[54] Use of recombinant baculoviruses and 1H nuclear magnetic resonance to study tyrosine phosphorylation by a soluble insulin receptor protein-tyrosine kinase
- 1 January 1991
- book chapter
- Published by Elsevier
- Vol. 200, 660-669
- https://doi.org/10.1016/0076-6879(91)00178-y
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Insulin receptor tyrosine kinase structure and functionBiochemical Society Transactions, 1991
- Phosphorylation of tyrosines 1158, 1162 and 1163 on a synthetic dodecapeptide by the insulin receptor protein-tyrosine kinaseBiochemical and Biophysical Research Communications, 1991
- Secretion of the extracellular domain of the human insulin receptor from insect cells by use of a baculovirus vectorBiochemical Journal, 1989
- Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mappingBiochemical Journal, 1988
- Protein Carbon-13 Spin Systems by a Single Two-Dimensional Nuclear Magnetic Resonance ExperimentScience, 1988
- Three-dimensional NMR spectroscopy of a protein in solutionNature, 1988
- Truncation of the ectodomain of the human insulin receptor results in secretion of a soluble insulin binding protein from transfected CHO cellsJournal of Molecular Recognition, 1988
- Trends in the Development of Baculovirus Expression VectorsNature Biotechnology, 1988
- The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signallingCell, 1985
- Human insulin receptor and its relationship to the tyrosine kinase family of oncogenesNature, 1985