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1.
Figure 1

Figure 1. From: Competitive Activity-Based Protein Profiling Identifies Aza-?-Lactams as a Versatile Chemotype for Serine Hydrolase Inhibition.

Structures and competitive ABPP of ABL/OBL compounds. (A) Structures of ABL/OBL compounds. (B and C) Competitive ABPP gels of mouse brain membrane (B) and soluble (C, Figure S1) proteomes treated with ABLs/OBLs (30 min) followed by FP-Rh (1 µM, 30 min). Serine hydrolases inhibited by individual ABLs and OBLs are labeled. (D) Competitive ABPP gel of mock- versus mouse ABHD10 (mABHD10)-transfected COS-7 cell proteomes treated with ABL117, followed by FP-Rh (1 µM, 30 min). Fluorescent images shown in gray scale.

Andrea M. Zuhl, et al. J Am Chem Soc. ;134(11):5068-5071.
2.
Figure 2

Figure 2. From: Competitive Activity-Based Protein Profiling Identifies Aza-?-Lactams as a Versatile Chemotype for Serine Hydrolase Inhibition.

Competitive ABPP of ABL303 in situ. (A) Structures of ABL probes. (B and C) Gel-based ABPP of membrane (B) and soluble (C) proteomes from Neuro-2A cells treated with ABL303 (10 - 0.001 µM, 2 h), afforded an (D) IC50 value of 21 nM for inhibition of ABHD10 and no significant inhibition of PME-1. Data are presented as mean values ± SEM; n = 3/group. (E) ABPP-SILAC analysis of Neuro-2A cells treated with ABL303 (red) or ABL127 (black) (100 nM, 2 h; heavy samples) versus DMSO (light samples) revealed selective inhibition of ABHD10 and PME-1, respectively. Data are reported as mean values ± SEM of all peptides quantified for each serine hydrolase.

Andrea M. Zuhl, et al. J Am Chem Soc. ;134(11):5068-5071.

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