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Clinical and biochemical characteristics of the study cohort.
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Clinical and biochemical characteristics of the study cohort.
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Clinical and biochemical characteristics of the study cohort.
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Clinical and biochemical characteristics of the study cohort.
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Clinical and biochemical characteristics of the study cohort.
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Clinical and biochemical characteristics of the study cohort.
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Cell Signaling Technology Inc gfp
IP mediated trimerization and receptor-independent activation in cells. a - b Sedimentation velocity analytical ultracentrifugation (SVAUC) <t>of</t> <t>arrestin-3.</t> 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 <t>GFP-arrestin-3</t> 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
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Bio-Rad high-performance liquid chromatography (hplc) variant ii analyzer
IP mediated trimerization and receptor-independent activation in cells. a - b Sedimentation velocity analytical ultracentrifugation (SVAUC) <t>of</t> <t>arrestin-3.</t> 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 <t>GFP-arrestin-3</t> 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
High Performance Liquid Chromatography (Hplc) Variant Ii Analyzer, supplied by Bio-Rad, 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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Philips Healthcare eds mira ii
IP mediated trimerization and receptor-independent activation in cells. a - b Sedimentation velocity analytical ultracentrifugation (SVAUC) <t>of</t> <t>arrestin-3.</t> 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 <t>GFP-arrestin-3</t> 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
Eds Mira Ii, supplied by Philips Healthcare, 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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Image Search Results


Clinical and biochemical characteristics of the study cohort.

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: HbA1c (VARIANT II TURBO HbA1c Kit—2.0, Bio-Rad Laboratories, Hercules, USA), hsCRP (wide-range CRP, Siemens AG, Erlangen, Germany), gamma-GT (enzymatic caloric test, Roche Diagnostics), triglycerides (enzymatic caloric test, Roche Diagnostics), cholesterol (enzymatic caloric test, Roche Diagnostics), HDL (enzymatic caloric test, Roche Diagnostics), and LDL was calculated with the Friedewald equation (all triglyceride levels were below 400 mg/dl).

Techniques:

Fasting serum NEFA profiles and total NEFA concentrations.

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: HbA1c (VARIANT II TURBO HbA1c Kit—2.0, Bio-Rad Laboratories, Hercules, USA), hsCRP (wide-range CRP, Siemens AG, Erlangen, Germany), gamma-GT (enzymatic caloric test, Roche Diagnostics), triglycerides (enzymatic caloric test, Roche Diagnostics), cholesterol (enzymatic caloric test, Roche Diagnostics), HDL (enzymatic caloric test, Roche Diagnostics), and LDL was calculated with the Friedewald equation (all triglyceride levels were below 400 mg/dl).

Techniques:

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

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 (Cell Signaling #C29F4, 1:1000 dilution), the Flag tag (Sigma #F3165, 1:500 dilution), arrestin (F4C1) or GFP (JL-8, Choltech #632381, 1:2000 dilution), respectively.

Techniques: Activation Assay, Sedimentation, Analytical Ultracentrifugation, Molecular Weight, Labeling, Comparison, Mutagenesis, Expressing, Variant Assay, Transfection, Phospho-proteomics