Michelle I Lapin PT, DPT
Physical Therapist
200 W COUNTY LINE RD STE 250 HIGHLANDS RANCH CO, 80129About
Michelle Lapin is a physical therapist practicing in HIGHLANDS RANCH, CO. Michelle Lapin specializes in physical treatment to help a patient reduce pain, restore mobility, rehabilitate an injury, or increase movement and overall function. As a physical therapist, Michelle Lapin can treat multiple conditions with exercises, ultrasound, electrical stimulation, joint mobilization, heat, ice, massage, laser or light therapy and more. Michelle Lapin will create a treatment plan based on the patients specific injury or condition, and might target a specific body part or body system based on the individual.
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Expert Publications
Data provided by the National Library of Medicine- Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis.
- A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.
- Domain deletion in the extracellular portion of the EGF-receptor reduces ligand binding and impairs cell surface expression.
- Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
- Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells.
- Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells.
- All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor.
- Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors.
- Metabolic effects induced by epidermal growth factor (EGF) in cells expressing EGF receptor mutants.
- Signal transduction by epidermal growth factor receptor.
- Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation.
- A point mutation at the ATP-binding site of the EGF-receptor abolishes signal transduction.
- Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing.
- A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis.
- The conformation of insulin-like growth factors: relationships with insulins.
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