Dr. Steven E Shoelson M.D.
Endocrinology-Diabetes | Endocrinology, Diabetes & Metabolism
1 Joslin Pl Joslin Diabetes Cent Boston MA, 02215About
Dr. Steven Shoelson practices Endocrinology in Boston, MA. Dr. Shoelson 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. Shoelson examines patients, determines means of testing, diagnoses, and decides the best treatment methods.
Education and Training
Univ of Chicago, Pritzker Sch of Med, Chicago Il 1985
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Crystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1.
- Crystal structure of human frataxin.
- Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor regulation of apoptosis.
- Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkbeta.
- Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action.
- Structure of the globular tail of nuclear lamin.
- Genetic variability in insulin action inhibitor Ikkbeta (IKBKB) does not play a major role in the development of type 2 diabetes.
- Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand.
- Diabetes mutations delineate an atypical POU domain in HNF-1alpha.
- Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the association of IRS-1/IRS-2 with the insulin receptor.
- Identification and functional characterization of a novel mutation of hepatocyte nuclear factor-1alpha gene in a Korean family with MODY3.
- Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5.
- YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase.
- Substitution of the insulin receptor transmembrane domain with the c-neu/erbB2 transmembrane domain constitutively activates the insulin receptor kinase in vitro.
- Polyoma virus middle T antigen-pp60c-src complex associates with purified phosphatidylinositol 3-kinase in vitro.
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