Dr. Gregg Donald Parks D.C.
Chiropractor
500 E Philadelphia Ave Boyertown PA, 19512About
Dr. Gregg Parks is a Chiropractor practicing in Boyertown, PA. Dr. Parks specializes in preventing, diagnosing, and treating conditions associated with the neuromusculoskeletal system, while improving each patients functionality and quality of life. Conditions treated include sciatica, neck pain, and arthritis pain, among many others. Dr. Parks seeks to reduce pain and discomfort through manipulation and adjustment of the spine.
Education and Training
Doctor of Chiropractic – Palmer College of Chiropractic – ,Bachelors of Science – Michigan State University –
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Highly diverse intergenic regions of the paramyxovirus simian virus 5 cooperate with the gene end U tract in viral transcription termination and can influence reinitiation at a downstream gene.
- Spacing constraints on reinitiation of paramyxovirus transcription: the gene end U tract acts as a spacer to separate gene end from gene start sites.
- Increased readthrough transcription across the simian virus 5 M-F gene junction leads to growth defects and a global inhibition of viral mRNA synthesis.
- RNA replication from the simian virus 5 antigenomic promoter requires three sequence-dependent elements separated by sequence-independent spacer regions.
- The V protein of human parainfluenza virus 2 antagonizes type I interferon
- A novel CD8-independent high-avidity cytotoxic T-lymphocyte response directed against an epitope in the phosphoprotein of the paramyxovirus simian virus 5.
- Molecular cloning of the NP and L genes of simian virus 5: identification of highly conserved domains in paramyxovirus NP and L proteins.
- Proteolytic processing of the cardioviral P2 region: primary 2A/2B cleavage in clone-derived precursors.
- Characterization of Mengo virus neutralization epitopes.
- Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain.
- Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains.
- Folding and oligomerization properties of a soluble and secreted form of the paramyxovirus hemagglutinin-neuraminidase glycoprotein.
- Proteolytic cleavage of encephalomyocarditis virus capsid region substrates by precursors to the 3C enzyme.
- Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation.
- Site-specific mutations at a picornavirus VP3/VP1 cleavage site disrupt in vitro processing and assembly of capsid precursors.
Treatments
- Diversified
- Gonstead
- Activator Methods
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