The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
An amplified sensitivity arising from covalent modification in biological systems.
Open accessAbstract
The transient and steady-state behavior of a reversible covalent modification system is examined. When the modifying enzymes operate outside the region of first-order kinetics, small percentage changes in the concentration of the effector controlling either of the modifying enzymes can give much larger percentage changes in the amount of modified protein. This amplification of the response to a stimulus can provide additional sensitivity in biological control, equivalent to that of allosteric proteins with high Hill coefficients.
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
Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*
Koshland, D. E., Némethy, G., & Filmer, D. (1966) · Biochemistry · doi:10.1021/bi00865a047 · Cited by 3,013
Self-citationTransforming gene product of Rous sarcoma virus phosphorylates tyrosine
Hunter, T., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,332
Phosphorylation-Dephosphorylation of Enzymes
Krebs, E. G., & Beavo, J. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004423 · Cited by 2,205
Protein kinase activity associated with the avian sarcoma virus src gene product.
Collett, M. S., & Erikson, R. L. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.4.2021 · Cited by 1,105
Greengard, P. (1978) · Science · doi:10.1126/science.22932 · Cited by 965
Studies on the Mechanism of Hormone Action
Sutherland, E. W. (1972) · Science · doi:10.1126/science.177.4047.401 · Cited by 687
Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron
Perutz, M. F. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.001551 · Cited by 667
Levinson, A. D., Oppermann, H., Levintow, L., Varmus, H. E., & Bishop, J. M. (1978) · Cell · doi:10.1016/0092-8674(78)90024-7 · Cited by 653
The phosphorylase b to a converting enzyme of rabbit skeletal muscle
Krebs, E. G., & Fischer, E. H. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90273-6 · Cited by 484
Protein methylation in behavioural control mechanisms and in signal transduction
Springer, M. S., Goy, M. F., & Adler, J. (1979) · Nature · doi:10.1038/280279a0 · Cited by 439
Cited by
Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell
Tyson, J. J., Chen, K. C., & Novak, B. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00017-6 · Cited by 1,583
Cell-signalling dynamics in time and space
Kholodenko, B. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1838 · Cited by 1,347
Ultrasensitivity in the mitogen-activated protein kinase cascade.
Huang, C. Y., & Ferrell, J. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.19.10078 · Cited by 1,186
Design principles of biochemical oscillators
Novák, B., & Tyson, J. J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2530 · Cited by 1,137
Defying death after DNA damage
Rich, T., Allen, R. L., & Wyllie, A. H. (2000) · Nature · doi:10.1038/35037717 · Cited by 724
Metadata
- Authors
- Goldbeter, A., & Koshland, D. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1981-11
- Volume
- 78
- Issue
- 11
- Pages
- 6840-6844
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2041603328
- Cited by
- 1,206
- References
- 19
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- green
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: An amplified sensitivity arising from covalent modification in biological systems. https://app.cochat.ai/papers/10.1073/pnas.78.11.6840
- The paper
- Goldbeter, A., & Koshland, D. E. (1981). An amplified sensitivity arising from covalent modification in biological systems. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.78.11.6840
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.