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ft671 (MedChemExpress)

Name: ft671
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Rating: 94 (27 reviews)

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Silencing and inhibition of Usp7 and Usp10 reduces seeded Tau aggregation induced by AD-TAU seeds in wildtype CTX. ( A ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 1 with 1 µM individual siRNA Usp7 #13, Usp10 #14, smartpool Mapt (siMapt) or non-targeting control (neg. con). At DIV 7, cultures were treated with 1 µg/µL AD-TAU seeds and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. ( B ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 7 with 1 µg/µL AD-TAU seeds and at DIV 8 incubated with the indicated concentrations of <t>FT671,</t> Spautin-1, or DMSO and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. IC 50 values of 410 nM for FT671 and of 590 nM for Spautin-1 were calculated. Data are presented as percentage seeded mouse Tau aggregation normalized to total protein, mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Ft671, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 27 article reviews

ft671 - by Bioz Stars, 2026-02

94/100 stars

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1) Product Images from "Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation"

Article Title: Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms262211062

Figure Legend Snippet: Silencing and inhibition of Usp7 and Usp10 reduces seeded Tau aggregation induced by AD-TAU seeds in wildtype CTX. ( A ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 1 with 1 µM individual siRNA Usp7 #13, Usp10 #14, smartpool Mapt (siMapt) or non-targeting control (neg. con). At DIV 7, cultures were treated with 1 µg/µL AD-TAU seeds and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. ( B ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 7 with 1 µg/µL AD-TAU seeds and at DIV 8 incubated with the indicated concentrations of FT671, Spautin-1, or DMSO and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. IC 50 values of 410 nM for FT671 and of 590 nM for Spautin-1 were calculated. Data are presented as percentage seeded mouse Tau aggregation normalized to total protein, mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Techniques Used: Inhibition, Isolation, Incubation, Control

USP7 and USP10 inhibitors reduce seeded TAU aggregation and increase polyubiquitination of TAU inclusions in CTX from rTg4510 mice. Cortical neurons isolated from rTg4510 mouse embryos were incubated at DIV 7 with 2 ng/µL S1p or P3 TAU seeds and at DIV 8 incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO and harvested at DIV 15 to measure seeded TAU aggregation by the TAU aggregation assay ( A ) presented as percentage seeded TAU aggregation normalized to total protein, mean ± SD from 5 wells, representative from 3 independent experiments and by immunocytochemistry and quantifications of pS422-TAU ( B ) and polyubiquitination by P4D1 ( C ) immunoreactivity shown as Spot Total Intensity/healthy nuclei count as mean ± SD from 5 wells representative from 3 independent experiments. Following IC 50 values were calculated for FT671, GNE-6640, and Spautin-1, respectively: ( A ) 400–440 nM, 680–730 nM, and 560–650 nM; ( B ) 400–540 nM, 780–840 nM, and 600–690 nM; ( C ) 460–510 nM, 740–780 nM, and 580–640 nM. ( D ) P4D1 polyubiquitin and pS422-TAU immunoreactivity of P3-induced seeded TAU inclusions is presented as Spot Total Intensity/Spot as mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was conducted; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001).

Figure Legend Snippet: USP7 and USP10 inhibitors reduce seeded TAU aggregation and increase polyubiquitination of TAU inclusions in CTX from rTg4510 mice. Cortical neurons isolated from rTg4510 mouse embryos were incubated at DIV 7 with 2 ng/µL S1p or P3 TAU seeds and at DIV 8 incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO and harvested at DIV 15 to measure seeded TAU aggregation by the TAU aggregation assay ( A ) presented as percentage seeded TAU aggregation normalized to total protein, mean ± SD from 5 wells, representative from 3 independent experiments and by immunocytochemistry and quantifications of pS422-TAU ( B ) and polyubiquitination by P4D1 ( C ) immunoreactivity shown as Spot Total Intensity/healthy nuclei count as mean ± SD from 5 wells representative from 3 independent experiments. Following IC 50 values were calculated for FT671, GNE-6640, and Spautin-1, respectively: ( A ) 400–440 nM, 680–730 nM, and 560–650 nM; ( B ) 400–540 nM, 780–840 nM, and 600–690 nM; ( C ) 460–510 nM, 740–780 nM, and 580–640 nM. ( D ) P4D1 polyubiquitin and pS422-TAU immunoreactivity of P3-induced seeded TAU inclusions is presented as Spot Total Intensity/Spot as mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was conducted; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001).

