Dr. Philip John Thomas D.D.S.
Dentist (Pediatric) | Pediatric Dentistry
5 Doctor Cir Longview TX, 75605About
Dr. Philip Thomas is a pediatric dentist practicing in Longview, TX. Dr. Thomas specializes in the oral health of children. Pediatric dentists tend to patients ranging in age from infancy to teenaged years. As a pediatric dentist, Dr. Thomas takes care of a childs teeth, gums and mouth. Children can face dental problems like tooth decay and gum disease without proper care. Pediatric dentists can provide dental examinations, give cleanings and treatments, repair cavitities and dental injuries like fractured or knocked-out teeth, diagnose oral conditions and more.
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Expert Publications
Data provided by the National Library of Medicine- Mutations that change the position of the putative gamma-phosphate linker in the nucleotide binding domains of CFTR alter channel gating.
- CFTR degradation and aggregation.
- In vitro CFTR folding assays.
- A protein sequence that can encode native structure by disfavoring alternate conformations.
- Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters.
- Conformational remodeling of proteasomal substrates by PA700, the 19 S regulatory complex of the 26 S proteasome.
- ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.
- The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3- cotransport isoform 3.
- Endoproteolytic activity of the proteasome.
- Assessment of protein folding/solubility in live cells.
- Organic solutes rescue the functional defect in delta F508 cystic fibrosis transmembrane conductance regulator.
- Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator.
- Dynamic control of cystic fibrosis transmembrane conductance regulator Cl(-)/HCO3(-) selectivity by external Cl(-).
- Gating of CFTR by the STAS domain of SLC26 transporters.
- Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein.
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