The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Multiple modes of ligand recognition: Crystal structures of cyclin‐dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine
Abstract
Cyclin‐dependent kinases (CDKs) are conserved regulators of the eukaryotic cell cycle with different isoforms controlling specific phases of the cell cycle. Mitogenic or growth inhibitory signals are mediated, respectively, by activation or inhibition of CDKs which phosphorylate proteins associated with the cell cycle. The central role of CDKs in cell cycle regulation makes them a potential new target for inhibitory molecules with anti‐proliferative and/or anti‐neoplastic effects. We describe the crystal structures of the complexes of CDK2 with a weakly specific CDK inhibitor, N6‐(δ2‐isopentenyl)adenine, and a strongly specific inhibitor, olomoucine. Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP. The N6‐benzyl substituent in olomoucine binds outside the conserved binding pocket and is most likely responsible for its specificity. The structural information from the CDK2‐olomoucine complex will be useful in directing the search for the next generation inhibitors with improved properties. © 1995 Wiley‐Liss, Inc.
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
A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4.
Serrano, M., Hannon, G. J., & Beach, D. (1993) · Nature · doi:10.1038/366704a0 · Cited by 3,650
A cell cycle regulator potentially involved in genesis of many tumor types
Kamb, A., Gruis, N. A., Weaver-Feldhaus, J., Liu, Q., Harshman, K., Tavtigian, S. V., Stockert, E., Day, R. S., Johnson, B. E., & Skolnick, M. H. (1994) · Science · doi:10.1126/science.8153634 · Cited by 2,751
Matsushime, H., Ewen, M. E., Strom, D. K., Kato, J.-Y., Hanks, S. K., Roussel, M. F., & Sherr, C. J. (1992) · Cell · doi:10.1016/0092-8674(92)90360-o · Cited by 897
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Cited by
Meijer, L., Borgne, A., Mulner, O., Chong, J. P. J., Blow, J. J., Inagaki, N., Inagaki, M., Delcros, J., & Moulinoux, J. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-2-00527.x · Cited by 1,352
Self-citationThe influence of natural products upon drug discovery (Antiquity to late 1999)
Newman, D. J., Cragg, G. M., & Snader, K. M. (2000) · Natural Product Reports · doi:10.1039/a902202c · Cited by 1,293
De Azevedo, W. F., Leclerc, S., Meijer, L., Havlicek, L., Strnad, M., & Kim, S. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0518a.x · Cited by 729
Self-citationInhibition of Cyclin‐Dependent Kinases by Purine Analogues
Veselý, J., Havliček, L., Strnad, M., Blow, J. J., Donella‐Deana, A., Pinna, L., Letham, D. S., Kato, J., Detivaud, L., Leclerc, S., et al. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00771.x · Cited by 632
Self-citationPharmacological inhibitors of cyclin-dependent kinases
Knockaert, M., Greengard, P., & Meijer, L. (2002) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(02)02071-0 · Cited by 537
Self-citation
Metadata
- Authors
- Schulze‐Gahmen, U., Brandsen, J., Jones, H. D., Morgan, D. O., Meijer, L., Vesely, J., & Kim, S.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 1995-08
- Volume
- 22
- Issue
- 4
- Pages
- 378-391
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2160053097
- Cited by
- 279
- References
- 4
- FWCI
- 6.63
- 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: Multiple modes of ligand recognition: Crystal structures of cyclin‐dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine. https://app.cochat.ai/papers/10.1002/prot.340220408
- The paper
- Schulze‐Gahmen, U., Brandsen, J., Jones, H. D., Morgan, D. O., Meijer, L., Vesely, J., & Kim, S. (1995). Multiple modes of ligand recognition: Crystal structures of cyclin‐dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340220408
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.