Dr. Melissa Diane Tsai PT, DPT
Physical Therapist
1061 Harmon Avenue Suite 1d03 Fort Stewart GA, 31314About
Melissa Tsai is a physical therapist practicing in Fort Stewart, GA. Melissa Tsai specializes in physical treatment to help a patient reduce pain, restore mobility, rehabilitate an injury, or increase movement and overall function. As a physical therapist, Melissa Tsai can treat multiple conditions with exercises, ultrasound, electrical stimulation, joint mobilization, heat, ice, massage, laser or light therapy and more. Melissa Tsai will create a treatment plan based on the patients specific injury or condition, and might target a specific body part or body system based on the individual.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Structural analysis of phospholipase A2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network.
- Structural analysis of phospholipase A2 from functional perspective. 2. Characterization of a molten globule-like state induced by site-specific mutagenesis.
- Tumor suppressor INK4: determination of the solution structure of p18INK4C and demonstration of the functional significance of loops in p18INK4C and p16INK4A.
- Contributions of residues of pancreatic phospholipase A2 to interfacial binding, catalysis, and activation.
- Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity.
- Diagnosis of herniated intervertebral disc assisted by 3-dimensional, multiaxial, magnetic resonance imaging.
- Tumor suppressor INK4: comparisons of conformational properties between p16(INK4A) and p18(INK4C).
- Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.
- Tumor suppressor INK4: quantitative structure-function analyses of p18INK4C as an inhibitor of cyclin-dependent kinase 4.
- Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data.
- II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides.
- Structural basis of the anionic interface preference and kcat* activation of pancreatic phospholipase A2.
- DNA polymerase beta: contributions of template-positioning and dNTP triphosphate-binding residues to catalysis and fidelity.
- Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9.
- Somatic INK4a-ARF locus mutations: a significant mechanism of gene inactivation in squamous cell carcinomas of the head and neck.
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