Table_1_Red and processed meat and pancreatic cancer risk: a meta-analysis.DOCX

BackgroundThe relationship between red and processed meat consumption and pancreatic cancer risk is controversial and no study has looked specifically at the correlation for 6 years. We conducted a meta-analysis to summarize the evidence about the association between them.MethodsWe systematically searched PubMed, Embase and Cochrane Library for studies of red or processed meat consumption and pancreatic cancer published from December 2016 to July 2022. We performed random-effects models to pool the relative risks from individual studies. Subgroup analyses were used to figure out heterogeneity. We also performed publication bias analysis.ResultsSeven cohort studies and one case–control study that contained a total of 7,158 pancreatic cancer cases from 805,177 participants were eligible for inclusion. The combined RRs (95% CI) comparing highest and lowest categories were 1.07 (95% CI: 0.91–1.26; p = 0.064) for red meat and 1.04 (95% CI: 0.81–1.33; p = 0.006) for processed meat with statistically significant heterogeneity.ConclusionThis meta-analysis suggested that red and processed meat consumption has no relationship with pancreatic cancer risk.</p

Prussian Blue: A Potential Material to Improve the Electrochemical Performance of Lithium–Sulfur Batteries

The Prussian blue, as a potential adsorbent of polysulfides to suppress the dissolution and shuttle of polysulfides for lithium–sulfur batteries, has been studied in this work. Our results show that Prussian blue improves the electrochemical reaction kinetics during discharge/charge processes. More importantly, the cathode with Prussian blue exhibits better cycling stability and higher discharge capacity retention (722 mAh g^–1 at 0.2 A g^–1 after 100 cycles) than the one without Prussian blue (151 mAh g^–1). These improvements of electrochemical performances are ascribed to the fact that Prussian blue is very effective in suppressing the dissolution of polysulfides into liquid electrolyte by chemical adsorption

Banding patterns of pHZ2031 respectively linearized using four different but unique restriction enzymes (EcoRV, EcoRI, XhoI and NdeI) before treatment with activated Tris-buffer

<p><b>Copyright information:</b></p><p>Taken from "DNA modification by sulfur: analysis of the sequence recognition specificity surrounding the modification sites"</p><p></p><p>Nucleic Acids Research 2007;35(9):2944-2954.</p><p>Published online 16 Apr 2007</p><p>PMCID:PMC1888814.</p><p>© 2007 The Author(s)</p> Two fragments adding up to the size of linearized pHZ2031 (5.4 kb) were always seen at their expected positions after cleavage at a common modification site, as exemplified by cleavage at specific modification site 10 (), indicated as two white asterisks in each respective gel panel. (EcoRV: 4182 and 1231; EcoRI: 3027 and 2386; XhoI: 3976 and 1437; NdeI: 4687 and 726)

The <i>dnd</i> island in the <i>Salmonella enterica</i> serovar Saintpaul SARA23 genome that is currently being sequenced.

<p>(A) The top axis corresponds to the <i>dnd</i> island-bearing contig (NCBI Refseq accession no. NZ_ABAM01000005), while the lower axis represents a magnified view of the region shown in the red box. The symbol ‘k’ in the coordinates denotes kilobase pairs. (B) A schematic view of the lower axis (above) illustrating the location of the 19.7-kb <i>dnd</i> island (orange line), the <i>leuX</i> tRNA gene integration site (red arrow head), and the upstream/downstream flanking regions (black lines) that are conserved across 14 completely sequenced <i>Salmonella enterica</i> genomes. The ‘5end’ and ‘3end’ backbone labels refer to the 5′- and 3′-flanking backbone segments in relation to the orientation of the <i>leuX</i> tRNA gene, respectively. (C) SynView-facilated synteny mapping of the <i>dnd</i> islands and immediate flanking sequences from three species: <i>Salmonella enterica</i> serovar Saintpaul SARA23 (19.7-kb island) [topmost], <i>Escherichia coli</i> B7A (17.9-kb tRNA-proximal end of island) [middle] and <i>Enterobacter</i> sp. 638 (16.9-kb island) [lower most]. The <i>dnd</i> genes are highlighted in blue, while these and other island-harboured genes are marked by orange frames. Individual genes are hyperlinked to related information that can be accessed using GBrowse. Light-blue-shaded trapezoids link orthologous genes between the three species.</p

Table_1_Rapid visual detection of Enterocytozoon hepatopenaei by recombinase polymerase amplification combined with lateral flow dipstick.docx

