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PREP gene

Known as: PREP, PROLYL ENDOPEPTIDASE, PROLYL OLIGOPEPTIDASE 
National Institutes of Health

Papers overview

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2005
2005
Effect of Prolyl Endopeptidase Inhibition on Arginine‐Vasopressin and Thyrotrophin‐Releasing Hormone Catabolism in the Rat Brain
Compound S 17092 is a potent and selective inhibitor of prolyl endopeptidase (EC 3.4.21.26, PEP) that may be of therapeutic value… 
Highly Cited
2001
Highly Cited
2001
Structures of Prolyl Oligopeptidase Substrate/Inhibitor Complexes
Structure determination of the inactive S554A variant of prolyl oligopeptidase complexed with an octapeptide has shown that… 
Highly Cited
1996
Highly Cited
1996
New prolyl endopeptidase inhibitors: in vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1]heptane, and perhydroindole derivatives.
A series of potent and selective prolylendopeptidase (PEP) inhibitors of the alpha-keto heterocyclic type has been obtained by… 
Highly Cited
1994
Highly Cited
1994
Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts.
Highly Cited
1994
Highly Cited
1994
Synthesis and structure-activity relationships of peptidyl alpha-keto heterocycles as novel inhibitors of prolyl endopeptidase.
The preparation and in vitro prolyl endopeptidase (PEP) inhibitory activity of a series of alpha-keto heterocyclic compounds is… 
Highly Cited
1992
Highly Cited
1992
Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine.
Review
1992
Review
1992
Oligopeptidases, and the emergence of the prolyl oligopeptidase family.
Oligopeptidases are endopeptidases that are not proteinases in the strict sense, since they do not hydrolyse peptide bonds in… 
Highly Cited
1991
Highly Cited
1991
Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene.
The prolyl endopeptidase [EC 3.4.21.26] gene of Flavobacterium meningosepticum was cloned in Escherichia coli with the aid of an… 
Highly Cited
1986
Highly Cited
1986
Delineation of a Particulate Thyrotropin‐Releasing Hormone‐Degrading Enzyme in Rat Brain by the Use of Specific Inhibitors of Prolyl Endopeptidase and Pyroglutamyl Peptide Hydrolase
Abstract: The degradation of thyrotropin‐releasing hormone in rat brain homogenates was studied in the presence of N… 
Highly Cited
1979
Highly Cited
1979
PURIFICATION AND PROPERTIES OF A PROLYL ENDOPEPTIDASE FROM RABBIT BRAIN
Abstract— An enzyme with the specificity of a prolyl endopeptidase was purified about 880‐fold from rabbit brain. The enzyme… 
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