Hmgb1 cleavage by complement c1s and its potent anti-in fl ammatory product

HIGHLIGHTS

  • who: . et al. from the University Milano-Bicocca, Italy have published the article: HMGB1 cleavage by complement C1s and its potent anti-in fl ammatory product, in the Journal: (JOURNAL)
  • what: To compare the C1s enzymatic activity, free or within the C1 complex, the authors aimed to use the same C1s molar concentration and secure C1 assembly using C1 concentrations above 0.25 mM. Since free C1s is more efficient, it was further used for the experiments aiming to decipher the C1s cleavage sites in HMGB1. HMGB1 contains atypical features Knowing that the HMGB1 A . . .

     

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