Signal peptide peptidase (SPP) and the homologous SPP-like (SPPL) proteases SPPL2a,
SPPL2b, SPPL2c and SPPL3 belong to the family of GxGD intramembrane proteases …

Signal peptide peptidase (SPP) and the four SPP‐like proteases SPPL2a, SPPL2b, SPPL2c
and SPPL3 constitute a family of aspartyl intramembrane proteases with homology to …

SPP (signal peptide peptidase) is an aspartyl intramembrane cleaving protease, which
processes a subset of signal peptides, and is linked to the quality control of ER …

Intramembrane proteolysis describes the cleavage of substrate proteins within their
hydrophobic transmembrane segments. Several families of intramembrane proteases have …

Intramembrane-cleaving proteases are members of a novel type of enzyme that hydrolyse
substrate proteins within transmembrane regions. The presently known proteases that …

Intramembrane proteolysis is now firmly established as a prominent biological process, and
structure elucidation is emerging as the new frontier in the understanding of these novel …

Five genes encode the five human signal peptide peptidases (SPPs), which are
intramembrane-cleaving aspartyl proteases (aspartyl I-CLiPs). SPPs have been conserved …

Signal peptide peptidase (SPP) and the four related SPP-like (SPPL) proteases are
homologues of the presenilins, which comprise the catalytic centre of the γ-secretase …

Signal peptide peptidase-like 3 (SPPL3) is a Golgi-resident intramembrane-cleaving
protease that is highly conserved among multicellular eukaryotes pointing to pivotal …

Type I signal peptidase (SPase I) catalyzes the cleavage of the amino-terminal signal
sequences from preproteins destined for cell export. Preproteins contain a signal sequence …