Journal: PLoS ONE

Article Title: Changes in Muscle Cell Metabolism and Mechanotransduction Are Associated with Myopathic Phenotype in a Mouse Model of Collagen VI Deficiency

doi: 10.1371/journal.pone.0056716

Figure Lengend Snippet: Panel A: Histograms and representative immunoblot images of IDH1 and IDH2 in gastrocnemius, tibialis anterior and diaphragm from Col6a1 −/− and wild-type mice (n = 4; mean ± S.D.; Student’s T-test). Panel B: schematic representation of IDHs pathways. Grey and empty rectangles contain gene names of deregulated proteins observed by 2D-DIGE and western blotting, respectively. Arrows indicate the protein trend in gastrocnemius (G), tibialis anterior (T) and diaphragm (D). For 2D-DIGE, the arrows direction indicates up- and down-regulation, the thickness the % of spot variation. = /↓ or = /↑ indicate the differential expression of isoforms of the same protein in a given muscle. For western blotting, the arrows direction indicates the up- and down-regulation of relative variation of Col6a1 −/− versus control wild-type muscle.

Article Snippet: Blots were incubated with rabbit or goat polyclonal primary antibodies (Cell Signaling Technology and Santa Cruz Biotechnology) as follows: anti-TN-C (1∶500), anti-ROCK1 (1∶500), anti PI3K (1∶1000), anti FAK (1∶1000), anti-PPARγ (1∶1000), anti-PPARα (1∶1000), anti-PPARβ (1∶1000), anti-Sirt1 (1∶1000), anti-Sirt3 (1∶1000), anti-FASN (1∶1000), anti-IDH1 (1∶1000), anti-IDH2 (1∶1000) and anti β-tubulin (1∶1000).

Techniques: Western Blot, Expressing

Journal: Fluids and Barriers of the CNS

Article Title: Induced pluripotent stem cell-derived cells model brain microvascular endothelial cell glucose metabolism

doi: 10.1186/s12987-022-00395-z

Figure Lengend Snippet: Western blot antibodies

Article Snippet: IDH1 , Cell Signaling Technology , 8137S.

Techniques: Western Blot

Journal: NPJ Precision Oncology

Article Title: Secondary IDH1 resistance mutations and oncogenic IDH2 mutations cause acquired resistance to ivosidenib in cholangiocarcinoma

doi: 10.1038/s41698-022-00304-5

Figure Lengend Snippet: a Immunoblot analysis of IDH1 expression in TF-1 cells infected with lentivirus expressing the indicated IDH1 variants and treated with vehicle-control (DMSO), 500 nM ivosidenib (IVO), or 500 nM LY3410738 (LY), as indicated. b , c Quantification of (R) -2HG ( b ) and fold-change in (R) -2HG ( c ) in the TF-1 cell lines shown in a , as indicated. Shown are mean values (±SD) of duplicate experiments. d , e Proliferation under cytokine-poor conditions ( d ) and fold-change in day 15 cell counts ( e ) of the TF-1 cells shown in ( a ) The mean (±SD) cell counts of three replicates is shown. f Fold-change in intracellular (R) -2HG in TF-1 cells expressing IDH1 R132H (left) or IDH1 R132H/D279N (right) treated overnight with the indicated concentrations of LY3410738. Shown are mean values (±SD) of duplicate experiments. In all cases, representative results from at least two independent experiments are shown.

Article Snippet: Primary antibodies used: rabbit monoclonal HA-tag (Cell Signaling Technology, #3724) at a 1:1000 dilution, rabbit polyclonal anti-IDH1 (Cell Signaling Technology, #3997) at a 1:500 dilution, and mouse monoclonal anti-vinculin (Sigma, V9131) at a 1:1000 dilution.

Techniques: Western Blot, Expressing, Infection

Journal: NPJ Precision Oncology

Article Title: Secondary IDH1 resistance mutations and oncogenic IDH2 mutations cause acquired resistance to ivosidenib in cholangiocarcinoma

doi: 10.1038/s41698-022-00304-5

Figure Lengend Snippet: a Predicted binding mode of ivosidenib (IVO, carbons in yellow) in the allosteric site of IDH1 R132C (carbons in blue). IVO is recognized by IDH1 R132C principally by donating a hydrogen bond to the IDH1 D279 side chain and accepting a hydrogen bond from the IDH1 A111 backbone. Further specific intermolecular interactions involve aromatic contacts with IDH1 W267, IDH1 W124, and IDH1 Y285. b IVO is predicted to have impaired binding to IDH1 R132C/D279N (carbons in red) because the chlorophenyl ring clashes with the mutated asparagine side chain (orange X). c Predicted binding mode of LY3410738 (LY, carbons in green) in the allosteric site of IDH1 R132C (carbons in blue). LY3410738 covalently binds to IDH1 C269 and displays many favorable electrostatic interactions with the protein: the protonated piperazine makes an ionic interaction with the IDH1 D279 side chain and the inhibitor additionally makes two hydrogen bonds with the IDH1 I128 backbone and accepts a hydrogen bond from the IDH1 L120 backbone. d LY3410738 is predicted to adopt a similar covalent binding mode to IDH1 R132C/D279N as it does to IDH1 R132C by keeping all of its numerous anchor points and by replacing the ionic interaction with aspartate with a hydrogen bond to the oxygen of the asparagine-mutated side chain at position 279.

Article Snippet: Primary antibodies used: rabbit monoclonal HA-tag (Cell Signaling Technology, #3724) at a 1:1000 dilution, rabbit polyclonal anti-IDH1 (Cell Signaling Technology, #3997) at a 1:500 dilution, and mouse monoclonal anti-vinculin (Sigma, V9131) at a 1:1000 dilution.

Techniques: Binding Assay

Journal: iScience

Article Title: Targeting HOTAIRM1 ameliorates glioblastoma by disrupting mitochondrial oxidative phosphorylation and serine metabolism

doi: 10.1016/j.isci.2022.104823

Figure Lengend Snippet:

Article Snippet: IDH1 Rabbit polyclonal antibody , Cell Signaling Technology , # 3997; RRID: AB_1904011.

Techniques: Labeling, Recombinant, Transfection, Protease Inhibitor, Plasmid Preparation, Isolation, Reporter Assay, Microarray, shRNA, Negative Control, Software