nvs compounds cycloheximide chx focus biomolecules Search Results


nvs compounds cycloheximide chx focus biomolecules  (Focus Biomolecules)
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Focus Biomolecules nvs compounds cycloheximide chx focus biomolecules
(A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor <t>cycloheximide</t> (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment
Nvs Compounds Cycloheximide Chx Focus Biomolecules, supplied by Focus Biomolecules, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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(A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment

Journal: bioRxiv

Article Title: Drug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control

doi: 10.1101/2023.01.31.526456

Figure Lengend Snippet: (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment

Article Snippet: The NVS compounds, Bortezomib (BTZ, Merck, Cat# 504314), MLN4924 (Selleckchem, Cat# S7109) and Cycloheximide (CHX, Focus Biomolecules, Cat# 10-117) were all dissolved in DMSO, which also served as vehicle control.

Techniques: Western Blot, Negative Control, Incubation, Control, Mass Spectrometry, Ubiquitin Proteomics, Quantitative Proteomics