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Arginine mediates nuclear retention of TEAD4 Fig. 4: Arginine mediated nuclear retention of TEAD4. Full size image YAP1 (yes-associated protein 1) is the major effector of Hippo signaling pathway, which has been widely considered as a major coactivator of TEAD proteins. To evaluate whether arg...
In this study, we present a novel and therapeutically promising strain, Lactococcus lactis ssp. lactis Lc4, isolated from dairy sources. Lc4 demonstrated the ability to release the cytostatic agent - arginine deiminase (ADI) - into the post-cultivation supernatant when cultured under conditions mimick...
Gibson A, Hobbs AJ, Mirzazadeh D (1990) l - N G -nitroarginine is a potent inhibitor of non-adrenergic, non-cholinergic relaxations in the rat anococcygeus muscle. Eur J Pharmacol 183:1793Gibson A, Hobbs AJ, Mirzazadeh D (1990) L- N G -nitroarginine is a potent inhibitor of non...
Kinase extracts were analyzed using SILAC mass spectrometry following a previously established protocol26,61. An equal amount of s-SILAC reference ([13C6, 15N4] arginine (Arg 10) and [13C6 15N2] lysine (Lys 8)) (5 mg) lysate was added to non-labeled (5 mg) sample and analyzed on ...
Here, it was discovered that c-Myc is a downstream target of OGG1 under oxidative stress and that H4R3me2a is involved in this transcriptional regulation. The increased level of H4R3me2a induced by H2O2 is regulated by OGG1, which may directly interact with the specific arginine ...
The homologous regions include the conserved catalytic residues of iPLA2, including the GDSRG sequence, in which the arginine is replaced by a lysine in VipD. VipD has phospholipase A activity with diacyl glycerophospholipid substrates [34]; plasmalogen was not tested as a substrate. If the ...
For quantitative proteomic analysis of NAADP and TPC-interacting proteins, HEK293 cells were cultured in SILAC-compatible DMEM supplemented with 10% dialyzed fetal bovine serum and 100 mg/L 13C or 12C-labeled lysine and arginine (all reagents were from Thermo Fischer Scientific) for at least ...
were found to be conserved among the BilR genes from the five confirmed bilirubin-reducing species. A search for this Histidine, Glycine, Aspartic acid, Arginine (HGDR) motif within the Old Yellow Enzyme family revealed that it was nearly universally conserved within a larger clade of proteins ...