Mable Annette Mcdonal
Occupational Therapist (Pediatric) | Pediatrics
673 BAYWOOD POINTE MADISON MS, 39110About
Dr. Mable Mcdonal practices Occupational Medicine in MADISON, MS. Dr. Mcdonal evaluates the interaction between work and health. Occupational medicine physicians have general knowledge of worksite operations and are familiar with the toxic properties of materials used by employees and the potential hazards and stressors of work processes; in addition to being qualified to determine an employees physical and emotional fitness for work; diagnosing and treating occupational diseases; handling work related injuries; and having an understanding of rehabilitation methods, health education techniques, sanitation, and workers compensation laws.
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Data provided by the National Library of Medicine- N- and C-terminal domains direct cell type-specific sorting of chromogranin A to secretory granules.
- Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains.
- Evidence supporting a late Golgi location for lactosylceramide to ganglioside GM3 conversion.
- The DXD motif is required for GM2 synthase activity but is not critical for
- T3-activation of the rat growth hormone gene is inhibited by a zinc finger/homeodomain protein.
- Developmental and functional evidence of a role for Zfhep in neural cell development.
- Isoform-specific thyroid hormone receptor antibodies detect multiple thyroid hormone receptors in rat and human pituitaries.
- Parotid secretory granules: crossroads of secretory pathways and protein storage.
- Isolation and characterization of a cDNA encoding a chicken beta thyroid hormone receptor.
- 3,5,3'-triiodothyronine receptor auxiliary protein (TRAP) enhances receptor binding by interactions within the thyroid hormone response element.
- Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers.
- Thyroid hormone receptor mutations that interfere with transcriptional activation also interfere with receptor interaction with a nuclear protein.
- Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor.
- Basal and thyroid hormone receptor auxiliary protein-enhanced binding of thyroid hormone receptor isoforms to native thyroid hormone response elements.
- A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements.
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