31 research outputs found
Special Magnetic Catalyst with Lignin-Reduced Au–Pd Nanoalloy
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
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
ÎĽg), 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
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
ÎĽg), 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
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
ÎĽg), 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.)
<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
<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 16 of An identical-by-descent segment harbors a 12-bp insertion determining fruit softening during domestication and speciation in Pyrus
Additional file 16: Fig. S3. KEGG analysis of genes within the 3 Mbp IBD-ER
Additional file 13 of An identical-by-descent segment harbors a 12-bp insertion determining fruit softening during domestication and speciation in Pyrus
Additional file 13: Table S13. Names and sequences (5’ to 3’) of all oligonucleotide primers used in this study
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Enzymatic and Chemoenzymatic Syntheses of Disialyl Glycans and Their Necrotizing Enterocolitis Preventing Effects
Necrotizing enterocolitis (NEC) is
one of the most common and devastating
intestinal disorders in preterm infants. Therapies to meet the clinical
needs for this special and highly vulnerable population are extremely
limited. A specific human milk oligosaccharide (HMO), disialyllacto-<i>N</i>-tetraose (DSLNT), was shown to contribute to the beneficial
effects of breastfeeding as it prevented NEC in a neonatal rat model
and was associated with lower NEC risk in a human clinical cohort
study. Herein, gram-scale synthesis of two DSLNT analogs previously
shown to have NEC preventing effect is described. In addition, four
novel disialyl glycans have been designed and synthesized by enzymatic
or chemoenzymatic methods. Noticeably, two disialyl tetraoses have
been produced by enzymatic sialylation of chemically synthesized thioethyl
β-disaccharides followed by removal of the thioethyl aglycon.
Dose-dependent and single-dose comparison studies showed varying NEC-preventing
effects of the disialyl glycans in neonatal rats. This study helps
to refine the structure requirement of the NEC-preventing effect of
disialyl glycans and provides important dose-dependent information
for using DSLNT analogs as potential therapeutics for NEC prevention
in preterm infants
Additional file 14 of An identical-by-descent segment harbors a 12-bp insertion determining fruit softening during domestication and speciation in Pyrus
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