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Image Search Results
Journal: PLoS ONE
Article Title: Differences in the Serum Nonesterified Fatty Acid Profile of Young Women Associated with a Recent History of Gestational Diabetes and Overweight/Obesity
doi: 10.1371/journal.pone.0128001
Figure Lengend Snippet: Clinical and biochemical characteristics of the study cohort.
Article Snippet: The following additional laboratory parameters were analyzed:
Techniques:
Journal: PLoS ONE
Article Title: Differences in the Serum Nonesterified Fatty Acid Profile of Young Women Associated with a Recent History of Gestational Diabetes and Overweight/Obesity
doi: 10.1371/journal.pone.0128001
Figure Lengend Snippet: Fasting serum NEFA profiles and total NEFA concentrations.
Article Snippet: The following additional laboratory parameters were analyzed:
Techniques:
Journal: Nature Communications
Article Title: Structural basis of arrestin-3 activation and signaling
doi: 10.1038/s41467-017-01218-8
Figure Lengend Snippet: IP mediated trimerization and receptor-independent activation in cells. a - b Sedimentation velocity analytical ultracentrifugation (SVAUC) of arrestin-3. Measurements were performed in triplicate. a Representative SVAUC run in the absence of IP predicts a molecular weight matching a monomer. b In the presence of 100 µM IP , the predicted molecular weight is consistent with a trimer. c Representative size exclusion chromatograms of arrestin-3 (Arr3) in the presence and absence of IP . In the absence of IP , 60 µM arrestin-3 (black) elutes at volume corresponding to the Stokes radius of a globular protein with a molecular mass of 64 ± 5.9 kDa. In the presence of 100 μM IP , the elution volume is consistent with a globular protein of molecular mass 169.6 ± 9.7 kDa. The ratio of these molecular weights is consistent with IP -dependent trimer formation. Measurements were performed in triplicate, errors are ± SEM. d Plot of the probability of the distances between spin labels at S13 and A392 for 100 µM arrestin-3 in the presence of the indicated molar ratios of IP ; inset shows the location of the spin labeled sites in basal arrestin-3 (PDB entry 3P2D ). e Comparison of JNK3 activation by GFP-arrestin-3 and Cys-less mutant. GFP-tagged arrestin allowed comparison of the expression levels of wild-type and variant arrestin-3, as described , . JNK3 activation (mean ± SEM) was assessed by measuring the pp-JNK3 levels in COS7 cells co-transfected with HA-ASK1, HA-JNK3 and GFP or Venus-tagged wild-type and Cys-less arrestin-3. Assay was repeated five times and JNK3 phosphorylation was compared by one-way ANOVA followed by Bonferroni post hoc test with correction for multiple comparisons. *** p < 0.001
Article Snippet: The expression level of HA-ASK1, Flag-JNK3 and arrestin-3 were assessed by Western analysis using antibodies against the HA tag (
Techniques: Activation Assay, Sedimentation, Analytical Ultracentrifugation, Molecular Weight, Labeling, Comparison, Mutagenesis, Expressing, Variant Assay, Transfection, Phospho-proteomics