J T Parsons focuses on Tyrosine phosphorylation, Molecular biology, Proto-oncogene tyrosine-protein kinase Src, PTK2 and SH3 domain. His study with Tyrosine phosphorylation involves better knowledge in Phosphorylation. His study looks at the relationship between Molecular biology and fields such as Receptor tyrosine kinase, as well as how they intersect with chemical problems.
Proto-oncogene tyrosine-protein kinase Src is closely attributed to Protein tyrosine phosphatase in his work. His PTK2 research is multidisciplinary, incorporating elements of Cyclin-dependent kinase 9, Integrin, Paxillin, Focal adhesion and Focal Adhesion Kinase 2. His SH3 domain research integrates issues from Podosome, Peptide sequence, SH2 domain, Actin and Subcellular localization.
His primary scientific interests are in Proto-oncogene tyrosine-protein kinase Src, Cell biology, Molecular biology, Tyrosine phosphorylation and Phosphorylation. His studies deal with areas such as Avian sarcoma virus, Tyrosine kinase and Receptor tyrosine kinase as well as Proto-oncogene tyrosine-protein kinase Src. In Cell biology, J T Parsons works on issues like Cytoskeleton, which are connected to Actin.
His Molecular biology research is multidisciplinary, incorporating perspectives in Phenotype, Transfection and Protein kinase A. His Tyrosine phosphorylation research focuses on Protein phosphorylation and how it connects with LYN. In his research on the topic of Phosphorylation, Epidermal growth factor, Kinase and Cellular proteins is strongly related with Tyrosine.
J T Parsons spends much of his time researching Cell biology, Focal adhesion, Cell adhesion, Molecular biology and Computational biology. The study incorporates disciplines such as Cell cycle and Cytoskeleton in addition to Cell biology. His work deals with themes such as Neurite, Cell morphology and CDC42, GTPase, which intersect with Focal adhesion.
J T Parsons has included themes like Cell migration, Cell movement and Myosin in his Cell adhesion study. J T Parsons performs multidisciplinary study in Molecular biology and Vascular smooth muscle in his work. J T Parsons has researched Computational biology in several fields, including Tyrosine kinase, Genetics, Proto-oncogene tyrosine-protein kinase Src and Cdna cloning.
J T Parsons mainly investigates Cell biology, Cell adhesion, Focal adhesion, Cell migration and Microtubule dynamics. His work on Cytoskeleton expands to the thematically related Cell biology. His Cytoskeleton research incorporates elements of Cell morphology, CDC42, GTPase and Neurite.
His work carried out in the field of Cell migration brings together such families of science as Cell movement and Myosin. His Extracellular matrix research incorporates themes from Molecular biology, Platelet-derived growth factor, Platelet-derived growth factor receptor and Ectopic expression. His work on Stress fiber is being expanded to include thematically relevant topics such as Actin.
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pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.
M D Schaller;C A Borgman;B S Cobb;R R Vines.
Proceedings of the National Academy of Sciences of the United States of America (1992)
Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src.
M D Schaller;J D Hildebrand;J D Shannon;J W Fox.
Molecular and Cellular Biology (1994)
Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.
L Kornberg;H S Earp;J T Parsons;M Schaller.
Journal of Biological Chemistry (1992)
Focal Adhesion Kinase: a regulator of focal adhesion dynamics and cell movement
J T Parsons;K H Martin;J K Slack;J M Taylor.
Oncogene (2000)
Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains.
M D Schaller;C A Otey;J D Hildebrand;J T Parsons.
Journal of Cell Biology (1995)
Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets.
L Lipfert;B Haimovich;M D Schaller;B S Cobb.
Journal of Cell Biology (1992)
pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk.
M D Schaller;J T Parsons.
Molecular and Cellular Biology (1995)
Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK.
B. S. Cobb;M. D. Schaller;Tzeng-Horng Leu;J. T. Parsons.
Molecular and Cellular Biology (1994)
Focal adhesion kinase and associated proteins
M D Schaller;J T Parsons.
Current Opinion in Cell Biology (1994)
Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex.
Hong Wu;J. T. Parsons.
Journal of Cell Biology (1993)
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