Dr. David A Parry MD
Ear-Nose and Throat Doctor (ENT)
6320 N La Cholla Blvd Suite 300 Tucson AZ, 85741About
Dr. David Parry is an ear, nose and throat (ENT) doctor, also known as an otolaryngologist, practicing in Tucson, AZ. Dr. Parry specializes in diseases and disorders of the ear, nose and throat as well as other parts of the head and neck. Such structures an ENT may work on include the sinuses, larynx (voice box) and mouth in addition to the ear, nose and throat. There are seven areas of expertise that an ENT might specialize in, and these are: allergies; facial reconstructive surgery; head and neck; laryngology; otology/neurotology; pediatric otolaryngology; and rhinology.
Education and Training
University of Arizona College of Medicine 1999
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Tissue-specific co-expression and in vitro heteropolymer formation of the two small branchiostoma intermediate filament proteins A3 and B2.
- A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: structural analysis of trichocyte keratin.
- Cryo-electron microscopy of trichocyte (hard alpha-keratin) intermediate filaments reveals a low-density core.
- Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1.
- Modeling alpha-helical coiled-coil interactions: the axial and azimuthal alignment of 1B segments from vimentin intermediate filaments.
- Structural changes in trichocyte keratin intermediate filaments during keratinization.
- Macrofibril assembly in trichocyte (hard alpha-) keratins.
- Trichohyalin mechanically strengthens the hair follicle: multiple cross-bridging roles in the inner root shealth.
- Nucleation and growth of macrofibrils in trichocyte (hard-alpha) keratins.
- Alpha-helical coiled-coil oligomerization domains are almost ubiquitous in the collagen superfamily.
- In vivo and in vitro evidence that the four essential intermediate filament (IF) proteins A1, A2, A3 and B1 of the nematode Caenorhabditis elegans form an obligate heteropolymeric IF system.
- An unusual Ala12Thr polymorphism in the 1A alpha-helical segment of the companion layer-specific keratin K6hf: evidence for a risk factor in the etiology of the common hair disorder pseudofolliculitis barbae.
- Modeling effects of mutations in coiled-coil structures: case study using epidermolysis bullosa simplex mutations in segment 1a of K5/K14 intermediate filaments.
- Characteristic features of amino acid residues in coiled-coil protein structures.
- Fibrous proteins: new structural and functional aspects revealed.
Treatments
- Hearing Loss
- Allergies
- Ear Infection
- Birth Defects
- Hay Fever (allergic Rhinitis)
- Ear Wax
- Cleft Palate
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