31 research outputs found

    Special Magnetic Catalyst with Lignin-Reduced Au–Pd Nanoalloy

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    This study describes a new strategy to fabricate a special magnetic catalyst via facile coating Au–Pd nanoalloy catalysts onto a commercial magnetic stirring bar, without the incorporation of iron element. First, the abundant natural “waste” lignin was utilized as the reducing and stabilizing agent to prepare Au–Pd nanoalloys in a green manner. The Au–Pd nanoalloys were assumed to have a core–shell structure with an Au-rich core and a Pd-rich shell. The Au–Pd nanoalloys could be well dispersed in aqueous medium due to the stabilizing effect of lignin and be conveniently coated onto the surface of a commercial stirring bar. The Au<sub>1.0</sub>Pd<sub>1.0</sub> nanoalloy catalyst exhibited excellent catalytic activities in the reduction of 4-nitrophenol to 4-amnophenol by NaBH<sub>4</sub>, with a rate constant (<i>k</i>) of 0.239 min<sup>–1</sup>, which was higher than that of Au<sub>0.5</sub>Pd<sub>1.0</sub> and Au<sub>2.0</sub>Pd<sub>1.0</sub> nanoalloys and 4 times higher than that of a single-component Au or Pd nanoparticles. Besides, the catalytic ability of Au–Pd nanoalloy catalyst could be maintained even after seven cycles of catalysis. The catalytic rate constant was found to be positively correlated to the stirring speed of the bar. The scanning electron microscopy analysis revealed ravines and pores on the surface of lignin–nanoalloys composites, implying the possible mechanism of the catalytic activities. This study not only proved the feasibility of lignin for green synthesis of Au–Pd nanoalloys but also proposed a facile and innovated strategy for the future production of solid/liquid catalytic platforms where the developed method could be used to coat any surface interfacing the reagents

    Quantitative Phosphoproteomics Revealed Glucose-Stimulated Responses of Islet Associated with Insulin Secretion

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    As central tissue of glucose homeostasis, islet has been an important focus of diabetes research. Phosphorylation plays pivotal roles in islet function, especially in islet glucose-stimulated insulin secretion. A systematic view on how phosphorylation networks were coordinately regulated in this process remains lacking, partially due to the limited amount of islets from an individual for a phosphoproteomic analysis. Here we optimized the in-tip and best-ratio phosphopeptide enrichment strategy and a SILAC-based workflow for processing rat islet samples. With limited islet lysates from each individual rat (20–47 μg), we identified 8539 phosphosites on 2487 proteins. Subsequent quantitative analyses uncovered that short-term (30 min) high glucose stimulation induced coordinate responses of islet phosphoproteome on multiple biological levels, including insulin secretion related pathways, cytoskeleton dynamics, protein processing in ER and Golgi, transcription and translation, and so on. Furthermore, three glucose-responsive phosphosites (Prkar1a pT75pS77 and Tagln2 pS163) from the data set were proved to be correlated with insulin secretion. Overall, we initially gave an in-depth map of islet phosphoproteome regulated by glucose on individual rat level. This was a significant addition to our knowledge about how phosphorylation networks responded in insulin secretion. Also, the list of changed phosphosites was a valuable resource for molecular researchers in diabetes field

    Quantitative Phosphoproteomics Revealed Glucose-Stimulated Responses of Islet Associated with Insulin Secretion

    No full text
    As central tissue of glucose homeostasis, islet has been an important focus of diabetes research. Phosphorylation plays pivotal roles in islet function, especially in islet glucose-stimulated insulin secretion. A systematic view on how phosphorylation networks were coordinately regulated in this process remains lacking, partially due to the limited amount of islets from an individual for a phosphoproteomic analysis. Here we optimized the in-tip and best-ratio phosphopeptide enrichment strategy and a SILAC-based workflow for processing rat islet samples. With limited islet lysates from each individual rat (20–47 μg), we identified 8539 phosphosites on 2487 proteins. Subsequent quantitative analyses uncovered that short-term (30 min) high glucose stimulation induced coordinate responses of islet phosphoproteome on multiple biological levels, including insulin secretion related pathways, cytoskeleton dynamics, protein processing in ER and Golgi, transcription and translation, and so on. Furthermore, three glucose-responsive phosphosites (Prkar1a pT75pS77 and Tagln2 pS163) from the data set were proved to be correlated with insulin secretion. Overall, we initially gave an in-depth map of islet phosphoproteome regulated by glucose on individual rat level. This was a significant addition to our knowledge about how phosphorylation networks responded in insulin secretion. Also, the list of changed phosphosites was a valuable resource for molecular researchers in diabetes field

