Journal: Nature Communications

Article Title: B7-H3-mediated cis-inhibition of EGFR by a tumor-selective bispecific antibody enhances anti-tumor efficacy and minimizes toxicities

doi: 10.1038/s41467-026-69703-7

Figure Lengend Snippet: a In vitro synergy assay ( n = 3 biological replicates) and ( b ) Western blot analysis of IBI334 and Osimertinib in NCI-H1975 LTC cells ( n = 2 biological replicates). For Western blot analysis, cells were treated with 50 nM Osimertinib and/or 100 nM IBI334 for 4 h. c Synergy scores were calculated using the Synergy Finder+ algorithm based on the in vitro growth data from ( a ). d BALB/c nude mice ( n = 6 mice/group) bearing NCI-H1975 LTC tumors were treated with IBI334 (30 mg/kg, 4 doses bi-weekly), Osimertinib (10 mg/kg daily for 14 days), or combo. Arrows indicate antibody treatment, while lines denote the duration of Osimertinib treatment. e Representative IHC staining from the experiment in panel ( n = 2 mice). Tumors were collected 24 h post-second dose. Scale bar =50 µm. f In vitro synergy assay ( n = 3 biological replicates) and ( g ) Western blot analysis of IBI334 and AMG510 in NCI-H358 cells ( n = 2 biological replicates). Synergy scores were calculated using the Synergy Finder+ algorithm. For Western blot analysis, cells were treated with 5 nM IBI334, 15 nM AMG510, or both for 4 hours. h NOG mice ( n = 7 mice/group) bearing NCI-H358 tumors were treated with 4 doses of 10 mg/kg bi-weekly IBI334, 10 mg/kg daily of AM510 for 14 days, or their combination at the same dosage. Arrows indicate antibody treatment, while lines denote the duration of AMG510 treatment. For the in vitro efficacy of a and f, data represent mean ± SD. For the in vivo of d and h, data represent mean ± SEM, and statistical significance was assessed by two-way ANOVA with Tukey’s post hoc test. Source data are provided as a Source Data file.

Article Snippet: The small molecule inhibitors employed in this study included Osimertinib (MCE, HY-15772), AMG510 (MCE, HY-114277), MRTX133 (MCE, HY-134813), and LY3009120 (Macklin, L873098).

Techniques: In Vitro, Western Blot, Immunohistochemistry, In Vivo

Journal: iScience

Article Title: Proteomics- and BRET- screens identify SPRY2 as a Ras effector that impacts its membrane organization

doi: 10.1016/j.isci.2025.113974

Figure Lengend Snippet: K-RasG12V engagement with SPRY2 is sensitive to lipidation inhibitors (A) Confocal imaging shows that the plasma membrane localization of mNG-tagged SPRY2 in HEK cells is sensitive to lipidation inhibitors mevastatin (Mev) and/or 2-bromopalmitate (2-BP). Scale bars = 20 μm (B–D) Effect of mevastatin (Mev) and/or 2-bromopalmitate (2-BP) on interaction-BRET of nL-K-RasG12V with mNG-SPRY2 (B), mNG-N-SPRY2 (C) or mNG-C-SPRY2 (D) in HEK cells (donor:acceptor plasmid ratio = 1:8). Plotted are means ± SEM from N = 5 independent biological repeats analyzed using Welch's t test (B–D). (E) Dose-dependent disruption of nL-K-RasG12C/mNG-SPRY2 BRET-interaction after treatment with G12Ci AMG510 in HEK cells (donor:acceptor plasmid ratio = 1:40). Plotted are means ± SEM from N = 3–9 independent biological repeats. (F) Dose-dependent effect of SNAP-tagged SPRY2 or N-SPRY2 expression on nL-K-RasG12V/mNG-C-Raf-RBD BRET in HEK cells (donor:acceptor plasmid ratio = 1:8). Plotted are means ± SEM from N = 4 independent biological repeats with values at highest modulator concentration compared using Welch's t test. Dashed line indicates the response to 5 μM mevastatin (Mev) treatment, indicating full plasma membrane displacement. See also .

Article Snippet: AMG510 , Selleckchem , S8830.

Techniques: Imaging, Clinical Proteomics, Membrane, Plasmid Preparation, Disruption, Expressing, Concentration Assay