Dr. Henry S Earp MD
Endocrinology-Diabetes | Endocrinology, Diabetes & Metabolism
Lineberger Comprehensive Cancer Center 450 West Drive Cb 72 Chapel Hill NC, 27599About
Dr. Henry Earp practices Endocrinology in Chapel Hill, NC. Dr. Earp specializes in preventing, diagnosing, and treating diseases related to hormone imbalance, and the bodys glands in the endocrine system. Endocrinologists are trained and certified to treat a variety of conditions, including menopause, diabetes, infertility, and thyroid disorders, among many others. Dr. Earp examines patients, determines means of testing, diagnoses, and decides the best treatment methods.
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Interactions between two cytoskeleton-associated tyrosine kinases: calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase.
- A novel receptor tyrosine kinase, Mer, inhibits TNF-alpha production and lipopolysaccharide-induced endotoxic shock.
- Tyro-3 family receptors are essential regulators of mammalian spermatogenesis.
- Regulation of carbamoyl phosphate synthetase by MAP kinase.
- Inhibition of the calcium-dependent tyrosine kinase (CADTK) blocks monocyte spreading and motility.
- Alterations in hepatic chromatin template availability during infection.
- Phagocytosis and clearance of apoptotic cells is mediated by MER.
- Her4 mediates ligand-dependent antiproliferative and differentiation responses in human breast cancer cells.
- Platelet-derived growth factor (PDGF) alpha receptor activation modulates the calcium mobilizing activity of the PDGF beta receptor in Balb/c3T3 fibroblasts.
- Calcium-dependent increase in tyrosine kinase activity stimulated by angiotensin II.
- Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.
- Regulation of hepatic nuclear guanylate cyclase.
- Regulation of hepatic nuclear guanylate cyclase.
- Transient epidermal growth factor (EGF)-dependent suppression of EGF receptor autophosphorylation during internalization.
- Evidence that the epidermal growth factor receptor and non-tyrosine kinase hormone receptors stimulate phosphoinositide hydrolysis by independent pathways.
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