Techniques Used: Isolation, Incubation, Immunocytochemistry

Silencing and inhibition of Usp7 and Usp10 reduces seeded TAU aggregation in OHSCs from rTg4510 mice. ( A , B ) Organotypic hippocampal slice cultures (OHSCs) isolated from rTg4510 mouse pups were treated at DIV 0 with 1 µM siRNA Usp7 #13 or Usp10 #14 or non-targeting control (neg. control). At DIV 3, slices were incubated with 2 ng/µL S1p or P3 TAU seeds per slice. ( C , D ) OHSCs isolated from rTg4510 mouse pups were incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO 3 h before addition of 2 ng/µL S1p or P3 TAU seeds per slice at DIV 3. ( A , D ) Slices were methanol-fixed at DIV 8 and processed for AT8 and pS422-TAU immunocytochemistry to measure seeded TAU aggregation. Representative confocal images (5× objective) of nuclei stained with Hoechst (in gray) and P3-induced seeded TAU aggregation detected with AT8 (in green) and pS422-TAU (in red) immunoreactivity from 3 independent experiments. The scale bar corresponds to 500 µm ( A , C ). Quantifications of AT8 immunoreactivity from S1p and P3 seeded slices are shown as total AT8 intensity as mean ± SD from 6 to 10 individual slices presented as circles ( B , D ). Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (** p < 0.01, *** p < 0.001, **** p < 0.0001).

Figure Legend Snippet: Silencing and inhibition of Usp7 and Usp10 reduces seeded TAU aggregation in OHSCs from rTg4510 mice. ( A , B ) Organotypic hippocampal slice cultures (OHSCs) isolated from rTg4510 mouse pups were treated at DIV 0 with 1 µM siRNA Usp7 #13 or Usp10 #14 or non-targeting control (neg. control). At DIV 3, slices were incubated with 2 ng/µL S1p or P3 TAU seeds per slice. ( C , D ) OHSCs isolated from rTg4510 mouse pups were incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO 3 h before addition of 2 ng/µL S1p or P3 TAU seeds per slice at DIV 3. ( A , D ) Slices were methanol-fixed at DIV 8 and processed for AT8 and pS422-TAU immunocytochemistry to measure seeded TAU aggregation. Representative confocal images (5× objective) of nuclei stained with Hoechst (in gray) and P3-induced seeded TAU aggregation detected with AT8 (in green) and pS422-TAU (in red) immunoreactivity from 3 independent experiments. The scale bar corresponds to 500 µm ( A , C ). Quantifications of AT8 immunoreactivity from S1p and P3 seeded slices are shown as total AT8 intensity as mean ± SD from 6 to 10 individual slices presented as circles ( B , D ). Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (** p < 0.01, *** p < 0.001, **** p < 0.0001).

Techniques Used: Inhibition, Isolation, Control, Incubation, Immunocytochemistry, Staining

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Journal: International Journal of Molecular Sciences

Article Title: Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation

doi: 10.3390/ijms262211062

Figure Lengend Snippet: Silencing and inhibition of Usp7 and Usp10 reduces seeded Tau aggregation induced by AD-TAU seeds in wildtype CTX. ( A ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 1 with 1 µM individual siRNA Usp7 #13, Usp10 #14, smartpool Mapt (siMapt) or non-targeting control (neg. con). At DIV 7, cultures were treated with 1 µg/µL AD-TAU seeds and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. ( B ) Cortical neurons isolated from wildtype mouse embryos were incubated at DIV 7 with 1 µg/µL AD-TAU seeds and at DIV 8 incubated with the indicated concentrations of FT671, Spautin-1, or DMSO and harvested at DIV 15 to measure seeded Tau aggregation by the mouse Tau aggregation assay. IC 50 values of 410 nM for FT671 and of 590 nM for Spautin-1 were calculated. Data are presented as percentage seeded mouse Tau aggregation normalized to total protein, mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Article Snippet: The USP7 inhibitors GNE-6640 (HY-112937) and FT671 (HY-107985) and the USP10/13 inhibitor Spautin-1 (HY-12990) were purchased from MedChemExpress EU (Sollentuna, Sweden).

