William Michael Kavanaugh M.D.
Cardiologist | Cardiovascular Disease
4150 Clement St Department 111c San Francisco CA, 94121About
Dr. William Kavanaugh is a cardiologist practicing in San Francisco, CA. Dr. Kavanaugh specializes in diagnosing, monitoring, and treating diseases or conditions of the heart and blood vessels and the cardiovascular system. These conditions include heart attacks, heart murmurs, coronary heart disease, and hypertension. Dr. Kavanaugh also practices preventative medicine, helping patients maintain a heart-healthy life.
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM- Cardiovascular Disease
Provider Details
Expert Publications
Data provided by the National Library of Medicine- A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells.
- Semirational design of a potent, artificial agonist of fibroblast growth factor receptors.
- Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells.
- A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine.
- cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF beta-receptor.
- Deorphanization of the human leukocyte tyrosine kinase (LTK) receptor by a
- In vivo imaging of protease activity by Probody therapeutic activation.
- Serotonin-induced deoxyribonucleic acid synthesis in vascular smooth muscle cells involves a novel, pertussis toxin-sensitive pathway.
- An alternative to SH2 domains for binding tyrosine-phosphorylated proteins.
- PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine.
- Tyrosine 508 of the 85-kilodalton subunit of phosphatidylinositol 3-kinase is phosphorylated by the platelet-derived growth factor receptor.
- Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors.
- Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways.
- A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain.
- SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase.
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