Genetics & Hearing Loss (Genetics and Hearing Loss) by Charles I. Berlin, Bronya J. Keats

By Charles I. Berlin, Bronya J. Keats

For medical researchers in audiology and otolaryngology, this 5th publication within the Kresge- Mirmelstein Award sequence good points the complaints of the 1998 symposium. The ebook contains contributions from best researchers on genetic explanations of listening to loss and contains a CD-ROM containing audio and video pictures from a Balinese village with a wide genetically deaf inhabitants that experience followed an indication language indigenous to their tradition. The CD-ROM additionally positive aspects samples of yankee signal Language and Cued Speech. within the culture of Berlin's past paintings this publication provides attractive new and evocative info for either researchers and clinicians.

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Steel, K. P. (1993). Light (Blt), a mutation causing melanocyte death, leads to strial dysfunction in the inner ear. Pigment Cell Research, 6, 215–225. , Jackson, I. J. & Steel, K. P. (1995). Mutations at the W locus affect survival of neural crest-derived melanocytes in the mouse. Mechanisms of Development, 50, 139–150. , & Steel, K. P. (1998). Combined cochleo-saccular and neuroepithelial abnormalities in the Varitint-waddler-J (VaJ) mouse. Hearing Research, 123, 125–136. , & Thorne, T. (1999).

Figure 2–4. The stereocilia of shaker-2 mutants are abnormally short. The stereocilia on a single outer hair cell from the cochlea of a normal mouse (left panel) shows long stereocilia arranged in a V-shaped array. A comparable outer hair cell from a shaker-2 mutant (right panel) has stereocilia arranged in the typical pattern, but these stereocilia are markedly reduced in size (ϳ7500ϫ magnification in both panels). 42 GENETICS AND HEARING LOSS EPIDEMIOLOGY OF DFNB3 Once the mutation in MYO15 segregating in Bengkala was identified, it became possible to determine the carrier frequency of this mutation among hearing individuals from Bengkala who have no known deaf relatives.

Like all myosins, myosin-15 has a highly conserved motor domain that contains an actin and an ATP binding sites. Upstream of the motor domain is a novel 1223 amino acid N-terminal domain. Downstream of the motor domain are two IQ motifs that are predicted to interact with calmodulin or related calcium binding proteins. Based on similarity to regions observed in other proteins, several functional domains are recognizable within the myosin-15 tail. , 1998). Additional similarity with other proteins was observed in the region encoded by exons 43 to 48.

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