Kimberly Hibbs RDH
Dental Hygienist
6600 VAN AALST BLVD FORT BENNING GA, 31905About
Kimberly Hibbs RDH is a top Dental Hygienist in FORT BENNING, GA. With a passion for the field and an unwavering commitment to their specialty, Kimberly Hibbs RDH is an expert in changing the lives of their patients for the better. Through their designated cause and expertise in the field, Kimberly Hibbs RDH is a prime example of a true leader in health care. As a leader and expert in their field, Kimberly Hibbs RDH is passionate about enhancing patient quality of life. They embody the values of communication, safety, and trust when dealing directly with patients. In FORT BENNING, GA, Kimberly Hibbs RDH is a true asset to their field and dedicated to the profession of medicine.
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Expert Publications
Data provided by the National Library of Medicine- The structural basis of paramyxovirus invasion.
- Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.
- Sendai virus recombinant vaccine expressing hPIV-3 HN or F elicits protective immunity and combines with a second recombinant to prevent hPIV-1, hPIV-3 and RSV infections.
- Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.
- Human PIV-2 recombinant Sendai virus (rSeV) elicits durable immunity and combines with two additional rSeVs to protect against hPIV-1, hPIV-2, hPIV-3, and RSV.
- Effect of hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 on growth and pathogenicity of Sendai/human parainfluenza type 3 chimera virus in mice.
- Residues in the heptad repeat a region of the fusion protein modulate the virulence of Sendai virus in mice.
- The pH of activation of the hemagglutinin protein regulates H5N1 influenza virus pathogenicity and transmissibility in ducks.
- Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin.
- An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli.
- The receptor-binding domain of influenza virus hemagglutinin produced in Escherichia coli folds into its native, immunogenic structure.
- Illumination of parainfluenza virus infection and transmission in living animals reveals a tissue-specific dichotomy.
- Stalking influenza diversity with a universal antibody.
- Acid stability of the hemagglutinin protein regulates H5N1 influenza virus
- The pH of activation of the hemagglutinin protein regulates H5N1 influenza virus replication and pathogenesis in mice.
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