Mr. David John O'connell P.T.
Physical Therapist
1455 S Michigan Ave Suite 230 Chicago IL, 60605About
David O'connell is a physical therapist practicing in Chicago, IL. David O'connell 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 O'connell can treat multiple conditions with exercises, ultrasound, electrical stimulation, joint mobilization, heat, ice, massage, laser or light therapy and more. David O'connell 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- Integrated protein array screening and high throughput validation of 70 novel neural calmodulin-binding proteins.
- Identification of a high-affinity network of secretagogin-binding proteins involved in vesicle secretion.
- Protein networks involved in vesicle fusion, transport, and storage revealed by array-based proteomics.
- Probing calmodulin protein-protein interactions using high-content protein arrays.
- Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation.
- CHD5 is required for neurogenesis and has a dual role in facilitating gene expression and polycomb gene repression.
- Sorcin links calcium signaling to vesicle trafficking, regulates Polo-like kinase 1 and is necessary for mitosis.
- CX3CL1 is up-regulated in the rat hippocampus during memory-associated synaptic plasticity.
- Virtual screening using combinatorial cyclic peptide libraries reveals protein interfaces readily targetable by cyclic peptides.
- A chromatin-independent role of Polycomb-like 1 to stabilize p53 and promote cellular quiescence.
- Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease?
- A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions.
- Identification of α-helix 4 (α4) of Rab11a as a novel Rab11-binding domain (RBD): Interaction of Rab11a with the Prostacyclin Receptor.
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