Techniques: Inhibition, Isolation, Incubation, Control

Journal: International Journal of Molecular Sciences

Article Title: Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation

doi: 10.3390/ijms262211062

Figure Lengend Snippet: USP7 and USP10 inhibitors reduce seeded TAU aggregation and increase polyubiquitination of TAU inclusions in CTX from rTg4510 mice. Cortical neurons isolated from rTg4510 mouse embryos were incubated at DIV 7 with 2 ng/µL S1p or P3 TAU seeds and at DIV 8 incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO and harvested at DIV 15 to measure seeded TAU aggregation by the TAU aggregation assay ( A ) presented as percentage seeded TAU aggregation normalized to total protein, mean ± SD from 5 wells, representative from 3 independent experiments and by immunocytochemistry and quantifications of pS422-TAU ( B ) and polyubiquitination by P4D1 ( C ) immunoreactivity shown as Spot Total Intensity/healthy nuclei count as mean ± SD from 5 wells representative from 3 independent experiments. Following IC 50 values were calculated for FT671, GNE-6640, and Spautin-1, respectively: ( A ) 400–440 nM, 680–730 nM, and 560–650 nM; ( B ) 400–540 nM, 780–840 nM, and 600–690 nM; ( C ) 460–510 nM, 740–780 nM, and 580–640 nM. ( D ) P4D1 polyubiquitin and pS422-TAU immunoreactivity of P3-induced seeded TAU inclusions is presented as Spot Total Intensity/Spot as mean ± SD from 5 wells representative from 3 independent experiments. Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was conducted; asterisks indicate significance (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: The USP7 inhibitors GNE-6640 (HY-112937) and FT671 (HY-107985) and the USP10/13 inhibitor Spautin-1 (HY-12990) were purchased from MedChemExpress EU (Sollentuna, Sweden).

Techniques: Isolation, Incubation, Immunocytochemistry

Journal: International Journal of Molecular Sciences

Article Title: Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation

doi: 10.3390/ijms262211062

Figure Lengend Snippet: Silencing and inhibition of Usp7 and Usp10 reduces seeded TAU aggregation in OHSCs from rTg4510 mice. ( A , B ) Organotypic hippocampal slice cultures (OHSCs) isolated from rTg4510 mouse pups were treated at DIV 0 with 1 µM siRNA Usp7 #13 or Usp10 #14 or non-targeting control (neg. control). At DIV 3, slices were incubated with 2 ng/µL S1p or P3 TAU seeds per slice. ( C , D ) OHSCs isolated from rTg4510 mouse pups were incubated with the indicated concentrations of FT671, GNE-6044, Spautin-1 or DMSO 3 h before addition of 2 ng/µL S1p or P3 TAU seeds per slice at DIV 3. ( A , D ) Slices were methanol-fixed at DIV 8 and processed for AT8 and pS422-TAU immunocytochemistry to measure seeded TAU aggregation. Representative confocal images (5× objective) of nuclei stained with Hoechst (in gray) and P3-induced seeded TAU aggregation detected with AT8 (in green) and pS422-TAU (in red) immunoreactivity from 3 independent experiments. The scale bar corresponds to 500 µm ( A , C ). Quantifications of AT8 immunoreactivity from S1p and P3 seeded slices are shown as total AT8 intensity as mean ± SD from 6 to 10 individual slices presented as circles ( B , D ). Brown–Forsythe and Welch ANOVA with Dunnett’s T3 post hoc test was performed; asterisks indicate significance (** p < 0.01, *** p < 0.001, **** p < 0.0001).

Article Snippet: The USP7 inhibitors GNE-6640 (HY-112937) and FT671 (HY-107985) and the USP10/13 inhibitor Spautin-1 (HY-12990) were purchased from MedChemExpress EU (Sollentuna, Sweden).

Techniques: Inhibition, Isolation, Control, Incubation, Immunocytochemistry, Staining

a Schematic representation of the generation of USP7-797-resistant variants. CHP-212 cells were exposed to 10 μM USP7-797 for 5 days, refreshing with drug-free media, and repeating for 5 cycles. Six drug-resistant monoclonal cells (R1-R6) were selected. b Dose-response curves of USP7i USP7-797 and FT671 in parental and resistant cells following a 5-day exposure. Left panel, the IC 50 values of USP7-797 and FT671 were determined using SRB assays. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments). Right panel, the resistance factor (RF) was calculated by comparing the average IC 50 value of the resistant cells to that of the parental cells. c The chemical structure and dose-response curves of another USP7i GNE-6640 in the parental and resistant cells. Cells were treated with GNE-6640 for 5 days, and cell viability was assessed using SRB assays. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments). d The IC 50 values of MLN4924, KSQ4279, Adriamycin, Bortezomib, TAXOL, and VCR in parental and resistant cells were determined using SRB assays following 3 days exposure. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments).

