Results 1 to 10 of about 486 (117)

Canonical or noncanonical? Structural plasticity of serine protease-binding loops in Kunitz-STI protease inhibitors. [PDF]

open access: bronzeProtein Sci, 2023
AbstractThe Kunitz‐Soybean Trypsin Inhibitor (Kunitz‐STI) family is a large family of proteins with most of its members being protease inhibitors. The versatility of the inhibitory profile and the structural plasticity of these proteins, make this family a promising scaffold for designing new multifunctional proteins.
Guerra Y   +4 more
europepmc   +6 more sources

Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop? [PDF]

open access: bronzeJournal of Structural Biology, 2016
Bi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylated proteins able to inhibit serine and aspartic proteases. Here we report six crystal structures of the wild-type and a non-glycosylated mutant of the bifunctional inhibitor E3Ad obtained at different pH values and space groups.
Yasel Guerra   +4 more
core   +8 more sources

Poplar protease inhibitor expression differs in an herbivore specific manner. [PDF]

open access: yesBMC Plant Biol, 2021
Eberl F   +6 more
europepmc   +3 more sources

Plant Kunitz Inhibitors and Their Interaction with Proteases: Current and Potential Pharmacological Targets. [PDF]

open access: yesInt J Mol Sci, 2022
Bonturi CR   +7 more
europepmc   +1 more source

Abl depletion via autophagy mediates the beneficial effects of quercetin against Alzheimer pathology across species. [PDF]

open access: yesCell Death Discov, 2023
Schiavi A   +13 more
europepmc   +1 more source

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