    Quantitative Phosphoproteomics Revealed Glucose-Stimulated Responses of Islet Associated with Insulin Secretion

    No full text
    As central tissue of glucose homeostasis, islet has been an important focus of diabetes research. Phosphorylation plays pivotal roles in islet function, especially in islet glucose-stimulated insulin secretion. A systematic view on how phosphorylation networks were coordinately regulated in this process remains lacking, partially due to the limited amount of islets from an individual for a phosphoproteomic analysis. Here we optimized the in-tip and best-ratio phosphopeptide enrichment strategy and a SILAC-based workflow for processing rat islet samples. With limited islet lysates from each individual rat (20–47 μg), we identified 8539 phosphosites on 2487 proteins. Subsequent quantitative analyses uncovered that short-term (30 min) high glucose stimulation induced coordinate responses of islet phosphoproteome on multiple biological levels, including insulin secretion related pathways, cytoskeleton dynamics, protein processing in ER and Golgi, transcription and translation, and so on. Furthermore, three glucose-responsive phosphosites (Prkar1a pT75pS77 and Tagln2 pS163) from the data set were proved to be correlated with insulin secretion. Overall, we initially gave an in-depth map of islet phosphoproteome regulated by glucose on individual rat level. This was a significant addition to our knowledge about how phosphorylation networks responded in insulin secretion. Also, the list of changed phosphosites was a valuable resource for molecular researchers in diabetes field

    Characterisation of the whole-genome wide hexokinase gene family unravels the functional divergence in pear (<i>Pyrus bretschneideri</i> Rehd.)

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    <p>Hexokinase genes <i>(HXK</i>) encode enzymes that play an important role in fruit quality and plant development because they participate in the first step of the glycolytic pathway for sugar accumulation and metabolism. In this study, the authors conducted analysis of the phylogeny, gene structure, and expression of <i>HXK</i> genes in pear (<i>Pyrus bretschneideri</i> Rehd.), comparing them with 7 other plant species. A total of 10 <i>HXK</i> protein sequences from pear and 33 <i>HXK</i>s from 7 other species were identified and clustered into 4 groups, matching their motif classification. Duplication events and motif structure variation attributed the diversification of <i>HXK</i> genes, supported by differential expression pattern of <i>PbrHXKs</i> from pear fruit transcriptome data and qRT – PCR verification. Combining pear fruit soluble sugar content data and analyses above, <i>PbrHXK1</i>and <i>PbrHXK3</i> were identified as important candidate genes in sorbitol, fructose, and glucose accumulation during pear fruit development. <i>PbrHXK1</i>and <i>PbrHXK3</i> were identified as important candidate genes in sorbitol, fructose, and glucose accumulation during pear fruit development. Subsequent research on these highly expressed <i>PbrHXKs</i> will benefit the enhancement of sugar content and quality in pear.</p

    A novel nonsense NBEAL2 gene mutation causing severe bleeding in a patient with gray platelet syndrome

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    <p>Gray platelet syndrome (GPS) is a rare, inherited bleeding disorder characterized by the defect of platelet α-granule. Up to date, these are only four studies identifying NBEAL2 gene correlated with GPS. In the current report, we present a Chinese GPS patient who had severe bleeding tendency, abnormalities of platelet functions, and absence of platelet α-granules. Genomic DNA sequencing for the patient identified a nonsense mutation (g.27713C>A) of NBEAL2 gene (g.NG__031914.1) resulting in a premature protein (p.Glu1726*). In comparison with the reported patients, we conclude that homozygotes with nonsense or deletion mutation leading to a premature stop codon exhibit more serious bleeding problem than those with missense mutations.</p

    Additional file 14 of An identical-by-descent segment harbors a 12-bp insertion determining fruit softening during domestication and speciation in Pyrus

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    Additional file 14: Fig. S1. Distribution of IBD tract lengths within populations (cultivated Asian-cultivated Asian, wild Asian-wild Asian, cultivated European-cultivated European, and wild European-wild European) and between populations (cultivated Asian-wild Asian, cultivated Asian-cultivated European, cultivated Asian-wild European, wild Asian-cultivated European, wild Asian-wild European, and cultivated European-wild European). WE, wild European; CA, cultivated Asian; WE, wild European; and CE, cultivated European
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