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The prolyl oligopeptidase family
Cellular and Molecular Life Sciences CMLS, 2002A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze peptides containing more than about 30 residues. This group is unrelated to the classical trypsin and subtilisin families, and includes dipeptidyl peptidase IV, acylaminoacyl peptidase and oligopeptidase B, in addition to the prototype prolyl oligopeptidase.
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Structure, Function and Biological Relevance of Prolyl Oligopeptidase
Current Protein & Peptide Science, 2008A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze proteins and peptides containing more than 30 residues. The crystal structure of prolyl oligopeptidase (POP) has shown that the enzyme is composed of a peptidase domain with an alpha/beta hydrolase fold and a seven-bladed beta-propeller domain.
Szeltner, Zoltán, Polgár, László
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Prolyl oligopeptidase stimulates the aggregation of α-synuclein
Peptides, 2008Despite its thorough enzymological and biochemical characterization the exact function of prolyl oligopeptidase (PO, E.C. 3.4.21.26) remains unclear. The positive effect of PO inhibitors on learning and memory in animal models for amnesia, enzyme activity measurements in patient samples and (neuro)peptide degradation studies link the enzyme with ...
Brandt, Inger +8 more
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Evolutionary relationships of the prolyl oligopeptidase family enzymes
European Journal of Biochemistry, 2004The prolyl oligopeptidase (POP) family of serine proteases includes prolyl oligopeptidase, dipeptidyl peptidase IV, acylaminoacyl peptidase and oligopeptidase B. The enzymes of this family specifically hydrolyze oligopeptides with less than 30 amino acids.
Jarkko I, Venäläinen +2 more
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Prolyl oligopeptidase and bipolar disorder
Clinical Neuroscience Research, 2004Abstract Many clinical psychiatrists have identified biochemical changes within patients that are common to a particular disorder. Other researchers, using in vitro approaches, have identified effects of psychiatric drugs in cell-based systems and have used these to propose a therapeutic mode of action for these drugs.
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Versatility of Prolyl Oligopeptidase B in Peptide Macrocyclization
ACS Synthetic Biology, 2017Cyclic peptides are promising compounds for new chemical biological tools and therapeutics due to their structural diversity, resistance to proteases, and membrane permeability. Amatoxins, the toxic principles of poisonous mushrooms, are biosynthesized on ribosomes as 35mer precursor peptides, which are ultimately converted to hydroxylated bicyclic ...
R. Michael Sgambelluri +2 more
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Structure-Function Properties of Prolyl Oligopeptidase Family Enzymes
Cell Biochemistry and Biophysics, 2006Prolyl oligopeptidase family enzymes regulate the activity of biologically active peptides and peptide hormones, and they are implicated in diseases, including amnesia, depression, diabetes, and trypanosomiasis. Distinctively, these enzymes hydrolyze only relatively short peptide substrates, while large structured peptides and proteins are not usually ...
Dean, Rea, Vilmos, Fülöp
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Molecular and Biochemical Parasitology, 2012
African trypanosomosis is a parasitic disease in man and animals caused by protozoan parasites of the genus Trypanosoma. Nagana, the cattle form of the disease, is caused by Trypanosoma congolense, Trypanosoma vivax and Trypanosoma brucei brucei.
Kangethe, Richard T. +4 more
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African trypanosomosis is a parasitic disease in man and animals caused by protozoan parasites of the genus Trypanosoma. Nagana, the cattle form of the disease, is caused by Trypanosoma congolense, Trypanosoma vivax and Trypanosoma brucei brucei.
Kangethe, Richard T. +4 more
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1994
Publisher Summary This chapter focuses on prolyl oligopeptidases. This enzyme degrades a variety of proline-containing peptides by cleaving the peptide bond at the carboxy side of proline residues. Prolyl oligopeptidase is a cytosolic serine peptidase that may be involved in the metabolism of peptide hormones and neuropeptides.
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Publisher Summary This chapter focuses on prolyl oligopeptidases. This enzyme degrades a variety of proline-containing peptides by cleaving the peptide bond at the carboxy side of proline residues. Prolyl oligopeptidase is a cytosolic serine peptidase that may be involved in the metabolism of peptide hormones and neuropeptides.
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Purification and Characterization of Prolyl Oligopeptidase from Bovine Lens
Experimental Eye Research, 1994Prolyl oligopeptidase (EC 3.4.21.26) has been purified 26,000-fold from bovine lens tissue by anion-exchange chromatography, gel filtration and isoelectric focussing, with an overall yield of 11%. The purified enzyme exhibited an isoelectric point of 4.8, a pH optimum of 7.5 and a molecular mass of 72 kDa under both native and denaturing conditions ...
K K, Sharma, B J, Ortwerth
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