David Benjamin Mcintosh DPT
Physical Therapist
4802 S 109th East Ave Tulsa OK, 74146About
David Mcintosh is a physical therapist practicing in Tulsa, OK. David Mcintosh 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, David Mcintosh can treat multiple conditions with exercises, ultrasound, electrical stimulation, joint mobilization, heat, ice, massage, laser or light therapy and more. David Mcintosh 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.
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Expert Publications
Data provided by the National Library of Medicine- Importance of conserved N-domain residues Thr441, Glu442, Lys515, Arg560, and Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site.
- Glutamate-183 in the conserved TGES motif of domain A of sarcoplasmic reticulum Ca2+-ATPase assists in catalysis of E2/E2P partial reactions.
- Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+-activated states of sarcoplasmic reticulum Ca2+-ATPase.
- Structural studies of a stabilized phosphoenzyme intermediate of Ca2+-ATPase.
- Asparagine 706 and glutamate 183 at the catalytic site of sarcoplasmic reticulum Ca2+-ATPase play critical but distinct roles in E2 states.
- Purification of human malaria parasite hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT) using immobilized Reactive Red 120.
- ATP-binding modes and functionally important interdomain bonds of sarcoplasmic reticulum Ca2+-ATPase revealed by mutation of glycine 438, glutamate 439, and arginine 678.
- Unexpected phosphoryl transfer from Asp351 to fluorescein attached to Lys515 in sarcoplasmic reticulum Ca2+-ATPase.
- Critical interaction of actuator domain residues arginine 174, isoleucine 188, and lysine 205 with modulatory nucleotide in sarcoplasmic reticulum Ca2+-ATPase.
- Modulatory ATP binding affinity in intermediate states of E2P dephosphorylation of sarcoplasmic reticulum Ca2+-ATPase.
- Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca(2+)-ATPase by Competitive Inhibition of [γ-(32)P]TNP-8N3-ATP Photolabeling.
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