Tara L. Davis

TL;DR: It is found that regions of the isomerase domain outside the proline-binding surface impart isoform specificity for both in vivo substrates and drug design, and it is hypothesized that there is a well-defined molecular surface corresponding to the substrate-binding S2 position that is a site of diversity in the cyclophilin family.

TL;DR: Systematic mutagenic analysis of the peptide−Gβ1 interface indicates that distinct sets of amino acids within this interface are required for biennial activation of G protein through a novel Gβγ-dependent, nucleotide exchange-independent mechanism.

TL;DR: It is shown that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipid and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.

TL;DR: It is shown that locking the switch into the trans isomer leads to shortened circadian periods, and isomerization is regulated by the cyclophilin family of peptidyl-prolyl isomerases, highlighting the potential for regulation of BMAL1 protein dynamics in period determination.

TL;DR: The coupled pathway of residues that connect the juxtamembrane segment, the activation loop, and the catalytic residues of the kinase domain likely delineates a molecular recognition pathway for most of the Eph RTKs, helping to characterize the dynamic nature of these physiologically important enzymes.