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Full-Text Articles in Medicine and Health Sciences
Specific S100 Proteins Bind Tumor Necrosis Factor And Inhibit Its Activity, Alexey S. Kazakov, Marina Y. Zemskova, Gleb K. Rystsov, Alisa A. Vologzhannikova, Eugenia I. Deryusheva, Victoria A. Rastrygina, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Specific S100 Proteins Bind Tumor Necrosis Factor And Inhibit Its Activity, Alexey S. Kazakov, Marina Y. Zemskova, Gleb K. Rystsov, Alisa A. Vologzhannikova, Eugenia I. Deryusheva, Victoria A. Rastrygina, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Molecular Medicine Faculty Publications
Tumor necrosis factor (TNF) inhibitors (anti-TNFs) represent a cornerstone of the treatment of various immune-mediated inflammatory diseases and are among the most commercially successful therapeutic agents. Knowledge of TNF binding partners is critical for identification of the factors able to affect clinical efficacy of the anti-TNFs. Here, we report that among eighteen representatives of the multifunctional S100 protein family, only S100A11, S100A12 and S100A13 interact with the soluble form of TNF (sTNF) in vitro. The lowest equilibrium dissociation constants (Kd) for the complexes with monomeric sTNF determined using surface plasmon resonance spectroscopy range from 2 nM to 28 nM. The …
Calcium-Bound S100p Protein Is A Promiscuous Binding Partner Of The Four-Helical Cytokines, Alexey S. Kazakov, Eugenia I. Deryusheva, Maria E. Permyakova, Andrey S. Sokolov, Victoria A. Rastrygina, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Calcium-Bound S100p Protein Is A Promiscuous Binding Partner Of The Four-Helical Cytokines, Alexey S. Kazakov, Eugenia I. Deryusheva, Maria E. Permyakova, Andrey S. Sokolov, Victoria A. Rastrygina, Vladimir N. Uversky, Eugene A. Permyakov, Sergei E. Permyakov
Molecular Medicine Faculty Publications
S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to four-helical cytokines, we have probed the interaction of Ca2+-bound recombinant human S100P with a panel of 32 …