Dr. Thomas John Baranski MD
Endocrinology-Diabetes | Endocrinology, Diabetes & Metabolism
4570 Childrens Pl Saint Louis MO, 63110Rating
5/5
About
Dr. Thomas Baranski practices Endocrinology in Saint Louis, MO. Dr. Baranski 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. Baranski examines patients, determines means of testing, diagnoses, and decides the best treatment methods.
Education and Training
Washington Univ Sch Of Med- St Louis Mo 1992
Provider Details
Expert Publications
Data provided by the National Library of Medicine- C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.
- Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation.
- Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function.
- Functional reconstitution of the angiotensin II type 2 receptor and G(i) activation.
- An activation switch in the ligand binding pocket of the C5a receptor.
- Constitutive activation and endocytosis of the complement factor 5a receptor: evidence for multiple activated conformations of a G protein-coupled receptor.
- C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast.
- C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor.
- Lysosomal enzyme phosphorylation. I. Protein recognition determinants in both lobes of procathepsin D mediate its interaction with UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase.
- Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides.
- Essential role for the second extracellular loop in C5a receptor activation.
- Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solution NMR study using semisynthetic Galpha subunits.
- Expressed protein ligation to study protein interactions: semi-synthesis of the G-protein alpha subunit.
- Genetic analysis of the first and third extracellular loops of the C5a receptor reveals an essential WXFG motif in the first loop.
- Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting.
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ST LOUIS CHILDRENS HOSPITALl
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