Results 31 to 40 of about 717 (174)
Prolyl Oligopeptidase, Inositol Phosphate Signalling and Lithium Sensitivity [PDF]
CNS & Neurological Disorders - Drug Targets, 2011 Inhibition of prolyl oligopeptidase (PO) elevates inositol phosphate (IP) signalling and reduces cell sensitivity to lithium (Li+). This review discusses recent evidence that shows PO acts via the multiple inositol polyphosphate phosphatase (MIPP) to regulate gene expression.
openaire +2 more sources
Transcriptome of Sphaerospora molnari (Cnidaria, Myxosporea) blood stages provides proteolytic arsenal as potential therapeutic targets against sphaerosporosis in common carp [PDF]
, 2020 Background Parasites employ proteases to evade host immune systems, feed and replicate and are often the target of anti-parasite strategies to disrupt these interactions.
Eszterbauer, Edit +4 more
core +1 more source
Structure and Localization of the Mouse Prolyl Oligopeptidase Gene [PDF]
Journal of Biological Chemistry, 1999 We have cloned and characterized the genomic structure of the mouse gene for prolyl oligopeptidase that is mapped to chromosome 10B2-B3. The gene is about 92 kilobases in size and contains 15 exons. All exon-intron junction sequences conform to the GT/AG rule.
A, Kimura +3 more
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ChemBioChem, Volume 27, Issue 8, April 2026.We previously developed a genetically encoded metal‐responsive system using bipyridylalanine (BpyAla) to reversibly control protein function. Here we probe the mechanism in Pyrococcus furiosus prolyl oligopeptidase. Metal‐competition assays, 19F NMR spectroscopy, and molecular dynamics show Ni(II)‐mediated BpyAla2 coordination induces localized ...
Payal +7 more
wiley +1 more source
New tricks of prolyl oligopeptidase inhibitors - A common drug therapy for several neurodegenerative diseases [PDF]
, 2019 Changes in prolyl oligopeptidase (PREP) expression levels, protein distribution, and activity correlate with aging and are reported in many neurodegenerative conditions. Together with decreased neuropeptide levels observed in aging and neurodegeneration,
Julku, Ulrika +5 more
core +1 more source
Kinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase
Biochemistry, 2017 Prolyl oligopeptidase B from Galerina marginata (GmPOPB) has recently been discovered as a peptidase capable of breaking and forming peptide bonds to yield a cyclic peptide. Despite the relevance of prolyl oligopeptidases in human biology and disease, a kinetic analysis pinpointing rate-limiting steps for a member of this enzyme family is not available.
Clarissa M. Czekster, James H. Naismith
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ChemSusChem, Volume 19, Issue 5, 13 March 2026.This study explored the cascade depolymerization of a polyether‐polyester polyurethane based on a combination of low‐temperature thermal treatment and enzymatic hydrolysis. Heat pretreatment changed the physicochemical properties of polyurethane, followed by cutinase‐catalyzed hydrolysis, leading to an increase in weight loss and the production of two ...
Shengwei Sun +8 more
wiley +1 more source
Pharmacoepidemiology and Drug Safety, Volume 34, Issue 12, December 2025.ABSTRACT Background Mounting evidence indicates that Type 2 diabetes mellitus (T2DM) is a public health challenge globally, and its occurrence is anticipated to surge in the forthcoming years. Dipeptidyl peptidase‐4 (DPP‐4) serves as a target for its treatment, with its inhibitors effectively preserving the levels of glucose‐dependent insulinotropic ...
Chinyere Aloke +4 more
wiley +1 more source
The effect of prolyl oligopeptidase inhibitors on alpha-synuclein aggregation and autophagy cannot be predicted by their inhibitory efficacy [PDF]
, 2020 Previous studies have shown that prolyl oligopeptidase (PREP) negatively regulates autophagy and increases the aggregation of alpha-synuclein (alpha Syn), linking it to the pathophysiology of Parkinson's disease.
Hellinen, Laura +10 more
core +1 more source
Unveiling Prolyl Oligopeptidase Ligand Migration by Comprehensive Computational Techniques [PDF]
Biophysical Journal, 2015 Prolyl oligopeptidase (POP) is a large 80 kDa protease, which cleaves oligopeptides at the C-terminal side of proline residues and constitutes an important pharmaceutical target. Despite the existence of several crystallographic structures, there is an open debate about migration (entrance and exit) pathways for ligands, and their coupling with protein
Kotev, Martin +4 more
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