A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation
- 8 March 2001
- journal article
- Published by Springer Nature in Oncogene
- Vol. 20 (10) , 1229-1234
- https://doi.org/10.1038/sj.onc.1204215
Abstract
Oncogene is one of the world’s leading cancer journals. It is published weekly and covers all aspects of the structure and function of Oncogenes. Oncogene also publishes 8 Reviews issues a year, on a broad range of topics.Keywords
This publication has 35 references indexed in Scilit:
- Role of the TFG N-terminus and coiled-coil domain in the transforming activity of the thyroid TRK-T3 oncogeneOncogene, 1998
- Sequence profiles of immunoglobulin and immunoglobulin-like domainsJournal of Molecular Biology, 1997
- Ligand-independent Activation of Fibroblast Growth Factor Receptors by Point Mutations in the Extracellular, Transmembrane, and Kinase DomainsJournal of Biological Chemistry, 1996
- Deletions in the Extracellular Domain of Rat TrkA Lead to an Altered Differentiative Phenotype in Neurotrophin Responsive CellsMolecular and Cellular Neuroscience, 1996
- Physiology of the NeurotrophinsAnnual Review of Neuroscience, 1996
- Brain-derived neurotrophic factor, neurotrophin-3, and neurotrophin-4 bind to a single leucine-rich motif of TrkBBiochemistry, 1995
- NGF Binding to the trk Tyrosine Kinase Receptor Requires the Extracellular Immunoglobulin-like DomainsMolecular and Cellular Neuroscience, 1995
- Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndromeNature Genetics, 1995
- The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transductionCell, 1995
- PC12 cell mutants that possess low- but not high-affinity nerve growth factor receptors neither respond to nor internalize nerve growth factor.The Journal of cell biology, 1986