Informational masking with speech-on-speech intelligibility: Pupil response and time-course of learning

ABSTRACTInformational masking (IM) can greatly reduce speech intelligibility, but the neural mechanisms underlying IM are not understood. Binaural differences between target and masker can improve speech perception. In general, improvement in masked speech intelligibility due to provision of spatial cues is called spatial release from masking. Here, we focused on an aspect of spatial release from masking, specifically, the role of spatial attention. We hypothesized that in a situation with IM background sound 1) attention to speech recruits lateral frontal cortex (LFCx), and 2) LFCx activity varies with direction of spatial attention. Using functional near infrared spectroscopy (fNIRS), we assessed LFCx activity bilaterally in normal-hearing listeners. In experiment 1, two talkers were simultaneously presented. Listeners either attended to the target talker (speech task) or they listened passively to an unintelligible, scrambled version of the acoustic mixture (control task). Target and masker differed in pitch and interaural time difference (ITD). Relative to the passive control, LFCx activity increased during attentive listening. Experiment 2 measured how LFCx activity varied with ITD, by testing listeners on the speech task in experiment 1, except that talkers either were spatially separated by ITD or co-located. Results show that directing of auditory attention activates LFCx bilaterally. Moreover, right LFCx is recruited more strongly in the spatially separated as compared with co-located configurations. Findings hint that LFCx function contributes to spatial release from masking in situations with IM.

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A computational model for assessment of speech intelligibility in informational masking

Frontiers of Electrical and Electronic Engineering ◽

10.1007/s11460-012-0189-8 ◽

2012 ◽

Vol 7 (1) ◽

pp. 107-115

Author(s):

Xihong Wu ◽

Jing Chen

Keyword(s):

Computational Model ◽

Speech Intelligibility ◽

Informational Masking

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Ultrastructural Changes of the Symbiotic Chlorella-Like Alga Isolated from Hydra Viridis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100054212 ◽

1982 ◽

Vol 40 ◽

pp. 320-321

Author(s):

K.W. Lee ◽

R.H. Meints ◽

D. Kuczmarski ◽

J.L. Van Etten

Keyword(s):

Time Course ◽

Reciprocal Cross ◽

Ultrastructural Level ◽

Ultrastructural Changes ◽

Symbiotic Relationship ◽

Cell Recognition ◽

Green Hydra ◽

Different Strains ◽

Hydra Viridis

The physiological, biochemical, and ultrastructural aspects of the symbiotic relationship between the Chlorella-like algae and the hydra have been intensively investigated. Reciprocal cross-transfer of the Chlorellalike algae between different strains of green hydra provide a system for the study of cell recognition. However, our attempts to culture the algae free of the host hydra of the Florida strain, Hydra viridis, have been consistently unsuccessful. We were, therefore, prompted to examine the isolated algae at the ultrastructural level on a time course.

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Destruction of Actin Filaments by Osmium Tetroxide

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100079772 ◽

1977 ◽

Vol 35 ◽

pp. 466-467

Author(s):

P. Maupin-Szamier ◽

T. D. Pollard

Keyword(s):

Actin Filaments ◽

Time Course ◽

Osmium Tetroxide ◽

Rabbit Muscle ◽

Muscle Actin ◽

Sodium Phosphate Buffer ◽

Transmission Electron ◽

The Difference ◽

Rates Of Decay ◽

Short Time

We have studied the destruction of rabbit muscle actin filaments by osmium tetroxide (OSO4) to develop methods which will preserve the structure of actin filaments during preparation for transmission electron microscopy.Negatively stained F-actin, which appears as smooth, gently curved filaments in control samples (Fig. 1a), acquire an angular, distorted profile and break into progressively shorter pieces after exposure to OSO4 (Fig. 1b,c). We followed the time course of the reaction with viscometry since it is a simple, quantitative method to assess filament integrity. The difference in rates of decay in viscosity of polymerized actin solutions after the addition of four concentrations of OSO4 is illustrated in Fig. 2. Viscometry indicated that the rate of actin filament destruction is also dependent upon temperature, buffer type, buffer concentration, and pH, and requires the continued presence of OSO4. The conditions most favorable to filament preservation are fixation in a low concentration of OSO4 for a short time at 0°C in 100mM sodium phosphate buffer, pH 6.0.

