Patricia Sue Pound OT
Occupational Therapist
1206 E NATIONAL AVE BRAZIL IN, 47834About
Dr. Patricia Pound practices Occupational Medicine in BRAZIL, IN. Dr. Pound 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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Expert Publications
Data provided by the National Library of Medicine- Carboxyl-terminal phosphorylation regulates the function and subcellular
- The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation.
- Genetic variation in Fitzroya cupressoides (alerce), a threatened South American conifer.
- Mechanism of A-kinase-anchoring protein 79 (AKAP79) and protein kinase C interaction.
- Akt/protein kinase B is regulated by autophosphorylation at the hypothetical
- Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol.
- Sphingosine is a novel activator of 3-phosphoinositide-dependent kinase 1.
- The development and application of molecular markers for abiotic stress tolerance in barley.
- The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain.
- p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1).
- Cellular signaling: pivoting around PDK-1.
- The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1.
- The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase.
- Membrane binding kinetics of protein kinase C betaII mediated by the C2 domain.
- Effects of population disjunction on isozyme variation in the widespread Pilgerodendron uviferum.
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