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 The oligomeric structure of high molecular weight adiponectin. The oligomeric structure of high molecular weight adiponectin. FEBS Lett. (0014-5793) 2007 imex curation Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. 2009-01-08 Only protein-protein interactions bovin-serum Bovine serum serum Serum biochemical biochemical predetermined predetermined participant predetermined Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. FEBS Lett. (0014-5793) 2007 2009-01-08 Only protein-protein interactions imex curation The oligomeric structure of high molecular weight adiponectin. The oligomeric structure of high molecular weight adiponectin. FEBS Lett. (0014-5793) 2007 imex curation Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. 2009-01-08 Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. FEBS Lett. (0014-5793) 2007 2009-01-08 Only protein-protein interactions imex curation The oligomeric structure of high molecular weight adiponectin. The oligomeric structure of high molecular weight adiponectin. FEBS Lett. (0014-5793) 2007 imex curation Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. 2009-01-08 Only protein-protein interactions mouse-3t3_l1 Mus musculus embryonic cells Fibroblast-like. Adipose like when confluent 3t3_l1 Mouse embryo cells Fibroblast-like. Adipose like when confluent comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Suzuki S., Wilson-Kubalek EM., Wert D., Tsao TS., Lee DH. FEBS Lett. (0014-5793) 2007 2009-01-08 Only protein-protein interactions imex curation adipo_bovin Adiponectin ADIPOQ ACRP30 APM1 Adipocyte, C1q and collagen domain-containing protein 30 kDa adipocyte complement-related protein Adipocyte complement-related 30 kDa protein Adipose most abundant gene transcript 1 protein protein protein bovin Bos taurus (Bovine) Bovine MLLQGALLLLLALPSHGEDNMEDPPLPKGACAGWMAGIPGHPGHNGTPGRDGRDGTPGEKGEKGDPGLVGPKGDTGETGITGIEGPRGFPGTPGRKGEPGESAYVYRSAFSVGLERQVTVPNVPIRFTKIFYNQQNHYDGTTGKFLCNIPGLYYFSYHITVYLKDVKVSLYKNDKALLFTHDQFQDKNVDQASGSVLLYLEKGDQVWLQVYEGENHNGVYADNVNDSTFTGFLLYHNIVE 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 409122E49F3AF253 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 Adiponectin 4 predetermined predetermined participant predetermined 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: 18.0 physical association physical association F1 FEBS-Letters mint adipoq-1 3 Adiponectin 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 18.0 direct interaction direct interaction F2 FEBS-Letters mint adipoq-1 2 Adiponectin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction F4 FEBS-Letters It is hardly visible an oligomeric architecture. mint