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Substrate-induced conformational changes occur in all cleaved forms of caspase-6.
Modeling nonaqueous proton wires built from helical peptides: biased proton transfer driven by helical dipoles.
Phosphorylation regulates assembly of the caspase-6 substrate-binding groove.
Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics.
Discovery of an allosteric site in the caspases.
Searching for new allosteric sites in enzymes.
Robust production of a peptide library using methodological synchronization.
Dissecting an allosteric switch in caspase-7 using chemical and mutational probes.
A designed redox-controlled caspase.
Mechanism of zinc-mediated inhibition of caspase-9.
Structural basis of fluorescence quenching in caspase activatable-GFP.
A tunable, modular approach to fluorescent protease-activated reporters.
A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.
Co-delivery of protein and small molecule therapeutics using nanoparticle-stabilized nanocapsules.
Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.
Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apoptotic Activity by Two Distinct Mechanisms.
The Unique Cofactor Region of Zika Virus NS2B-NS3 Protease Facilitates Cleavage of Key Host Proteins.
Rare human Caspase-6-R65W and Caspase-6-G66R variants identify a novel regulatory region of Caspase-6 activity.
Caspase-9 CARD?:?core domain interactions require a properly formed active site.
Chemoproteomics Using Nucleotide Acyl Phosphates Reveals an ATP Binding Site at the Dimer Interface of Procaspase-6.