MOESM3 of Effects of nitrogen availability on polymalic acid biosynthesis in the yeast-like fungus Aureobasidium pullulans

Additional file 3. Table S2. Numbers of genes in mainly enriched pathways under nitrogen-sufficient conditions

MOESM1 of Effects of nitrogen availability on polymalic acid biosynthesis in the yeast-like fungus Aureobasidium pullulans

Additional file 1. Table S1. Primers for the gene transcription level analysis

Additional file 1 of Functional characterization of a farnesyl diphosphate synthase from Dendrobium nobile Lindl

Additional file 1: Table S1. Primers used in thisstudy. Primer sequences for the restriction sites are shown in bold. Table S2.Relevant FPPSs sequences for phylogenetic analysis. Table S3. a. Correlationanalysis between AACT and FPPS. b. Correlation analysis between HMGR and FPPS. c.Correlation analysis between HMGS and FPPS. d. Correlation analysis between MK andFPPS. e. Correlation analysis between PMK and FPPS. f. Correlation analysisbetween MVD and FPPS. g. Correlation analysis between TPS21 and FPPS. Fig.S1 The MVA and MEP pathways are the main steps in the synthesis ofdendrobine. Fig. S2. The relative expression of DnFPPS atdifferent tissues in D.nobile. Fig. S3 Agarose gelelectrophoresis of the core fragment amplification products of Dnfpps. Fig. S4 The relative expression ofdifferent genes at different time points in D.nobile after MeJAtreatment

Subangstrom Accuracy in pHLA‑I Modeling by Rosetta FlexPepDock Refinement Protocol

Flexible peptides binding to human leukocyte antigen (HLA) play a key role in mediating human immune responses and are also involved in idiosyncratic adverse drug reactions according to recent research. However, the structural determinations of pHLA complexes remain challenging under the present conditions. In this paper, the performance of a new peptide docking method, namely FlexPepDock, was systematically investigated by a benchmark of 30 crystallized structures of peptide-HLA class I complexes. The docking results showed that the near-native pHLA-I models with peptide bb-RMSD less than 2 Å were ranked in the top 1 model for 100% (70/70) docking cases, and the subangstrom models with peptide bb-RMSD less than 1 Å were ranked in the top 5 lowest-energy models for 65.7% (46/70) docking cases. Furthermore, 10 out of 70 docking cases ranked the subangstrom all-atom models in the top 5 lowest-energy models. The results showed that the FlexPepDock can generate high-quality models of pHLA-I complexes and can be widely applied to pHLA-I modeling and mechanism research of peptide-mediated immune responses

VirD: A Virion Display Array for Profiling Functional Membrane Proteins

To facilitate high-throughput biochemical analyses of membrane proteins, we have developed a novel display technology in a microarray format. Both single-pass (cluster of differentiation 4, CD4) and multiple-pass (G protein-coupled receptor 77, GPR77) human transmembrane proteins were engineered to be displayed in the membrane envelop of herpes simplex virions. These viruses produce large spherical virions displaying multiple copies of envelop proteins. Our aim was to engineer this virus to express these human proteins during the virus productive cycle and incorporate the human proteins into the virion during the assembly process. Another strategy presented includes engineering a fusion of glycoprotein C (gC), a major constituent of herpes simplex virus type 1 (HSV-1) virions, by hijacking the <i>cis</i>-acting signals to direct incorporation of the chimeric protein into the virion. The expression of the human proteins in infected cells, at the cell surface and in purified virions, is in the correct transmembrane orientation, and the proteins are biochemically functional. Purified virions printed on glass slides form a high-density Virion Display (VirD) Array, and the displayed proteins were demonstrated to retain their native conformations and interactions on the VirD Array judging by similar assays, such as antibody staining, as well as lectin and ligand binding. This method can be readily scaled or tailored for different modalities including a high-content, high-throughput platform for screening ligands and drugs of human membrane proteins

