Tyrosine phosphorylation: thirty years and counting
By T. Hunter. Current Opinion in Cell Biology, 2009
664 citations recorded by the source corpus.
In the 30 years since its discovery, tyrosine phosphorylation has emerged as a fundamentally important mechanism of signal transduction and regulation in all eukaryotic cells, governing many processes, including cell proliferation, cell cycle progression, metabolic homeostasis, transcriptional activation, neural transmission, differentiation and development, and aging. Perturbations in tyrosine phosphorylation underlie many human diseases, and in particular cancer, and this has prompted the development of inhibitors of tyrosine kinases implicated in disease, a number of which have been approved for clinical use. The following is a brief personal reflection on some of the salient findings over the past 30 years that led to the development of tyrosine kinase inhibitors for disease therapy.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/f2c7ceb74334212b13ed86cfb4867b211d638d07
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In Molecular Biology
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Citations in the corpus
- The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review) (2017, neutral): “The latter can phosphorylate STKs and TKs (17); at least 125 of the human protein kinases are STKs (18).”
- Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. (2014, background): “There are several reasons for the relatively low number of Tyr phosphorylation events (Hunter, 2009).”
- Protein Kinases: Evolution of Dynamic Regulatory Proteins (2010, background): “The tremendous diversity of the protein kinase family was later revealed when Src, the transforming protein from Rous Sarcoma Virus, was discovered to be a kinase that phosphorylates tyrosine rather than serine or threonine [3].”
- Feedback regulation of EGFR signalling: decision making by early and delayed loops (2011, background): “The availability of the first GF–RTK pair spearheaded a new research field of signal transduction by Tyr phosphorylatio”