New bisesquiterpenoid lactone from the wild rhizome of <i>Atractylodes macrocephala</i> Koidz grown in Qimen

<p>The rhizomes of <i>Atractylodes macrocephala</i> are used as both a food source and traditional Chinese medicine in China. A phytochemical investigation was carried out on wild <i>A. macrocephala</i> grown in Qimen County in eastern China, and yielded a novel bisesquiterpenoid lactone, namely, biatractylenolide II (<b>1</b>), along with two known compounds, atractylenolide II (<b>2</b>) and taraxeryl acetate (<b>3</b>). The structure and relative configuration of the new compound were elucidated mainly by 1D and 2D NMR spectroscopic methods in combination with HRESIMS experiments. This paper describes the isolation and structural elucidation of the new bisesquiterpenoid lactone (<b>1</b>).</p

MOESM1 of Metabolic regulations of a decoction of Hedyotis diffusa in acute liver injury of mouse models

Additional file 1. The minimum standards checklist

MOESM2 of Metabolic regulations of a decoction of Hedyotis diffusa in acute liver injury of mouse models

Additional file 2. The up-regulated and down-regulated metabolites in different categories among control, LPS/GALN group and LPS/GALN + HD group

Combined Electrosorption and Chemisorption of As(V) in Water by Using Fe-rGO@AC Electrode

A novel method of arsenic removal from water, combined electrosorption and chemisorption (CEC), has been presented in this work in order to deeply eliminate arsenic in water. This method was proposed using a mixture of activated carbon (AC) and reduced graphene–iron composite (Fe-rGO) as the electrode (Fe-rGO@AC). The results showed that the AC had a better electrosorption performance, while Fe-rGO was more suitable for chemisorption of As­(V). The Fe-rGO@AC electrode combined the electrosorption with chemisorption. It was confirmed that the combination accelerated the adsorption rate of Fe-rGO. The AC on the electrode accelerated the mobility of arsenic ions and concentrated them in the electrical double layer (EDL) by means of electrostatic force underpotential. Meanwhlie, the concentrated As­(V) ions reacted with Fe-rGO, contributing to a higher arsenic chemisorption on Fe-rGO. Therefore, the combination of electrosorption with chemisorption was an effective process for arsenic removal

Human and Mouse CD137 Have Predominantly Different Binding CRDs to Their Respective Ligands

<div><p>Monoclonal antibodies (mAbs) to CD137 (a.k.a. 4-1BB) have anti-tumor efficacy in several animal models and have entered clinical trials in patients with advanced cancer. Importantly, anti-CD137 mAbs can also ameliorate autoimmunity in preclinical models. As an approach to better understand the action of agonistic and antagonistic anti-CD137 mAbs we have mapped the binding region of the CD137 ligand (CD137L) to human and mouse CD137. By investigating the binding of CD137L to cysteine rich domain II (CRDII )and CRDIII of CD137, we found that the binding interface was limited and differed between the two species in that mouse CD137L mainly combined with CRDII and human CD137L mainly combined with CRDIII.</p></div

Additional file 1 of Activation of oxytocin receptors in mouse GABAergic amacrine cells modulates retinal dopaminergic signaling

Additional file 1: Fig. S1. The expression of OxtRs in mouse retina. Fig. S2. Example images showing OxtR-eYFP neurons are Brn3a (A) or melanopsin (B) positive in the GCL. Fig. S3. eYFP+ neurons in Oxtr-Cre; Ai3 mice are mainly GABAergic, but not glycinergic amacrine cells. Fig. S4. Distribution of OxtR-eYFP neurons in Oxtr-Cre; Ai3 mouse retina. Fig. S5. ChAT and CRH ACs are partially co-localized with OxtR-eYFP neurons, and oxytocin elevates DA level. Fig. S6. The effects of oxytocin and OxtR antagonist on the amplitude of ERG b-wave. Fig. S7. Effects of oxytocin on b-wave amplitude in the presence of V1AR or DA receptor antagonists

Identification and binding analysis of mCD137 to mCD137L via PAGE gel.

<p>(A) Identification of purified mL ( mCD137L-mFc ) and mE ( mCD137-hFc ). Samples were run on a 10%SDS-PAGE gel without 2-ME by Coomassie brilliant blue staining. (B) Western blot analysis of mE,mE4,mE3,mE2 binding to mCD137L. mCD28 and mL were used as negative or positive controls, respectively. Western blot analysis was performed on a 10%SDS-PAGE gel with 2-ME. Bound mL was detected by HRP-goat-anti-mouse IgG. (C) Western blot analysis of mCD137L binding to mCD137 via 10%SDS-PAGE gel in the absence of 2-ME. mE and mE3 run on 10%SDS-PAGE gel, followed by detecting with mL and HRP-goat-anti-mouse IgG in succession. Left panel, Ponceau S staining. Right panel, Western blotting (ECL).</p

Mapping of mCD137 CRDs binding to mCD137L by ELISA assay.

<p>(A) Designs of recombinant murine CD137 proteins. Schematic representation of the entire extracellular region of CD137 is shown on top with the amino acid residue numbers noted, including its leader (1–23 aa). mE, mE4, mE3 and mE2 represent the expressed mCD137 segments covering different CRDs (I, II, III, IV). (B) Identification of purified Fc-fusion proteins expressed with pCDH (mE, mE4, mE3 and mE2) and pCDM-L (mE100 and mCD137L, i.e.mL) in reducing gel: left panel, SDS-PAGE gel with Ponceau S staining; right panel, Western blotting (ECL). (C) Binding of mCD137L to various recombinant mE or subdomains by ELISA assay. Affinity-purified mCD137L (1 µg/ml) was coated on plastic, followed by adding expressed supernatants of mCD137 fragments and subsequently detected by HRP-goat-anti-human IgG. (D) A quantitative binding ELISA in which mCD137L was coated with 1 µg/ml; after blocking with milk, four purified mCD137 protein fragments (mE,mE4,mE3,mE2 ) were added with decreased concentrations 10 µg/ml, 5 µg/ml, 1 µg/ml, 0.1 µg/ml and detected by HRP-goat-anti-human IgG. The binding experiment was repeated 3 times with different batch supernatants. Control was culture supernatant from cells that had not been transfected. *P/N>2.1.</p

Comparison of CD137 core CRDs binding to CD137L between mouse and human.

<p>Note: rCD137, Recombinant CD137; +,binding; −,no binding; STP, hinge-like region; m/h, mouse/human.</p

Cross binding of hCD137L to mCD137 via PAGE gel.

<p>mCD137 extracellular region (mE) and hCD137 extracellular region (hE) were run on 10% SDS-PAGE gel without 2-ME, then stained by Ponceau S(left panel) and followed by Western blotting with hCD137L-mFc and HRP-goat-anti-mouse IgG for detection (ECL,right panel).</p