Journal: Nature Communications

Article Title: USP7 V517F mutation as a mechanism of inhibitor resistance

doi: 10.1038/s41467-025-56981-w

Figure Lengend Snippet: a Schematic representation of the generation of USP7-797-resistant variants. CHP-212 cells were exposed to 10 μM USP7-797 for 5 days, refreshing with drug-free media, and repeating for 5 cycles. Six drug-resistant monoclonal cells (R1-R6) were selected. b Dose-response curves of USP7i USP7-797 and FT671 in parental and resistant cells following a 5-day exposure. Left panel, the IC 50 values of USP7-797 and FT671 were determined using SRB assays. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments). Right panel, the resistance factor (RF) was calculated by comparing the average IC 50 value of the resistant cells to that of the parental cells. c The chemical structure and dose-response curves of another USP7i GNE-6640 in the parental and resistant cells. Cells were treated with GNE-6640 for 5 days, and cell viability was assessed using SRB assays. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments). d The IC 50 values of MLN4924, KSQ4279, Adriamycin, Bortezomib, TAXOL, and VCR in parental and resistant cells were determined using SRB assays following 3 days exposure. Data are presented as mean ± SD ( n = 3 technical replicates; 3 independent experiments).

Article Snippet: FT671, GNE-6640, and Taxol were purchased from MedChemExpress (Monmouth Junction, NJ, USA).

Techniques:

USP7 inhibitors reduce EBNA1 protein levels. (A) Raji cells were treated with DMSO or GNE6776 (40 μM) for 96 h and then assayed by Western blot for EBNA1, USP7, or loading control β‐Actin (actin). Molecular weight markers are indicated to the left. (B) Quantification of EBNA1 levels relative to actin for three biological replicates shown in panel A. (C) YCCEL1 cells were treated with DMSO or GNE6776 (20 μM) for 48 h and then assayed by Western blot for EBNA1, USP7, Zta, Ea‐D or loading control β‐Actin. (D) Quantification of EBNA1 levels relative to actin for 3 biological replicates shown in panel C. (E) SNU719 cells was treated with DMSO or (R)‐FT671 (30 μM) for 96 h and then assayed by Western blot for EBNA1, USP7, Zta, Ea‐D or loading control β‐Actin. (F) Quantification of EBNA1 levels relative to actin for 3 biological replicates shown in panel E. (G) SNU719 cells were treated with DMSO or XL177A (30 μM) for 6 days and then assayed by Western blot for EBNA1, USP7, Ea‐D or loading control β‐Actin. (H) Quantification of EBNA1 levels relative to actin for three biological replicates shown in panel E. (I) AGS cells were transfected with the empty vector (EV) or vector expressing Flag‐tagged EBNA1. At 24 h posttransfection, the media was replaced with either normal media containing DMSO or 20 µM of GNE6776 for 48 h. (J) Densitometry of FLAG‐EBNA1 levels normalized to β‐actin for three replicates shown in panel I. The error bar represents the standard deviation mean (sdm). *** p < 0.0005 ** p < 0.01, * p < 0.0.05 using a two‐tailed student t ‐test.

Journal: Journal of Medical Virology

Article Title: USP7 Inhibitors Destabilize EBNA1 and Suppress Epstein‐Barr Virus Tumorigenesis

doi: 10.1002/jmv.70168

Figure Lengend Snippet: USP7 inhibitors reduce EBNA1 protein levels. (A) Raji cells were treated with DMSO or GNE6776 (40 μM) for 96 h and then assayed by Western blot for EBNA1, USP7, or loading control β‐Actin (actin). Molecular weight markers are indicated to the left. (B) Quantification of EBNA1 levels relative to actin for three biological replicates shown in panel A. (C) YCCEL1 cells were treated with DMSO or GNE6776 (20 μM) for 48 h and then assayed by Western blot for EBNA1, USP7, Zta, Ea‐D or loading control β‐Actin. (D) Quantification of EBNA1 levels relative to actin for 3 biological replicates shown in panel C. (E) SNU719 cells was treated with DMSO or (R)‐FT671 (30 μM) for 96 h and then assayed by Western blot for EBNA1, USP7, Zta, Ea‐D or loading control β‐Actin. (F) Quantification of EBNA1 levels relative to actin for 3 biological replicates shown in panel E. (G) SNU719 cells were treated with DMSO or XL177A (30 μM) for 6 days and then assayed by Western blot for EBNA1, USP7, Ea‐D or loading control β‐Actin. (H) Quantification of EBNA1 levels relative to actin for three biological replicates shown in panel E. (I) AGS cells were transfected with the empty vector (EV) or vector expressing Flag‐tagged EBNA1. At 24 h posttransfection, the media was replaced with either normal media containing DMSO or 20 µM of GNE6776 for 48 h. (J) Densitometry of FLAG‐EBNA1 levels normalized to β‐actin for three replicates shown in panel I. The error bar represents the standard deviation mean (sdm). *** p < 0.0005 ** p < 0.01, * p < 0.0.05 using a two‐tailed student t ‐test.

