John Malloy O.T.
Occupational Therapist
185 WOODY CIRCLE TRYON NC, 28782About
Dr. John Malloy practices Occupational Medicine in TRYON, NC. Dr. Malloy 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- Interaction of nucleotides with Asp(351) and the conserved phosphorylation loop of sarcoplasmic reticulum Ca(2+)-ATPase.
- Fast kinetic analysis of conformational changes in mutants of the Ca(2+)-ATPase of sarcoplasmic reticulum.
- Importance of stalk segment S5 for intramolecular communication in the sarcoplasmic reticulum Ca2+-ATPase.
- Importance of transmembrane segment M3 of the sarcoplasmic reticulum Ca2+-ATPase
- Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.
- ATP binding residues of sarcoplasmic reticulum Ca2+-ATPase.
- Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin.
- Deduced amino acid sequence and E1-E2 equilibrium of the sarcoplasmic reticulum Ca(2+)-ATPase of frog skeletal muscle. Comparison with the Ca(2+)-ATPase of rabbit fast twitch muscle.
- Mutational analysis of the role of Glu309 in the sarcoplasmic reticulum Ca(2+)-ATPase of frog skeletal muscle.
- Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca(2+)-ATPase of sarcoplasmic reticulum.
- Structural basis for the E1/E1P-E2/E2P conformation changes in the sarcoplasmic reticulum Ca(2+)-ATPase studied by site-specific mutagenesis.
- Mutational analysis of the role of Lys684 in the Ca(2+)-ATPase of sarcoplasmic reticulum.
- CrATP-induced Ca2+ occlusion in mutants of the Ca(2+)-ATPase of sarcoplasmic reticulum.
- Functional consequences of alterations to Gly310, Gly770, and Gly801 located in the transmembrane domain of the Ca(2+)-ATPase of sarcoplasmic reticulum.
- Interdependence of Ca2+ occlusion sites in the unphosphorylated sarcoplasmic reticulum Ca(2+)-ATPase complex with CrATP.
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RUTHERFORD REGIONAL MEDICAL CENTERl
288 SOUTH RIDGECREST AVE RUTHERFORDTON NC 28139MARGARET R PARDEE MEMORIAL HOSPITALl
800 N JUSTICE ST HENDERSONVILLE NC 28791ST LUKES HOSPITALl
101 HOSPITAL DRIVE COLUMBUS NC 28722