), etc. [16–18].”
Targeting the AMP-regulated kinase family to treat diabetes: a research update
Sun, G., & Rutter, G. A. (2011) · Diabetes Management · doi:10.2217/dmt.11.11 · Cited by 2
Antidiabetic Drugs and their Potential Use in COVID-19: A Mechanistic Approach
Balderas-Renterı́a, I., Espinosa-Rodríguez, B. A., Nieto-Moreno, A. M., Llerena, J. L. G., Rico-Torres, T. A., Carranza‐Rosales, P., & Méndez-López, L. F. (2022) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530322666220516115604 · Cited by 1
AMPK Regulation of Cardiac Metabolism in Heart Disease
An, D., Kim, M., & Rodrigues, B. B. (2008) · Springer eBooks · doi:10.1007/978-0-387-09552-3_21 · Cited by 1
Investigating the role and regulation of the AMPK-related kinase NUAK1
Bull, D. (2013) · doi:10.25560/23995 · Cited by 1
Geminivirus AL2 and L2 proteins interact with and inactivate adenosine kinase
Wang, H. (2004) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1
Glucose sensing and the regulation of the AMP-activated protein kinase in yeast
Rubenstein, E. M. (2008) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Qin, Y., Sekine, I., Fan, M., Takiguchi, Y., Tada, Y., Shingyoji, M., Hanazono, M., Yamaguchi, N., & Tagawa, M. (2017) · Cancer Cell International · doi:10.1186/s12935-017-0493-8 · Cited by 1
“PEM-treated cells accumulated ZMP, an intermediated AMP analogue, activated the APMK [10, 11].”
Nutrient and energy sensing in skeletal muscle
Deshmukh, A. S. (2009) · Figshare · Cited by 1
Nucleotide regulation of AMP-activated protein kinase
Underwood, E. (2013) · UCL Discovery (University College London) · Cited by 1
Regulatory Circuits Linking Energy Status to Growth
Jansen, W. M. (2017) · Utrecht University Repository (Utrecht University) · Cited by 1
Han, S.-D., Lee, J., Noh, Y., Jin, M., & Kim, J. S. (2018) · Preprints.org · doi:10.20944/preprints201808.0448.v2
Han, S.-D., Lee, J., Noh, Y., Jin, M., & Kim, J. S. (2018) · Preprints.org · doi:10.20944/preprints201808.0448.v1
“PP2A is known to regulate AMPK activation and tau phosphorylation [18,19].”
InfluentialReynolds, A. R. (2015) · UKnowledge (University of Kentucky)
Hardie, D. G. (2001) · Cell and molecular responses to stress · doi:10.1016/s1568-1254(01)80013-9
Skeletal muscle metabolic flexibility : The roles of AMP-activated protein kinase and calcineurin
Long, Y. C. (2007) · Figshare
The role of AMP-activated protein kinase in endothelial VEGF signalling
Reihill, J. A. (2009) · Enlighten: Theses (The University of Glasgow)
Die Rolle der AMP-Kinase bei der Regulation des Vasotonus
Kreutz, C.-P. (2013) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.16547
Regulation of metabolism and inflammation in liver and skeletal muscle
Nerstedt, A. (2013) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Pham, M. N. (2014) · UA Campus Repository (The University of Arizona)
The Effect of Myostatin on Glucose Metabolism and Insulin Sensitivity
Ghozlan, M. (2013) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/28087
The AMPK signalling pathway in cancer and DNA damage
Dandapani, M. (2013) · Discovery Research Portal (University of Dundee)
Resposta à insulina no músculo esquelético de ratos tratados com apocinina.
Fujiwara, H. (2013) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2013.tde-12062013-094713
Regulation of fatty acid oxidation by malonyl CoA in cardiac muscle
Lopaschuk, G. D., & Onay-Beşi̇kçi̇, A. (2003) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(03)33011-5
micein skeletal muscle of adenylate kinase-deficient Contraction-mediated phosphorylation of AMPK is
Hancock, C. R., Janssen, E., Terjung, R. L., Zierath, J. R., Kulkarni, S. S., Karlsson, H., Szekeres, F. L. M., Chibalin, A., Bontemps, F., Oscarsson, J., et al. (2015)
AMPK and Metabolic Remodeling in Cardiac Disease
Pulinilkunnil, T., Nagendran, J., & Dyck, J. R. B. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-891-7_5
Chen, X.-Y., Gu, X., Saiyin, H., Zhang, Y., Li, J., Wang, Y., Gao, R., Wang, Y., Najjar, S. M., Zhang, C., et al. (2012)
Roles of SnRK1, ADK, and APT1 in the Cellular Stress Response and Antiviral Defense
Mohannath, G. T. (2010) · OhioLink ETD Center (Ohio Library and Information Network)
Canagliflozin Potently Activates AMPK and Inhibits the Growth and Survival of Cancer Cells
Villani, L. A. (2015) · MacSphere (McMaster University) · doi:10.71548/8610
Pathways controlling metabolic and hypertrophic responses in skeletal muscle
Riedl, I. (2015) · Figshare
Mechanisms of vascular protection in chronic inflammatory disease
Thornton, C. C. (2014) · Spiral (Imperial College London) · doi:10.25560/26595
Glycogen turnover in heart-derived H9c2 cells
Cheung, K. (2009) · cIRcle (University of British Columbia) · doi:10.14288/1.0092002
AMP-activated protein kinase and hypertrophic remodeling of heart muscle cells
Saeedi, R. (2009) · cIRcle (University of British Columbia) · doi:10.14288/1.0070791
Magnesium Supplementation Through Drinking Water to Improve Pork Quality.
