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Mary Ann Cheatham
Researcher at Northwestern University
Publications - 90
Citations - 3213
Mary Ann Cheatham is an academic researcher from Northwestern University. The author has contributed to research in topics: Hair cell & Prestin. The author has an hindex of 28, co-authored 87 publications receiving 2958 citations.
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Journal ArticleDOI
Two-tone suppression in inner hair cell responses: correlates of rate suppression in the auditory nerve.
Mary Ann Cheatham,Peter Dallos +1 more
TL;DR: A proposal is advanced to explain the evolution of two-tone suppression in the peripheral auditory system and the use of excitatory versus non-excitatory suppressors and the explanation of low-side suppression areas is of special interest.
Journal ArticleDOI
Summating potential (SP) tuning curves.
Mary Ann Cheatham,Peter Dallos +1 more
TL;DR: Two methods were used to extract frequency specific information from the gross d.c. cochlear potential, the summating potential, to derive SP tuning curves using a two-tone simultaneous masking procedure and to obtain SP iso-response functions.
Journal ArticleDOI
Identifying components of the hair-cell interactome involved in cochlear amplification
TL;DR: A group of de novo genes closely associated with known deafness loci identified, and the data indicate that the hair cell tip link interacts directly with calcium binding proteins, shed light on some protein networks in cochlear hair cells.
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Low-frequency modulation of inner hair cell and organ of Corti responses in the guinea pig cochlea
Mary Ann Cheatham,Peter Dallos +1 more
TL;DR: An attempt is made to relate bias-induced changes in hair cell receptor potentials to modulations in single-unit rate responses to address variations in the temporal relationships between excitation and suppression measured in the auditory nerve.
Journal ArticleDOI
Cadherin 23-C Regulates Microtubule Networks by Modifying CAMSAP3's Function.
Satoe Takahashi,Vincent J. Mui,Samuel K. Rosenberg,Kazuaki Homma,Mary Ann Cheatham,Jing Zheng +5 more
TL;DR: It is demonstrated that the C isoform of CDH23 (CDH23-C) directly binds to CAMSAP3/Marshalin and modifies its function by inhibiting CAMS AP3/ Marshalin-induced bundle formation, a process that requires a tubulin-binding domain called CKK.