MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Activation of AMPK by berberine promotes adiponectin multimerization in 3T3-L1 adipocytes. Activation of AMPK by berberine promotes adiponectin multimerization in 3T3-L1 adipocytes. FEBS Lett. (0014-5793) 2011 Li Y., Wang P., Zhuang Y., Lin H., Li Y., Liu L., Meng Q., Cui T., Liu J., Li Z. suggested by lperfetto in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel western blot western blot Immuno blot Immuno blot Li Y., Wang P., Zhuang Y., Lin H., Li Y., Liu L., Meng Q., Cui T., Liu J., Li Z. suggested by lperfetto FEBS Lett. (0014-5793) 2011 Activation of AMPK by berberine promotes adiponectin multimerization in 3T3-L1 adipocytes. Activation of AMPK by berberine promotes adiponectin multimerization in 3T3-L1 adipocytes. FEBS Lett. (0014-5793) 2011 Li Y., Wang P., Zhuang Y., Lin H., Li Y., Liu L., Meng Q., Cui T., Liu J., Li Z. suggested by lperfetto in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation predetermined predetermined participant predetermined Li Y., Wang P., Zhuang Y., Lin H., Li Y., Liu L., Meng Q., Cui T., Liu J., Li Z. suggested by lperfetto FEBS Lett. (0014-5793) 2011 adipo_mouse Adiponectin Apm1 Adipocyte, C1q and collagen domain-containing protein 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Adipocyte-specific protein AdipoQ Adipoq Acdc Acrp30 protein protein mouse Mus musculus Mouse MLLLQALLFLLILPSHAEDDVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN DIP protein Q60994 original sequence version: 102 mint Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW 0ECC687D9A8E8123 adipoq-1 2 Adiponectin 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 3.0 physical association physical association f2c mint The decrease in LMW (trimer) adiponectin and the increase in HMW (high-molecular-weight) adiponectin were confirmed by velocity sedimentation on sucrose gradients (Fig. 2C). adipoq-1 1 Adiponectin 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 3.0 physical association physical association mint To investigate the effect of berberine on adiponectin multimerization during differentiation, we examined the level of adiponectin oligomers on 2-15% gradient gel electrophoresis under non-reducing and non-heat-denaturing conditions. This simple method has been used for the separation and semi-quantification of different adiponectin oligomers. The antibody, which is raised against the globular domain of adiponectin, recognizes specifically the oligomeric forms of adiponectin. When berberine was present during differentiation, the levels of LMW(trimer), MMW(hexamer) and HMW (high-molecular-weight) adiponectin were decreased f1c f2b f2d f4b f4c adipoq-1 1 Adiponectin 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 6.0 physical association physical association mint To investigate the effect of berberine on adiponectin multimerization during differentiation, we examined the level of adiponectin oligomers on 2-15% gradient gel electrophoresis under non-reducing and non-heat-denaturing conditions. This simple method has been used for the separation and semi-quantification of different adiponectin oligomers. The antibody, which is raised against the globular domain of adiponectin, recognizes specifically the oligomeric forms of adiponectin. When berberine was present during differentiation, the levels of LMW(trimer), MMW(hexamer) and HMW (high-molecular-weight) adiponectin were decreased f1c f2b f2d f4b f4c