Results 121 to 130 of about 902 (153)

5-Aminothiazoles Reveal a New Ligand-Binding Site on Prolyl Oligopeptidase Which is Important for Modulation of Its Protein-Protein Interaction-Derived Functions. [PDF]

J Med Chem
Pätsi HT, Kilpeläinen TP, Jumppanen M, Uhari-Väänänen J, Wielendaele PV, De Lorenzo F, Cui H, Auno S, Saharinen J, Seppälä E, Sipari N, Savinainen J, De Meester I, Lambeir AM, Lahtela-Kakkonen M, Myöhänen TT, Wallén EAA.   +16 more
europepmc   +1 more source

Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging. [PDF]

J Exp Bot
Hoernstein SNW, Miniera AA, Reski R.
europepmc   +1 more source

Resolving multiple conformations of a sub-80 kDa Chagas vaccine candidate by cryo-EM led integrative approach

Campeotto I, Batra S, Ragan T, Frank A, Kaplan M, Lancey C, Assadipapari M, Ying C, Struwe W, Hesketh E, Barfod L.   +10 more
europepmc   +1 more source

Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP and its antibody response characterisation

Batra S, Olmo F, Ragan TJ, Kaplan M, Calvaresi V, Frank AM, Lancey C, Assadipapari M, Ying C, Ying C, Struwe WB, Struwe WB, Hesketh E, Kelly JM, Barfod L, Campeotto I.   +15 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Prolyl oligopeptidase from Pyrococcus furiosus

Biochimica et Biophysica Acta (BBA) - General Subjects, 2001
Publisher Summary Prolyl oligopeptidase (POPase) also called “prolyl endopeptidase,” postproline cleaving enzyme is a serine protease that cleaves peptides at the carboxyl side of proline residues. The enzyme is widely distributed in nature and is found in organisms ranging from mammals to bacteria.
V J, Harwood, H J, Schreier
openaire   +4 more sources

Prolyl Oligopeptidase Structure and Dynamics

CNS & Neurological Disorders - Drug Targets, 2011
Prolyl oligopeptidase or prolyl endopeptidase (PREP; EC 3.4.21.26) is an atypical serine protease that hydrolyses peptides and peptide hormones after proline in peptides up to around 30 residues long. Evidence suggests an involvement in learning and memory, and the enzyme is implicated in diseases including amnesia and depression.
Dean, Rea, Vilmos, Fülöp
openaire   +2 more sources

Oligopeptidases, and the Emergence of the Prolyl Oligopeptidase Family

Biological Chemistry Hoppe-Seyler, 1992
Oligopeptidases are endopeptidases that are not proteinases in the strict sense, since they do not hydrolyse peptide bonds in proteins, but act only on smaller polypeptides or oligopeptides. These enzymes apparently perform important, specialized biological functions that include the modification or destruction of peptide messenger molecules ...
A J, Barrett, N D, Rawlings
openaire   +2 more sources

Isoquinoline alkaloids as prolyl oligopeptidase inhibitors

Fitoterapia, 2015
Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyses proline-containing peptides at the carboxy terminus of proline residues. It has been associated with schizophrenia, bipolar affective disorder, and related neuropsychiatric disorders and therefore may have important clinical implications.
Lucie, Cahlíková, Lucie, Hulová, Martina, Hrabinová, Jakub, Chlebek, Anna, Hošťálková, Markéta, Adamcová, Marcela, Šafratová, Daniel, Jun, Lubomír, Opletal, Miroslav, Ločárek, Kateřina, Macáková   +10 more
openaire   +2 more sources

Truncated prolyl oligopeptidase from Pyrococcus furiosus

Proteins: Structure, Function, and Bioinformatics, 2007
AbstractThe peptidase domain of prolyl oligopeptidase is covered by a propeller domain, which excludes large peptides and proteins from the catalytic triad. Previous studies indicated that some amino acids of the N‐terminal region constitute a part of the substrate entrance to the active site.
Tünde, Juhász, Zoltán, Szeltner, László, Polgár   +2 more
openaire   +2 more sources

Suggested functions for prolyl oligopeptidase: A puzzling paradox

Clinica Chimica Acta, 2007
Prolyl oligopeptidase (PO, E.C. 3.4.21.26) is a post-proline cleaving enzyme with endopeptidase activity towards peptides not longer than 30 amino acids. It has been purified and characterized from various mammalian and bacterial sources, but despite its thorough enzymological and structural characterization, the exact function of PO remains obscure ...
Brandt, Inger, Scharpe, Simon, Lambeir, Anne-Marie   +2 more
openaire   +3 more sources