The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
A Structural Basis for Substrate Specificities of Protein Ser/Thr Kinases: Primary Sequence Preference of Casein Kinases I and II, NIMA, Phosphorylase Kinase, Calmodulin-Dependent Kinase II, CDK5, and Erk1
Open accessAbstract
We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified substrate specificities of these kinases, together with known crystal structures of protein kinase A, CDK2, Erk2, twitchin, and casein kinase I, provide a structural basis for the substrate recognition of protein Ser/Thr kinases. In particular, the specific selection of amino acids at the +1 and -3 positions to the substrate serine/threonine can be rationalized on the basis of sequences of protein kinases. The identification of optimal peptide substrates of CDK5, casein kinases I and II, NIMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the potential in vivo targets of these kinases.
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Self-citationMechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
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[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
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Use of an oriented peptide library to determine the optimal substrates of protein kinases
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Self-citationAtomic structure of the MAP kinase ERK2 at 2.3 A resolution
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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
Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
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Mechanisms of specificity in protein phosphorylation
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Large-scale characterization of HeLa cell nuclear phosphoproteins
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Self-citationOne‐thousand‐and‐one substrates of protein kinase CK2?
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Metadata
- Authors
- Songyang, Z., Lu, K. P., Kwon, Y. T., Tsai, L.-H., Filhol, O., Cochet, C., Brickey, D. A., Soderling, T. R., Bartleson, C., Graves, D. J., DeMaggio, A. J., Hoekstra, M. F., Blenis, J., Hunter, T., & Cantley, L. C.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1996-11
- Volume
- 16
- Issue
- 11
- Pages
- 6486-6493
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2168259122
- Cited by
- 549
- References
- 23
- FWCI
- 9.15
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: A Structural Basis for Substrate Specificities of Protein Ser/Thr Kinases: Primary Sequence Preference of Casein Kinases I and II, NIMA, Phosphorylase Kinase, Calmodulin-Dependent Kinase II, CDK5, and Erk1. https://app.cochat.ai/papers/10.1128/mcb.16.11.6486
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- Songyang, Z., Lu, K. P., Kwon, Y. T., Tsai, L.-H., Filhol, O., Cochet, C., Brickey, D. A., Soderling, T. R., Bartleson, C., Graves, D. J., DeMaggio, A. J., Hoekstra, M. F., Blenis, J., Hunter, T., & Cantley, L. C. (1996). A Structural Basis for Substrate Specificities of Protein Ser/Thr Kinases: Primary Sequence Preference of Casein Kinases I and II, NIMA, Phosphorylase Kinase, Calmodulin-Dependent Kinase II, CDK5, and Erk1. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.16.11.6486
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