VirD: A Virion Display Array for Profiling Functional Membrane Proteins

To facilitate high-throughput biochemical analyses of membrane proteins, we have developed a novel display technology in a microarray format. Both single-pass (cluster of differentiation 4, CD4) and multiple-pass (G protein-coupled receptor 77, GPR77) human transmembrane proteins were engineered to be displayed in the membrane envelop of herpes simplex virions. These viruses produce large spherical virions displaying multiple copies of envelop proteins. Our aim was to engineer this virus to express these human proteins during the virus productive cycle and incorporate the human proteins into the virion during the assembly process. Another strategy presented includes engineering a fusion of glycoprotein C (gC), a major constituent of herpes simplex virus type 1 (HSV-1) virions, by hijacking the <i>cis</i>-acting signals to direct incorporation of the chimeric protein into the virion. The expression of the human proteins in infected cells, at the cell surface and in purified virions, is in the correct transmembrane orientation, and the proteins are biochemically functional. Purified virions printed on glass slides form a high-density Virion Display (VirD) Array, and the displayed proteins were demonstrated to retain their native conformations and interactions on the VirD Array judging by similar assays, such as antibody staining, as well as lectin and ligand binding. This method can be readily scaled or tailored for different modalities including a high-content, high-throughput platform for screening ligands and drugs of human membrane proteins

MOESM1 of Development of keratin nanoparticles for controlled gastric mucoadhesion and drug release

Additional file 1: Figure S1. The schematic diagram of the ultrasonic system for the synthesis of KNPs. Figure S2. The time-dependent changes in the average size of KNPs within 7 days. Figure S3. H&E histological examination of the main organs after oral administration of the KNP-3 for 7 days (original magnification 100 ×)

CMHX008 improves HFD induced systemic inflammation.

<p>C57BL/6 mice were fed with HFD or LFD for 16 weeks. Then HFD fed C57BL/6 mice were treated with CMHX008 (3 and 10 mg/kg, HFD-C3 and HFD-C10), rosiglitazone (3 mg/kg, HFD-Rosi) or vehicle (HFD-Veh or LFD-Veh) only, for additional 5 weeks. Trunk blood was collected at the end of the experiment. Serum was used for the measurement of TNF-α (A, IL-6 (B), IL-10 (C), and adiponectin (D). Data are the means ± S.E.M., n = 4–5; ^#<i>P<</i>0.05 <i>vs</i> LFD-Veh and *<i>P<</i>0.05 <i>vs</i> HFD-Veh.</p

CMHX008 differentially regulates PPARγ target genes in 3T3-L1 adipocytes.

<p>Post-confluent 3T3-L1 preadipocytes were incubated in differentiation medium for 2 days. The medium was changed to DMEM containing insulin and 10% FBS for another two days and then replaced again with fresh DMEM containing 10% FBS for another 3 days. Rosiglitazone and CMHX008 were administered at the initiation of differentiation and with every medium change. At day 7, the differentiation cells were harvested for total RNA extraction and the mRNA expression of adiponectin (A), Glut4 (B) and aP2 (D) was analyzed by real-time PCR, and secreted adiponectin in the culture medium was measured using adiponectin ELISA kit (B). Data are the means ± S.E.M. from six independent experiments. *: <i>P<</i>0.05; NS: no significance.</p

CMHX008 protects HFD induced obesity and insulin resistance.

<p>C57BL/6 mice were fed with HFD or LFD for 16 weeks. Then HFD fed C57BL/6 mice were treated with CMHX008 (3 and 10 mg/kg, HFD-C3 and HFD-C10), rosiglitazone (3 mg/kg, HFD-Rosi) or vehicle (HFD-Veh or LFD-Veh) only. After 4 weeks treatment, intra-peritoneal glucose tolerance tests (iGTTs) were performed (B) and area under curve (AUC) of iGTTs was calculated (B, inserted Figure). Changes in body weight (A), fasting insulin levels (C), morphology of adipocytes (D), quantified adipocyte size (E), mass of epididymal adipose tissues (WAT, F) and aP2 mRNA levels (G) were examined. Data are the means ± S.E.M., n = 6–8; ^#<i>P<</i>0.05 <i>vs</i> LFD-Veh and *<i>P<</i>0.05 <i>vs</i> HFD-Veh.</p