Fengli Zhang

TL;DR: It is shown that cyclophilin A, one of the most common PPIases, provides a catalytic environment that acts on the substrate through an electrostatic handle mechanism, which is described as an “electrostatic handle” mechanism.

TL;DR: The solution behavior of the two most prevalent CD147 extracellular isoforms are characterized through biochemical methods that include gel-filtration and native gel analysis as well as directly through multiple NMR methods, which suggest that CD147 homophilic interactions in vivo are mediated through other partners.

TL;DR: Surprisingly, a combination of point mutations has allowed for the specific regulation of many of the exchange processes that occur within CypA, suggesting that the dynamics of an enzyme may be engineered.

TL;DR: It is revealed that extracellular PPIA activity is cell type-dependent and that PPIA signals via multiple cellular receptors beyond the single transmembrane receptor previously identified, Extracellular Matrix MetalloPRoteinase Inducer (EMMPRIN).

TL;DR: It is shown that CXCL8 is dynamic on multiple timescales, which may help explain the versatility in this interleukin for engaging its target receptors.