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The time course of calcium deposition in shells of the barnacle (Balanus amphititre amphititre) during cyprid-juvenile metamorphosis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100168621 ◽

1994 ◽

Vol 52 ◽

pp. 178-179

Author(s):

Nancy R. Wallace ◽

Craig C. Freudenrich ◽

Karl Wilbur ◽

Peter Ingram ◽

Ann LeFurgey

Keyword(s):

Electron Microscopy ◽

Scanning Electron Microscopy ◽

Time Course ◽

Vertical Plane ◽

Mantle Cavity ◽

Qualitative Assessment ◽

Calcium Deposition ◽

Free Swimming ◽

Freeze Dried ◽

Scanning Electron

The morphology of balanomorph barnacles during metamorphosis from the cyprid larval stage to the juvenile has been examined by light microscopy and scanning electron microscopy (SEM). The free-swimming cyprid attaches to a substrate, rotates 90° in the vertical plane, molts, and assumes the adult shape. The resulting metamorph is clad in soft cuticle and has an adult-like appearance with a mantle cavity, thorax with cirri, and incipient shell plates. At some time during the development from cyprid to juvenile, the barnacle begins to mineralize its shell, but it is not known whether calcification occurs before, during, or after ecdysis. To examine this issue, electron probe x-ray microanalysis (EPXMA) was used to detect calcium in cyprids and juveniles at various times during metamorphosis.Laboratory-raised, free-swimming cyprid larvae were allowed to settle on plastic coverslips in culture dishes of seawater. The cyprids were observed with a dissecting microscope, cryopreserved in liquid nitrogen-cooled liquid propane at various times (0-24 h) during metamorphosis, freeze dried, rotary carbon-coated, and examined with scanning electron microscopy (SEM). EPXMA dot maps were obtained in parallel for qualitative assessment of calcium and other elements in the carapace, wall, and opercular plates.

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Arabidopsis 4-COUMAROYL-COA LIGASE 8 contributes to the biosynthesis of the benzenoid ring of coenzyme Q in peroxisomes

Biochemical Journal ◽

10.1042/bcj20190688 ◽

2019 ◽

Vol 476 (22) ◽

pp. 3521-3532

Author(s):

Eric Soubeyrand ◽

Megan Kelly ◽

Shea A. Keene ◽

Ann C. Bernert ◽

Scott Latimer ◽

...

Keyword(s):

Oxidative Metabolism ◽

Time Course ◽

Reverse Genetics ◽

De Novo ◽

Coenzyme Q ◽

Control Level ◽

Wild Type ◽

Fluorescent Reporters ◽

Coa Ligase ◽

Peroxisomal Targeting

Plants have evolved the ability to derive the benzenoid moiety of the respiratory cofactor and antioxidant, ubiquinone (coenzyme Q), either from the β-oxidative metabolism of p-coumarate or from the peroxidative cleavage of kaempferol. Here, isotopic feeding assays, gene co-expression analysis and reverse genetics identified Arabidopsis 4-COUMARATE-COA LIGASE 8 (4-CL8; At5g38120) as a contributor to the β-oxidation of p-coumarate for ubiquinone biosynthesis. The enzyme is part of the same clade (V) of acyl-activating enzymes than At4g19010, a p-coumarate CoA ligase known to play a central role in the conversion of p-coumarate into 4-hydroxybenzoate. A 4-cl8 T-DNA knockout displayed a 20% decrease in ubiquinone content compared with wild-type plants, while 4-CL8 overexpression boosted ubiquinone content up to 150% of the control level. Similarly, the isotopic enrichment of ubiquinone's ring was decreased by 28% in the 4-cl8 knockout as compared with wild-type controls when Phe-[Ring-13C6] was fed to the plants. This metabolic blockage could be bypassed via the exogenous supply of 4-hydroxybenzoate, the product of p-coumarate β-oxidation. Arabidopsis 4-CL8 displays a canonical peroxisomal targeting sequence type 1, and confocal microscopy experiments using fused fluorescent reporters demonstrated that this enzyme is imported into peroxisomes. Time course feeding assays using Phe-[Ring-13C6] in a series of Arabidopsis single and double knockouts blocked in the β-oxidative metabolism of p-coumarate (4-cl8; at4g19010; at4g19010 × 4-cl8), flavonol biosynthesis (flavanone-3-hydroxylase), or both (at4g19010 × flavanone-3-hydroxylase) indicated that continuous high light treatments (500 µE m−2 s−1; 24 h) markedly stimulated the de novo biosynthesis of ubiquinone independently of kaempferol catabolism.

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