The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein kinases: evolution of dynamic regulatory proteins
Open accessAbstract
Eukaryotic protein kinases evolved as a family of highly dynamic molecules with strictly organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for assembly of the entire molecule. Two non-consecutive hydrophobic structures termed “Spines” anchor all the elements important for catalysis to the F-helix. They make firm, but flexible, connections within the molecule providing a high level of internal dynamics of the protein kinase. During the course of evolution, protein kinases developed a universal regulatory mechanism associated with a large Activation Segment that can be dynamically folded and unfolded in the course of cell functioning. Protein kinases thus represent a unique, highly dynamic and precisely regulated set of switches that control most biological events in eukaryotic cells.
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
The RSK family of kinases: emerging roles in cellular signalling
Anjum, R., & Blenis, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2509 · Cited by 777
CASK Functions as a Mg2+-independent neurexin kinase
Mukherjee, K., Sharma, M., Urlaub, H., Bourenkov, G. P., Jahn, R., Südhof, T. C., & Wahl, M. C. (2008) · Cell · doi:10.1016/j.cell.2008.02.036 · Cited by 271
Cited by
ERK1/2 MAP kinases: Structure, function, and regulation
Roskoski, R. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,650
ERK signalling: A master regulator of cell behaviour, life and fate
Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185
AMPK: An Energy-Sensing Pathway with Multiple Inputs and Outputs
Hardie, D. G., Schaffer, B. E., & Brunet, A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.013 · Cited by 859
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Taipale, M., Krykbaeva, I., Koeva, M., Kayatekin, C., Westover, K. D., Karras, G. I., & Lindquist, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.047 · Cited by 879
An atlas of substrate specificities for the human serine/threonine kinome
Johnson, J. L., Yaron, T. M., Huntsman, E. M., Kerelsky, A., Song, J., Regev, A., Lin, T.-Y., Liberatore, K., Cizin, D. M., Cohen, B. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05575-3 · Cited by 728
Metadata
- Authors
- Taylor, S. S., & Kornev, A. P.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 36
- Issue
- 2
- Pages
- 65-77
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1970174659
- Cited by
- 945
- References
- 2
- FWCI
- 1.92
- 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: Protein kinases: evolution of dynamic regulatory proteins. https://app.cochat.ai/papers/10.1016/j.tibs.2010.09.006
- The paper
- Taylor, S. S., & Kornev, A. P. (2011). Protein kinases: evolution of dynamic regulatory proteins. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2010.09.006
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.
