Dr. David Bryan Hicks DO, MPH
Family Practitioner
390 N Broadway Concorde Professiona Pennsville NJ, 08070About
Dr. David Hicks is a family practitioner practicing in Pennsville, NJ. Dr. Hicks specializes in comprehensive health care for people of all ages. In addition to diagnosing and treating illnesses, family practitioners also put focus on preventative care with routine checkups, tests and personalized coaching on how to maintain a healthy lifestyle. Dr. Hicks possesses immense general knowledge on maintaining health and today, family practitioners provide more care for the underserved and rural populations than any other medical specialty.
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Expert Publications
Data provided by the National Library of Medicine- A tenth atp gene and the conserved atpI gene of a Bacillus atp operon have a role in Mg2+ uptake.
- An evaluation of detergents for NMR structural studies of membrane proteins.
- Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of Alkaliphilic Bacillus with the Bacillus consensus sequence results in defective oxidative phosphorylation and non-fermentative growth at pH 10.5.
- pKa of the essential Glu54 and backbone conformation for subunit c from the H+-coupled F1F0 ATP synthase from an alkaliphilic Bacillus.
- The Mrp Na+/H+ antiporter increases the activity of the malate:quinone oxidoreductase of an Escherichia coli respiratory mutant.
- The activity profile of the NhaD-type Na+(Li+)/H+ antiporter from the soda Lake Haloalkaliphile Alkalimonas amylolytica is adaptive for the extreme environment.
- Interaction between cytochrome caa3 and F1F0-ATP synthase of alkaliphilic Bacillus pseudofirmus OF4 is demonstrated by saturation transfer electron paramagnetic resonance and differential scanning calorimetry assays.
- Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host.
- Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4.
- Characterization of the Functionally Critical AXAXAXA and PXXEXXP Motifs of the ATP Synthase c-Subunit from an Alkaliphilic Bacillus.
- Cation/proton antiporter complements of bacteria: why so large and diverse?
- F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.
- A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring.
- The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.
- ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry.
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