Article Snippet: For cell culture, GNE6776 (MedChem Express‐ Cat: HY‐107986), XL177A (MedChem Express‐ Cat: HY‐138794), and (R)‐FT671 (Aobious‐ Cat: AOB12773) were resuspended in DMSO to make a stock solution and then diluted in fresh media to reach the final working concentration.

Techniques: Western Blot, Control, Molecular Weight, Transfection, Plasmid Preparation, Expressing, Standard Deviation, Two Tailed Test

GNE6776 inhibits EBNA1 DNA binding and EBV episome maintenance. (A) SNU719 cells were treated with DMSO or GNE6776 (20 μM) for 6 days and then assayed by ChIP‐qPCR with IgG control or EBNA1 antibody and assayed by qPCR with primers amplifying FR, Qp, or OriLyt regions of EBV genome. Bars represent the sdm of 3 biological replicates. (B) ChIP‐qPCR as described in panel A, except using antibodies for USP7 and IgG control. **** p <0.0001, *** p <0.001 using student two‐tailed t ‐test. (C) A replication assay in 293 T cells transfected with either EV or WT EBNA1 and then treated with either DMSO or GNE6776. ( n = 2) (D) Quantitation of the replication efficiency of panel E. (E) SNU719 cells treated with DMSO or GNE6776 followed by pulse‐field gel electrophoresis (PFGE) and Southern blot probed for EBV genome (Wp repeats, lower panel) or cellular loading control Chr 17 probe (top panel). (F) Quantification of EBV episome copy number averaging 3 biological replicates shown in panel C. Error bars are sdm. * p < 0.05 student two‐tailed t ‐test. (G) Digital droplet PCR (ddPCR) analysis of EBV DNA copy number in YCCEL1 cells treated with DMSO or GNE6776 using a probe for LMP1 gene relative to cellular RPP30. (H) ddPCR analysis of EBV DNA copy number in SNU719 cells treated with DMSO or XL177A. (I) Same as in panels E and F, except comparing DMSO with (R)‐FT671. * p < 0.05, ** p < 0.005, *** p < 0.0009 student two‐tailed t ‐test.

Journal: Journal of Medical Virology

Article Title: USP7 Inhibitors Destabilize EBNA1 and Suppress Epstein‐Barr Virus Tumorigenesis

doi: 10.1002/jmv.70168

Figure Lengend Snippet: GNE6776 inhibits EBNA1 DNA binding and EBV episome maintenance. (A) SNU719 cells were treated with DMSO or GNE6776 (20 μM) for 6 days and then assayed by ChIP‐qPCR with IgG control or EBNA1 antibody and assayed by qPCR with primers amplifying FR, Qp, or OriLyt regions of EBV genome. Bars represent the sdm of 3 biological replicates. (B) ChIP‐qPCR as described in panel A, except using antibodies for USP7 and IgG control. **** p <0.0001, *** p <0.001 using student two‐tailed t ‐test. (C) A replication assay in 293 T cells transfected with either EV or WT EBNA1 and then treated with either DMSO or GNE6776. ( n = 2) (D) Quantitation of the replication efficiency of panel E. (E) SNU719 cells treated with DMSO or GNE6776 followed by pulse‐field gel electrophoresis (PFGE) and Southern blot probed for EBV genome (Wp repeats, lower panel) or cellular loading control Chr 17 probe (top panel). (F) Quantification of EBV episome copy number averaging 3 biological replicates shown in panel C. Error bars are sdm. * p < 0.05 student two‐tailed t ‐test. (G) Digital droplet PCR (ddPCR) analysis of EBV DNA copy number in YCCEL1 cells treated with DMSO or GNE6776 using a probe for LMP1 gene relative to cellular RPP30. (H) ddPCR analysis of EBV DNA copy number in SNU719 cells treated with DMSO or XL177A. (I) Same as in panels E and F, except comparing DMSO with (R)‐FT671. * p < 0.05, ** p < 0.005, *** p < 0.0009 student two‐tailed t ‐test.

Techniques: Binding Assay, Control, Two Tailed Test, Transfection, Quantitation Assay, Nucleic Acid Electrophoresis, Southern Blot

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