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Filip Goossens

Researcher at University of Antwerp

Publications -  42
Citations -  2288

Filip Goossens is an academic researcher from University of Antwerp. The author has contributed to research in topics: Prolyl endopeptidase & Dipeptidyl peptidase. The author has an hindex of 24, co-authored 42 publications receiving 2251 citations.

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Journal ArticleDOI

Proline motifs in peptides and their biological processing.

TL;DR: The conformational restrictions imposed by proline motifs in a peptide chain appear to imply important structural or biological functions as can be deduced from their often remarkably high degree of conservation as found in many proteins and peptides.
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Plasma procarboxypeptidase U in men with symptomatic coronary artery disease.

TL;DR: Results suggest that a mechanism exists by which fibrinolytic function is impaired in a manner that is likely to result in more stable fibrin deposits and increase the risk of precocious CAD as well as early occlusion of venous bypass grafts.
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Alterations in plasma prolyl endopeptidase activity in depression, mania and schizophrenia: effects of antidepressants, mood stabilizers and antipsychotic drugs

TL;DR: The hypothesis that lower P EP activity could play a role in the pathophysiology of major depression, while increased PEP activity may be related to psychotic conditions, such as mania and schizophrenia is supported.
Journal Article

The unique properties of dipeptidyl-peptidase IV (DPP IV / CD26) and the therapeutic potential of DPP IV inhibitors.

TL;DR: In this paper, the properties and functions of dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5) were discussed, and the role of CD26 in the intestinal and renal handling of proline containing peptides, in cell adhesion, in peptide metabolism, in the immune system and in HIV infection.
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The Unique Properties of Dipeptidyl-Peptidase IV (DPP IV / CD26) and the Therapeutic Potential of DPP IV Inhibitors

TL;DR: The latest developments in the search for new inhibitors will be reported as well as the discovery of new natural substrates for DPP IV such as the glucagon-like peptides and the chemokines.