Frederick, B. (2003) · NCSU Libraries Repository (North Carolina State University Libraries)
Schofield, C. J. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)
St-Amand, E. (2015) · Corpus Université Laval (Université Laval)
Combination Therapeutic Strategies Targeting Growth and Metabolic Pathways in Prostate Cancer
Canatsey, R. D. (2016) · UA Campus Repository (The University of Arizona)
Candidata Scientarum-oppgave i molekylær cellebiologi
Dahl, M. B. (2005)
Loyd, C. (2014) · OhioLink ETD Center (Ohio Library and Information Network)
Samarasinghe, K. T. G. (2017) · Human Biology
Dite, T. A. (2018) · Minerva Access (University of Melbourne)
The role of folate in non-alcoholic fatty liver disease
Sid, V. (2019) · Mspace (University of Manitoba)
Regulation and Function of the Phosphatase PHLPP2 in Leukemia
Yan, Y. (2017) · University of Minnesota Digital Conservancy (University of Minnesota)
A role for AMPK in the regulation of mitosis and cytokinesis
Bremner, S. (2020) · Enlighten: Theses (The University of Glasgow) · doi:10.5525/gla.thesis.80254
Hardman, S. E. (2014) · ScholarsArchive (Brigham Young University)
Michell, B. J., Witters, L. A., Kemp, B. E., & Stapleton, D. (2005) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a000269.01
The Lysosome Signaling Platform: Adapting With the Times
Inpanathan, S., & Botelho, R. (2023) · doi:10.32920/21982901.v1
Vázquez-Lemus, D., Rodríguez-Cuevas, E. G., Hernández-Esquivel, A. A., Castro-Mercado, E., de la Cruz, H. R., Campos‐García, J., López‐Bucio, J., & García‐Pineda, E. (2025) · Acta Physiologiae Plantarum · doi:10.1007/s11738-025-03812-6
“The binding of ADP and AMP to the γ-subunit also induces a conformational change in the AMPK complex, rendering it resistant to dephosphorylation and inactivation by phosphatases (Davies et al. 1995; Suter et al. 2006; Oakhill et al. 2011; Xiao et al. 2011).”
Stimulus response coupling in the carotid body: a role for metabolic signalling
Holmes, A. P. (2013) · University of Birmingham Institutional Research Archive (University of Birmingham)
Liver Kinase B1/AMP-Activated Protein Kinase Signaling in the Diaphragm
Brown, J. D. (2010) · ScholarsArchive (Brigham Young University)
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739624
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739621
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739645
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739603
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739615
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739636
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26113160
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739606
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739618
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739633
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739639
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739612
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739609
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739642
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739648
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739654
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739651
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739627
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26739630
Liu, Y., Lu, S., Yang, J., Yang, Y., Jiao, L., Hu, J., Li, Y., Yang, F., Pang, Y., Zhao, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26113065
Isoform-specific roles and overlooked complexity of AMPKα in Alzheimer's disease
Zimmermann, H. R., Jester, H. M., Vassar, R. J., & Ma, T. (2026) · Brain medicine : · doi:10.61373/bm026y.0003
Etude de la cardioprotection contre l'infarctus du myocarde au cours de l'obésité expérimentale
Bouhidel, J. O. (2010) · theses.fr (ABES) · doi:10.70675/6ad8f864zee3fz4749za1d1z550c6bf7007c
Laboucarié, T. (2016) · theses.fr (ABES) · doi:10.70675/5c52847ez969az4bc3z9144zdedf14c308df
Desgeorges, T. (2019) · theses.fr (ABES) · doi:10.70675/fe0c7b78zdae7z461az8a90zaddc4adfb49c
Biochemical characterization of mTORC1 regulation by glutamine metabolism
Bodineau, C. (2020) · theses.fr (ABES) · doi:10.70675/9d5aaabdz81bdz4118zb3edze237bdd8dee0
Modulation of tumor immunogenicity with AMPK activation in acute myeloid leukemia
Mondésir, J. (2021) · theses.fr (ABES) · doi:10.70675/2693bda5ze768z4bf0z857bze1eb8ccccc80
Lanfranchi, M. (2021) · theses.fr (ABES) · doi:10.70675/247335b1zba7fz4005zafbdzdc43c088d75f
ALDOC modulates astrocytic glycolysis and AMPK/mTOR/HIF-1α signaling in Alzheimer’s disease
Zhang, Z., Bai, Y., Xiangjian, Z., Zhang, J., & Yang, G. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1847340
Metadata
- Authors
- Davies, S. P., Helps, N. R., Cohen, P., & Hardie, D. G.
- Affiliations
- University of Dundee (GB)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1995-12-27
- Volume
- 377
- Issue
- 3
- Pages
- 421-425
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2030636484
- Cited by
- 595
- References
- 19
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 18 · 2023: 11 · 2022: 16 · 2021: 25 · 2020: 23 · 2019: 17 · 2018: 21 · 2017: 28 · 2016: 25 · 2015: 30 · 2014: 36 · 2013: 32 · 2012: 35
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- AMPK, AMP, dephosphorylation, phosphorylation, allosteric activation, nucleotide binding, formycin A, energy homeostasis
- MeSH terms
- Protein Phosphatase 2C, Adenosine Monophosphate, Allosteric Regulation, Animals, Base Sequence, Cattle, Dose-Response Relationship, Drug, Enzyme Activation, Escherichia coli, Humans, Isoenzymes, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Nucleotides, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Recombinant Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Protein Phosphatase 2, AMP-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review