The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Interaction of a Protein Phosphatase with an Arabidopsis Serine-Threonine Receptor Kinase
Abstract
A protein phosphatase was cloned that interacts with a serine-threonine receptor-like kinase, RLK5, from Arabidopsis thaliana . The phosphatase, designated KAPP (kinase-associated protein phosphatase), is composed of three domains: an amino-terminal signal anchor, a kinase interaction (KI) domain, and a type 2C protein phosphatase catalytic region. Association of RLK5 with the KI domain is dependent on phosphorylation of RLK5 and can be abolished by dephosphorylation. KAPP may function as a signaling component in a pathway involving RLK5.
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Cites
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Cited by
A Putative Leucine-Rich Repeat Receptor Kinase Involved in Brassinosteroid Signal Transduction
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Brassinosteroids Plant counterparts to animal steroid hormones?
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Metadata
- Authors
- Stone, J. M., Collinge, M. A., Smith, R. D., Horn, M. A., & Walker, J. C.
- Venue
- Science
- Published
- 1994-11-04
- Volume
- 266
- Issue
- 5186
- Pages
- 793-795
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1974325028
- Cited by
- 272
- References
- 33
- FWCI
- 5.27
- Type
- journal article
- Language
- en
- Open access
- closed
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- Stone, J. M., Collinge, M. A., Smith, R. D., Horn, M. A., & Walker, J. C. (1994). Interaction of a Protein Phosphatase with an Arabidopsis Serine-Threonine Receptor Kinase. Science. https://doi.org/10.1126/science.7973632
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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.
