Search Results - "Szamosi, Ilona"
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The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity
Published in Biochimica et biophysica acta (01-01-2013)“…Prolyl oligopeptidase (POP) has emerged as a drug target for neurological diseases. A flexible loop structure comprising loop A (res. 189–209) and loop B (res…”
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A Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii
Published in The Journal of biological chemistry (01-06-2013)“…Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been under debate. Here we present the structure of a hexameric…”
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Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE
Published in The Journal of biological chemistry (21-01-2011)“…Acylaminoacyl peptidase from Aeropyrum pernix is a homodimer that belongs to the prolyl oligopeptidase family. The monomer subunit is composed of one hydrolase…”
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A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization
Published in The Journal of biological chemistry (14-06-2013)“…Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been under debate. Here we present the structure of a hexameric…”
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GAP43 shows partial co-localisation but no strong physical interaction with prolyl oligopeptidase
Published in Biochimica et biophysica acta (01-12-2010)“…It has recently been proposed that prolyl oligopeptidase (POP), the cytosolic serine peptidase with neurological implications, binds GAP43 (Growth-Associated…”
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Structure and Catalysis of Acylaminoacyl Peptidase
Published in The Journal of biological chemistry (21-01-2011)“…Acylaminoacyl peptidase from Aeropyrum pernix is a homodimer that belongs to the prolyl oligopeptidase family. The monomer subunit is composed of one hydrolase…”
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Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality
Published in Acta crystallographica. Section D, Biological crystallography. (01-03-2015)“…Acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments. In the case of AAP from Aeropyrum pernix (ApAAP),…”
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