Enterocytozoon hepatopenaei (EHP) is a high-impact pathogen in shrimp farming, causing huge economic losses to the global shrimp farming industry every year. However, current EHP detection methods are primarily based on the development of polymerase chain reaction (PCR) techniques that rely on sophisticated and expensive instruments. Consequently, a rapid, practical, and sensitive protocol for the detection of EHP is necessary. Recombinase polymerase amplification combined with a lateral flow dipstick (LFD-RPA) assay was developed using a pair of primers and nfo-probe targeting the conserved region of the spore wall protein gene. Under optimized reaction conditions, the LFD-RPA assay can detect 10 copies/μL of standard plasmid within 20 min at 40°C. Furthermore, the specificity of the LFD-RPA was also verified with other common pathogens of shrimp. Thirty-nine samples of Litopenaeus vannamei were collected in shrimp farms and detected using LFD-RPA and nested PCR. Thirty-two positive samples were detected by LFD-RPA. Compared with those of nested PCR, the diagnostic sensitivity and specificity of LFD-RPA were 100% and 100%, respectively. These results indicated the great application potential of the newly developed LFD-RPA assay for point-of-care diagnosis, epidemic surveillance, and epidemiological investigation of EHP.</p

Inferred phylogenetic relationship of the 31 bacterial and one archael organism carrying known <i>dnd</i> clusters (denoted by orange ‘G’ balls) and/or documented to exhibit the Dnd phenotype (denoted by purple ‘P’ balls).

<p>The tree shown was constructed on the basis of NCBI taxonomy (<a href="http://www.ncbi.nlm.nih.gov/Taxonomy/" target="_blank">http://www.ncbi.nlm.nih.gov/Taxonomy/</a>) by using iTOL <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0005132#pone.0005132-Letunic1" target="_blank">[11]</a>, which is now accessible via <i>dnd</i>DB.</p

<i>dnd</i> clusters present on mobile genetic elements comprising 25 genomic islands and one plasmid

a<p>The symbol ‘<i><u>A</u></i>’ indicates that the <i>dndA</i> gene is present in the reverse orientation with respect to the rest of the <i>dnd</i> gene cluster. The <i>dndBCDE</i> genes are invariably orientated in the same direction.</p>b<p>The 17.9 kb represents the <i>leuX</i>-proximal part of the island within the unfinished <i>E. coli</i> B7A genome.</p>c<p>The complete plasmid 3 was considered as a mobile element.</p

Discovery and Characterization of BlsE, a Radical <i>S</i>-Adenosyl-L-methionine Decarboxylase Involved in the Blasticidin S Biosynthetic Pathway

<div><p>BlsE, a predicted radical <i>S</i>-adenosyl-L-methionine (SAM) protein, was anaerobically purified and reconstituted <i>in vitro</i> to study its function in the blasticidin S biosynthetic pathway. The putative role of BlsE was elucidated based on bioinformatics analysis, genetic inactivation and biochemical characterization. Biochemical results showed that BlsE is a SAM-dependent radical enzyme that utilizes cytosylglucuronic acid, the accumulated intermediate metabolite in <i>blsE</i> mutant, as substrate and catalyzes decarboxylation at the C5 position of the glucoside residue to yield cytosylarabinopyranose. Additionally, we report the purification and reconstitution of BlsE, characterization of its [4Fe–4S] cluster using UV-vis and electron paramagnetic resonance (EPR) spectroscopic analysis, and investigation of the ability of flavodoxin (Fld), flavodoxin reductase (Fpr) and NADPH to reduce the [4Fe–4S]²⁺ cluster. Mutagenesis studies demonstrated that Cys₃₁, Cys_35, Cys₃₈ in the C×××C×MC motif and Gly₇₃, Gly₇₄, Glu₇₅, Pro₇₆ in the GGEP motif were crucial amino acids for BlsE activity while mutation of Met₃₇ had little effect on its function. Our results indicate that BlsE represents a typical [4Fe–4S]-containing radical SAM enzyme and it catalyzes decarboxylation in blasticidin S biosynthesis.</p></div

A meta-analysis of predictive value of blood biomarkers in gestational trophoblastic neoplasia - supplementary material

Supplementary figures 1&2</p

Kinetic parameters for BlsE and select mutant versions of BlsE.

*<p>Enzyme kinetic parameters were tested using CGA as the substrate with the concentration ranged from 0.025–800 <i>μ</i>M, as indicated. All the reactions were incubated at 25°C.</p