Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Filip Goossens"'
Autor:
Dirk Van Duppen, Bert Aertgeerts, L Seuntjens, Jasna Neirinckx, Karin Hannes, Annelies Van Linden, Filip Goossens
Publikováno v:
Patient Education and Counseling. 68:61-65
Objective: The project aimed to search for online evidence in a structured way in consultation with the patient, to investigate whether the evidence discovered changed decisions. Methods: We developed the ‘‘Online on-the-spot’’ method (OOS) a
Publikováno v:
Clinica chimica acta
Carboxypeptidase U (CPU, EC 3.4.17.20) is a recently described basic carboxypeptidase which circulates in plasma as an enzymatically inactive precursor procarboxypeptidase U (proCPU), also known as plasma carboxypeptidase B precursor or thrombin acti
Autor:
Carlo Altamura, Raf De Jongh, Willem Ombelet, Eugene Bosmans, Isabelle Libbrecht, A. Lin, Simon Scharpé, Karolien Stevens, Michael Maes, John Cox, Filip Goossens
Publikováno v:
Journal of affective disorders
Background: There is now some evidence that anxiety or anxiety disorders are related to increased activity of serum prolyl endopeptidase (PEP) and that major depression is related to lower serum PEP. The aims of the present study were to examine (i)
Autor:
Ann Van Gastel, Filip Goossens, Rosaria Pioli, A. Lin, Michael Maes, Stefania Bonaccorso, Laure Delmeire, Simon Scharpé
Publikováno v:
Journal of affective disorders
Background: It is reported that psychiatric disorders, such as depression and schizophrenia, are associated with changes in serum activity of prolyl endopeptidase (EC 3.4.21.26), a cytosolic endopeptidase, which cleaves peptide bonds on the carboxyls
Autor:
S.L. Scharpé, Filip Goossens, Dirk Hendriks, A.H. Lin, L. Juliano, K.A. Schatteman, M. A. Juliano, G. Vanhoof
Publikováno v:
Cytogenetics and cell genetics
A novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exhibiting 44% sequence identity and 62 % sequence similarity to pig kidney X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase ch
Publikováno v:
European Journal of Biochemistry. 233:432-441
Prolyl oligopeptidase was isolated and purified to homogeneity from human lymphocytes, yielding a specific activity of 7780 mU/mg. The molecular mass using size-exclusion chromatography matches the 76 kDa obtained by SDS/PAGE. This provides evidence
Autor:
Achiel Haemers, Dirk Hendriks, M. Borloo, A. Belyaev, Koen Augustyns, Filip Goossens, Padinchare Rajan, Simon Scharpé
Publikováno v:
Bioorganic and medicinal chemistry letters
ResearcherID
ResearcherID
Several acyclic and cyclic dipeptidyl acetals were synthesized. Among these, N-[N-benzyloxycarbonyl-(S)-prolyl]-(S)-prolinal dimethyl acetal 8 was shown to be a potent inhibitor of prolyl endopeptidase.
Publikováno v:
ResearcherID
Many biologically important peptide sequences contain proline. It confers unique conformational constraints on the peptide chain in that the side-chain is cyclized back onto the backbone amide position. Inside an alpha-helix the possibility of making
Autor:
Filip Goossens, Dirk Hendriks, Simon Scharpé, G. Vriend, C. Van Broeckhoven, I. De Meester, G. Vanhoof, L. Hendriks
Publikováno v:
Gene
The human cDNA encoding prolyl endopeptidase, a cytoplasmic endoprotease which hydrolyses the peptide bond at the C-terminal side of proline, was sequenced. After the isolation of the 3′ terminal fragment of the pep cDNA sequence from a human lymph
Autor:
A. Haemers, Christine Durinx, Gunther Bal, Koen Augustyns, Filip Goossens, W. Bollaert, X. M. Zhang, G. Thonus, Anne-Marie Lambeir, A. Belyaev
Publikováno v:
ChemInform. 30
This review deals with the properties and functions of dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5). This membrane anchored ecto-protease has been identified as the leukocyte antigen CD26. The following aspects of DPP IV/CD26 will be discussed : the