scholarly journals In vivo imaging of middle-ear and inner-ear microstructures of a mouse guided by SD-OCT combined with a surgical microscope

2014 ◽  
Vol 22 (8) ◽  
pp. 8985 ◽  
Author(s):  
Nam Hyun Cho ◽  
Jeong Hun Jang ◽  
Woonggyu Jung ◽  
Jeehyun Kim
2016 ◽  
Vol 8 (1) ◽  
pp. 260 ◽  
Author(s):  
Noah Bedard ◽  
Timothy Shope ◽  
Alejandro Hoberman ◽  
Mary Ann Haralam ◽  
Nader Shaikh ◽  
...  

2014 ◽  
Vol 35 (4) ◽  
pp. 725-729 ◽  
Author(s):  
Sylvia L. van Egmond ◽  
Fredy Visser ◽  
Frank A. Pameijer ◽  
Wilko Grolman

2006 ◽  
Vol 95 (5) ◽  
pp. 2951-2961 ◽  
Author(s):  
Wei Dong ◽  
Elizabeth S. Olson

The middle ear transmits environmental sound to the inner ear. It also transmits acoustic energy sourced within the inner ear out to the ear canal, where it can be detected with a sensitive microphone as an otoacoustic emission. Otoacoustic emissions are an important noninvasive measure of the condition of sensory hair cells and to use them most effectively one must know how they are shaped by the middle ear. In this contribution, forward and reverse transmissions through the middle ear were studied by simultaneously measuring intracochlear pressure in scala vestibuli near the stapes and ear canal pressure. Measurements were made in gerbil, in vivo, with acoustic two-tone stimuli. The forward transmission pressure gain was about 20–25 dB, with a phase–frequency relationship that could be fit by a straight line, and was thus characteristic of a delay, over a wide frequency range. The forward delay was about 32 μs. The reverse transmission pressure loss was on average about 35 dB, and the phase–frequency relationship was again delaylike with a delay of about 38 μs. Therefore to a first approximation the middle ear operates similarly in the forward and reverse directions. The observation that the amount of pressure reduction in reverse transmission was greater than the amount of pressure gain in forward transmission suggests that complex motions of the tympanic membrane and ossicles affect reverse more than forward transmission.


2018 ◽  
Vol 9 (3) ◽  
pp. 1216 ◽  
Author(s):  
Zaineb Al-Qazwini ◽  
Zhen Yu Gordon Ko ◽  
Kalpesh Mehta ◽  
Nanguang Chen

2015 ◽  
Vol 330 ◽  
pp. 142-146 ◽  
Author(s):  
Sho Kanzaki ◽  
Kotaro Watanabe ◽  
Masato Fujioka ◽  
Shinsuke Shibata ◽  
Masaya Nakamura ◽  
...  

2015 ◽  
Vol 36 (4) ◽  
pp. 687-693 ◽  
Author(s):  
Sylvia L. van Egmond ◽  
Fredy Visser ◽  
Frank A. Pameijer ◽  
Wilko Grolman
Keyword(s):  

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


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