The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Protein Tyrosine Kinase Structure and Function
Abstract
▪ Abstract Tyrosine phosphorylation is one of the key covalent modifications that occurs in multicellular organisms as a result of intercellular communication during embryogenesis and maintenance of adult tissues. The enzymes that carry out this modification are the protein tyrosine kinases (PTKs), which catalyze the transfer of the γ phosphate of ATP to tyrosine residues on protein substrates. Phosphorylation of tyrosine residues modulates enzymatic activity and creates binding sites for the recruitment of downstream signaling proteins. Two classes of PTKs are present in cells: the transmembrane receptor PTKs and the nonreceptor PTKs. Because PTKs are critical components of cellular signaling pathways, their catalytic activity is strictly regulated. Over the past several years, high-resolution structural studies of PTKs have provided a molecular basis for understanding the mechanisms by which receptor and nonreceptor PTKs are regulated. This review will highlight the important results that have emerged from these structural studies.
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Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
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Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
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Metadata
- Authors
- Hubbard, S. R., & Till, J. H.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2000-06
- Volume
- 69
- Issue
- 1
- Pages
- 373-398
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2104812730
- Cited by
- 1,171
- References
- 3
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- closed
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