Visualization 1 shows the focus changing with the applied voltage.

A video clip of our experiment is linked, which shows that the focal plane shifts from left to right of the target when the applied voltage is increased from zero to 5 kV and decteased to zero. In our experiment, the applied voltage was changed in steps of 0.5 kV

Additional file 15: of The similar and different evolutionary trends of MATE family occurred between rice and Arabidopsis thaliana

Tests for positive selection among codons of Arabidopsis MATE genes using site models. (DOC 19 kb

Additional file 13: of The similar and different evolutionary trends of MATE family occurred between rice and Arabidopsis thaliana

Type-I functional divergence sites identified between different subgroup pairs of rice and Arabidopsis. (DOC 20 kb

Figures, Tables, and Additional files

Fig.1 Phylogenetic relationships, exon-intron structure, and motif structures of BURP domain-containing gene. Fig. 2 Multiple sequence alignment of several BURP domain-containing protein sequences. Table 1. Promoter analysis of BURP domain-containing gene family.Table 2. Estimates of the dates of the segmental duplication events of the BURP domain-containing gene family. Table 3. Genes involved in tandem duplication and their 4DTv values. Table 4. Functional divergence between subfamilies of the BURP domain-containing gene family. Table 5. Tests for positive selection among codons of BURP domain-containing genes using site models. Table 6 Parameter estimation and likelihood ratio tests for the branch-site models. Data S1 Protein sequence data for the BURP domain-containing gene family. Data S2 Coding sequence data for the BURP domain-containing gene family. Data S3 Genome sequence data for the BURP domain-containing gene family. Data S4 1500 bp of nucleotide sequences upstream of the translation initiation codon of BURP genes. Data S5 Multiple sequence alignment of BURP domain-containing gene family. Data S6. Schematic of motifs of BURP domain-containing proteins. Data S7. Promoter analysis performed on the BURP domain-containing gene family

Endostar inhibits the proliferation of HUVECs in a dose-dependent manner.

<p>HUVECs (1×10⁴/well) were incubated in ECM (5% FBS, 1% ECGS) with different concentrations of Endostar for 24 h. Cell viability was quantified by an MTT assay. *P<0.05 versus the control group.</p

Endostar suppresses the expression of nuclear and total cellular β-catenin, cyclin D1 and VEGF in HUVECs.

<p>(A and B) HUVECs were incubated with different concentrations of Endostar for 24 h. The whole-cell extracts and the nuclear extracts were prepared and analyzed by Western blotting and probed with specific antibodies. *P<0.05 versus the control group. (C) HUVECs were treated with or without 20 mmol/l LiCl (a dose known to activate β-catenin) in the presence or absence of 100 µg/ml Endostar. After 24 h, the expression and cellular localization of β-catenin (red) was determined by immunofluorescence analysis. The nucleus was stained with DAPI (blue).</p

Endostar inhibits TCF/LEF-dependent transcriptional activity in HUVECs.

<p>(A) Inhibition of TCF/LEF-dependent transcriptional activity in HUVECs by Endostar. HUVECs were transfected with pGL3-OT (a TCF/LEF-responsive reporter) or pGL3-OF (a negative control) plasmids plus pRL-SV40 as internal control and treated with different concentrations of Endostar. After 24 h, the luciferase activities were measured using the dual-luciferase reporter assay system and normalized to Renilla luciferase activity. *P<0.05 versus the control group. (B) Endostar suppresses the mutant β-catenin-mediated increase in TCF/LEF-dependent transcriptional activity. The pcDNA3-S33Y-β-catenin (a constitutively stabilized mutant β-catenin) plasmid and the reporter plasmid were cotransfected into HUVECs. After 12 h, cells were incubated with different doses of Endostar and the luciferase activities were determined.^#P<0.05 versus the empty vector group. *P<0.05 versus the S33Y-β-catenin group.</p

Endostar inhibits HUVECs invasion in Transwell invasion assay.

<p>HUVECs were seeded in the top chamber of Transwell and treated with different concentrations of Endostar. The bottom chambers were filled with 500 µl ECM with 5% FBS and 1% ECGS. After 12 h, the invasive HUVECs were stained and quantified by manual counting. *P<0.05 versus the control group.</p

Novel 4‑Arylindolines Containing a Pyrido[3,2‑<i>d</i>]pyrimidine Moiety as the Programmed Cell Death-1/Programmed Cell Death-Ligand 1 Interaction Inhibitors for Tumor Immunotherapy

A series of pyrido[3,2-d]pyrimidine-containing 4-arylindolines were identified as potent inhibitors of the programmed cell death-1 (PD-1)/programmed cell death-ligand 1 (PD-L1) interaction by structural optimization of a 4-arylindoline precursor reported previously. Among them, compound N11 was the most promising inhibitor, showing an IC50 value of 6.3 nM against the PD-1/PD-L1 interaction at the biochemical level. In in vitro T-cell tumor co-culture models, N11 significantly promoted T-cell proliferation, activation, and infiltration into tumor spheres, demonstrating that it possessed excellent immunomodulatory activity. In addition, N11 exhibited favorable in vivo antitumor activity in an LLC/PD-L1 tumor-bearing mouse model. Flow cytometry analysis verified that the in vivo antitumor efficacy of N11 was dependent on the activation of the immune microenvironment. These findings suggest that N11 can serve as a new starting point for the future development of small-molecule antitumor immunomodulators targeting the PD-1/PD-L1 axis

Novel 4‑Arylindolines Containing a Pyrido[3,2‑<i>d</i>]pyrimidine Moiety as the Programmed Cell Death-1/Programmed Cell Death-Ligand 1 Interaction Inhibitors for Tumor Immunotherapy

A series of pyrido[3,2-d]pyrimidine-containing 4-arylindolines were identified as potent inhibitors of the programmed cell death-1 (PD-1)/programmed cell death-ligand 1 (PD-L1) interaction by structural optimization of a 4-arylindoline precursor reported previously. Among them, compound N11 was the most promising inhibitor, showing an IC50 value of 6.3 nM against the PD-1/PD-L1 interaction at the biochemical level. In in vitro T-cell tumor co-culture models, N11 significantly promoted T-cell proliferation, activation, and infiltration into tumor spheres, demonstrating that it possessed excellent immunomodulatory activity. In addition, N11 exhibited favorable in vivo antitumor activity in an LLC/PD-L1 tumor-bearing mouse model. Flow cytometry analysis verified that the in vivo antitumor efficacy of N11 was dependent on the activation of the immune microenvironment. These findings suggest that N11 can serve as a new starting point for the future development of small-molecule antitumor immunomodulators targeting the PD-1/PD-L1 axis