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Shanghai Model Organisms Center humanized pd 1 mouse model
A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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Icare Inc integrated care model in pd
A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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MathWorks Inc pk pd modeling mathworks
A Immunofluorescence analysis <t>of</t> <t>PD-1</t> binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.
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Image Search Results


A Immunofluorescence analysis of PD-1 binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A Immunofluorescence analysis of PD-1 binding to PD-L1 on RKO cells treated with TER. RKO cells were incubated with recombinant human PD-1 Alexa 647 protein and treated with the indicated concentrations of TER. Red fluorescence represents PD-1 binding; the nuclei were stained with Hoechst (blue). B Competitive ELISA assay measuring the inhibition of PD-1/PD-L1 interaction by TER. The binding between PD-1 and PD-L1 in the presence of increasing concentrations of TER was assessed. C The 3D structure of TER (upper panel) and its predicted binding pose within the active site of PD-1 (PDB ID: 3RRQ, lower panel). The key interacting residues include PHE56, SER57, ASN58, THR59, SER62, PHE63, PHE82, PRO83, GLN99, ASN102, GLY103, and ARG104. D Protein–ligand complex showing TER docked to PD-1, with the binding pocket highlighted. E Surface plasmon resonance (SPR) analysis showing the binding of TER to PD-1. αPD-L1 was used as a positive control. *** p < 0.001 and **** p < 0.0001 compared with the respective control.

Article Snippet: A humanized PD-1 mouse model (C57BL/6J background, genetically engineered to express the full-length human PD-1 protein) was obtained from the Shanghai Model Organisms Center (Shanghai, China).

Techniques: Immunofluorescence, Binding Assay, Incubation, Recombinant, Fluorescence, Staining, Competitive ELISA, Inhibition, SPR Assay, Positive Control, Control

A The viability of hPD-1 Jurkat-T cells and hPD-L1 CHO cells following treatment with the indicated concentrations of TER for 24 h. B Luciferase activity measured using a PD-1/PD-L1 blockade bioassay. hPD-1 Jurkat-T cells (effector cells) were co-cultured with hPD-L1-expressing aAPC/CHO-K1 cells (target cells) in the presence of indicated concentrations of TER. The luminescence signal indicates the level of TCR signaling activation. αPD-L1 was used as a positive control. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Journal: Oncogenesis

Article Title: Teriflunomide modulates the PD-1/PD-L1 axis and enhances antitumor immunity in colorectal cancer

doi: 10.1038/s41389-026-00607-3

Figure Lengend Snippet: A The viability of hPD-1 Jurkat-T cells and hPD-L1 CHO cells following treatment with the indicated concentrations of TER for 24 h. B Luciferase activity measured using a PD-1/PD-L1 blockade bioassay. hPD-1 Jurkat-T cells (effector cells) were co-cultured with hPD-L1-expressing aAPC/CHO-K1 cells (target cells) in the presence of indicated concentrations of TER. The luminescence signal indicates the level of TCR signaling activation. αPD-L1 was used as a positive control. * <0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 compared with the respective control.

Article Snippet: A humanized PD-1 mouse model (C57BL/6J background, genetically engineered to express the full-length human PD-1 protein) was obtained from the Shanghai Model Organisms Center (Shanghai, China).

Techniques: Luciferase, Activity Assay, Bioassay, Cell Culture, Expressing, Activation Assay, Positive Control, Control