Recepten uit de middeleeuwse bibliotheek

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Communication in pediatric healthcare: a state-of-the-art literature review of conversation-analytic research

Communication is central to pediatric care. Conversation analytic (CA) studies of recorded naturally occurring pediatric interactions contribute distinctive understandings; however, to date there has been no detailed review of CA’s unique contributions. We searched Medline, PsychINFO, Sciencedirect, Google Scholar, and the EM/CA Wiki database, identifying 74 empirical articles across diverse areas of pediatrics. Our state-of-the-art review highlights CA of clinician and caregiver conversations about a child patient, in addition to those involving the child. The findings have the potential to enhance clinical practice by illuminating how healthcare tasks are practically accomplished and enrich our knowledge of children’s participation in consultations by revealing the mechanisms that constrain and enable their involvement. We call for better synthesis of findings with broader CA literature (e.g., nonclinical child interactions, adult triadic clinical encounters, and fundamental knowledge of social interaction). We appeal for increased support for scholarly work in non-Western settings, and emphasize scope for applied initiatives. The data reported are in multiple languages. </p

Evolution of on whitened natural image patches when using advanced training methods.

<p>GRBM-196-196s were trained on the whitened natural image data set using CD-10, PCD-10, and PT-10 with 10 linearly distributed inverse temperatures. The learning curves are averaged over 10 trials. The gradient was restricted to one hundredth of the maximal data norm (0.48) and the learning rate for the variance parameter was set 100 times smaller than for the other parameters.</p

Illustration of a GRBM-2-2 from the perspective of a PoE and a MoG.

<p>Arrows indicate the roles of the visible bias vector and the weight vectors. (a) and (b) visualize the two experts of the GRBM. The red (dotted) and blue (dashed) circles indicate the two Gaussians each expert has. (c) visualizes the components in the GRBM seen as a MoG. The components are denoted by the green (filled) circles, and result from the product of the two experts. Notice how each component sits right between a red (dotted) and a blue (dash-dotted) circle.</p

In-Gel Microwave-Assisted Acid Hydrolysis of Proteins Combined with Liquid Chromatography Tandem Mass Spectrometry for Mapping Protein Sequences

We report an enabling method for mapping the protein sequence with high sequence coverage. This method combines the high separation power of gel electrophoresis for protein separation with the high sequence coverage capability of microwave-assisted acid hydrolysis (MAAH) mass spectrometry (MS). In-gel MAAH using 25% trifluoroacetic acid was developed and optimized for degrading the gel-separated protein into small peptides suitable for tandem MS sequencing. For bovine serum albumin (BSA) (∼67 kDa), with 4 μg of protein loading onto a gel for separation, followed by excising the protein gel band for in-gel MAAH and then injecting ∼2 μg of the resultant peptides into a liquid chromatography quadrupole time-of-flight mass spectrometer for analysis, 689 ± 54 (<i>n</i> = 3) unique peptides were identified with a protein sequence coverage of 99 ± 1%. Both the number of peptides detected and sequence coverage decreased as the sample amount decreased, mainly due to background interference: 316 ± 59 peptides and 94 ± 3% coverage for 2 μg loading, 136 ± 19 and 76 ± 5% for 1 μg loading, and 30 ± 2 and 32 ± 2% for 0.5 μg loading. To demonstrate the general applicability of the method, 10 gel bands from gel electrophoresis of an albumin-depleted human plasma sample were excised for in-gel MAAH LC-MS analysis. In total, 19 relatively high abundance proteins with molecular weights ranging from ∼8 to ∼160 kD could be mapped with coverage of 100% for six proteins (MW 8759 to 68 425 Da), 96–98% for five proteins (MW 11 458 to 36 431 Da), 92% for three proteins (MW 15 971 to 36 431 Da), 80–87% for four proteins (MW 42 287 to 162 134 Da), and 56% for one protein (MW 51 358 Da). Finally, to demonstrate the applicability of the method for more detailed analysis of complex protein mixtures, two-dimensional (2D) gel electrophoresis was combined with in-gel MAAH, affinity purification, and LC-MS/MS to characterize six bovine alpha-S1-casein phosphoprotein isoforms. Full sequence coverage was achieved for each protein, and six new modification sites were found

Spatial layout and size of the filters learned on whitened natural image patches.

<p>(a) for a GRBM-196-196 and (b) for a GRBM-196-588. The layout and size of the filters represented by the position and size of the bars. Each bar denotes the center position and the orientation of a Gabor function fitted to one of the learned filters. Thickness and length of each bar are proportional to the spatial-frequency bandwidth of the corresponding filters.</p

Amari errors of ICA and GRBM-2-2 on the blind source separation task over different trials.

<p>The Amari error compares the estimated with the true unmixing matrix. The box extends from the lower to the upper quantile values of the errors, with a line at the median. The whiskers extending from the box show the minimum-maximum range. As a base line, the Amari errors between the real unmixing matrices and random matrices are provided.</p

Sums of the mixing coefficients of a GRBMs-196-196 trained on whitened natural image patches.

<p>Sums of the mixing coefficients of a GRBMs-196-196 trained on whitened natural image patches.</p

In-Gel Microwave-Assisted Acid Hydrolysis of Proteins Combined with Liquid Chromatography Tandem Mass Spectrometry for Mapping Protein Sequences

We report an enabling method for mapping the protein sequence with high sequence coverage. This method combines the high separation power of gel electrophoresis for protein separation with the high sequence coverage capability of microwave-assisted acid hydrolysis (MAAH) mass spectrometry (MS). In-gel MAAH using 25% trifluoroacetic acid was developed and optimized for degrading the gel-separated protein into small peptides suitable for tandem MS sequencing. For bovine serum albumin (BSA) (∼67 kDa), with 4 μg of protein loading onto a gel for separation, followed by excising the protein gel band for in-gel MAAH and then injecting ∼2 μg of the resultant peptides into a liquid chromatography quadrupole time-of-flight mass spectrometer for analysis, 689 ± 54 (<i>n</i> = 3) unique peptides were identified with a protein sequence coverage of 99 ± 1%. Both the number of peptides detected and sequence coverage decreased as the sample amount decreased, mainly due to background interference: 316 ± 59 peptides and 94 ± 3% coverage for 2 μg loading, 136 ± 19 and 76 ± 5% for 1 μg loading, and 30 ± 2 and 32 ± 2% for 0.5 μg loading. To demonstrate the general applicability of the method, 10 gel bands from gel electrophoresis of an albumin-depleted human plasma sample were excised for in-gel MAAH LC-MS analysis. In total, 19 relatively high abundance proteins with molecular weights ranging from ∼8 to ∼160 kD could be mapped with coverage of 100% for six proteins (MW 8759 to 68 425 Da), 96–98% for five proteins (MW 11 458 to 36 431 Da), 92% for three proteins (MW 15 971 to 36 431 Da), 80–87% for four proteins (MW 42 287 to 162 134 Da), and 56% for one protein (MW 51 358 Da). Finally, to demonstrate the applicability of the method for more detailed analysis of complex protein mixtures, two-dimensional (2D) gel electrophoresis was combined with in-gel MAAH, affinity purification, and LC-MS/MS to characterize six bovine alpha-S1-casein phosphoprotein isoforms. Full sequence coverage was achieved for each protein, and six new modification sites were found

Illustration of 196 learned filters learned by a GRBM-196-196.

<p>The plot has been ordered from left to right and from top to bottom by the increasing average activation level of the corresponding hidden units.</p