The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
The Network of Glucokinase-Expressing Cells in Glucose Homeostasis and the Potential of Glucokinase Activators for Diabetes Therapy
Abstract
The glucose-phosphorylating enzyme glucokinase has structural, kinetic, and molecular genetic features that are ideal for its primary role as glucose sensor in a network of neuro/endocrine sentinel cells that maintain glucose homeostasis in many vertebrates including humans. The glucokinase-containing, insulin-producing β-cells of the pancreas take the prominent lead in this network, functioning in the aggregate as the master gland. The β-cells are also conceptualized as the prototype for all other glucose sensor cells, which determines our current understanding of many extrapancreatic glucose sensors. About 99% of the enzyme resides, however, in the hepato-parenchymal cells and serves its second role in a high-capacity process of blood glucose clearance. Two examples strikingly illustrate how pivotal a position glucokinase has in the regulation of glucose metabolism: 1) activating and inactivating mutations of the enzyme cause hypo- and hyperglycemia syndromes in humans described collectively as “glucokinase disease” and fully explained by the glucose sensor paradigm, and 2) glucokinase activator drugs (GKAs) have been discovered that bind to an allosteric site and increase the kcat and lower the glucose S0.5 of the enzyme. GKAs enhance glucose-stimulated insulin release from pancreatic islets and glucose disposition by the liver. They are now intensively explored to develop a novel treatment for diabetes. Future biophysical, molecular, genetic, and pharmacological studies hold much promise to unravel the evolving complexity of the glucokinase glucose sensor system.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Plum, F. (1960) · Archives of Neurology · doi:10.1001/archneur.1960.03840090124020 · Cited by 10,364
Fundamentals of Enzyme Kinetics
(1979) · Elsevier eBooks · doi:10.1016/c2013-0-04130-8 · Cited by 2,059
Ca2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion
Prentki, M., & Matschinsky, F. M. (1987) · Physiological Reviews · doi:10.1152/physrev.1987.67.4.1185 · Cited by 774
Self-citationA Lesson in Metabolic Regulation Inspired by the Glucokinase Glucose Sensor Paradigm
Matschinsky, F. M. (1996) · Diabetes · doi:10.2337/diab.45.2.223 · Cited by 729
Self-citationBAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
Danial, N. N., Gramm, C. F., Scorrano, L., Zhang, C.-Y., Krauss, S., Ranger, A. M., Robert Datta, S., Greenberg, M. E., Licklider, L. J., Lowell, B. B., et al. (2003) · Nature · doi:10.1038/nature01825 · Cited by 705
Froguel, P., Vaxillaire, M., Sun, F., Velho, G., Zouali, H., Butel, M. O., Lesage, S., Vionnet, N., Clément, K., Fougerousse, F., et al. (1992) · Nature · doi:10.1038/356162a0 · Cited by 630
Allosteric Activators of Glucokinase: Potential Role in Diabetes Therapy
Grimsby, J., Sarabu, R., Corbett, W. L., Haynes, N.-E., Bizzarro, F. T., Coffey, J. W., Guertin, K. R., Hilliard, D. W., Kester, R. F., Mahaney, P. E., et al. (2003) · Science · doi:10.1126/science.1084073 · Cited by 526
Self-citationStructural Basis for Allosteric Regulation of the Monomeric Allosteric Enzyme Human Glucokinase
Kamata, K., Mitsuya, M., Nishimura, T., Eiki, J.-I., & Nagata, Y. (2004) · Structure · doi:10.1016/j.str.2004.02.005 · Cited by 502
Multiple Hexokinases of Rat Tissues
Grossbard, L., & Schimke, R. T. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99866-2 · Cited by 482
Linkage of type 2 diabetes to the glucokinase gene
Hattersley, A. T., Turner, R. C., Patel, P., O'Rahilly, S., Hattersley, A. T., Patel, P., Wainscoat, J. S., Permutt, M. A., Tanazawa, Y., Chin, K. C., et al. (1992) · The Lancet · doi:10.1016/0140-6736(92)91958-b · Cited by 375
Cited by
Yamauchi, T., Nio, Y., Maki, T., Kobayashi, M., Takazawa, T., Iwabu, M., Okada-Iwabu, M., Kawamoto, S., Kubota, N., Kubota, T., et al. (2007) · Nature Medicine · doi:10.1038/nm1557 · Cited by 1,396
Glucosensing and glucose homeostasis: From fish to mammals
Polakof, S., Mommsen, T. P., & Soengas, J. L. (2011) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2011.07.006 · Cited by 295
Kadowaki, T., Yamauchi, T., & Kubota, N. (2008) · FEBS Letters · doi:10.1016/j.febslet.2007.11.070 · Cited by 272
Nutrient Control of Insulin Secretion in Isolated Normal Human Islets
Henquin, J.-C., Dufrane, D., & Nenquin, M. (2006) · Diabetes · doi:10.2337/db06-0868 · Cited by 228
New hepatic targets for glycaemic control in diabetes
Agius, L. (2007) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2007.09.001 · Cited by 155
Metadata
- Authors
- Matschinsky, F. M., Magnuson, M. A., Zelent, D., Jetton, T. L., Doliba, N., Han, Y., Taub, R., & Grimsby, J.
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2006-01-01
- Volume
- 55
- Issue
- 1
- Pages
- 1-12
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2087036494
- Cited by
- 300
- References
- 57
- FWCI
- 24.62
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Network of Glucokinase-Expressing Cells in Glucose Homeostasis and the Potential of Glucokinase Activators for Diabetes Therapy. https://app.cochat.ai/papers/10.2337/diabetes.55.01.06.db05-0926
- The paper
- Matschinsky, F. M., Magnuson, M. A., Zelent, D., Jetton, T. L., Doliba, N., Han, Y., Taub, R., & Grimsby, J. (2006). The Network of Glucokinase-Expressing Cells in Glucose Homeostasis and the Potential of Glucokinase Activators for Diabetes Therapy. Diabetes. https://doi.org/10.2337/diabetes.55.01.06.db05-0926
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
