Her primary scientific interests are in Dipeptidyl peptidase, Biochemistry, Molecular biology, Chemokine and Dipeptidyl peptidase-4. Her Dipeptidyl peptidase research incorporates elements of Oligopeptidase, Endocrinology, In vitro and Internal medicine. Her Molecular biology study combines topics from a wide range of disciplines, such as CC chemokine receptors, T cell and CXCL2.
Her Chemokine research includes themes of Biological activity and Chemotaxis. The various areas that she examines in her Dipeptidyl peptidase-4 study include Neuropeptide, Neuropeptide Y receptor and Renal ischemia. Her studies in Protease integrate themes in fields like Dipeptidyl peptidase 8, Chemokine receptor and Protein tyrosine phosphatase.
The scientist’s investigation covers issues in Dipeptidyl peptidase, Biochemistry, Internal medicine, Dipeptidyl peptidase-4 and Enzyme. Her Dipeptidyl peptidase study focuses on Dipeptidyl-peptidase II in particular. Her Biochemistry study frequently draws connections between adjacent fields such as Fibroblast activation protein, alpha.
Within one scientific family, Ingrid De Meester focuses on topics pertaining to Endocrinology under Internal medicine, and may sometimes address concerns connected to Vasoactive intestinal peptide and Transplantation. Her work in Dipeptidyl peptidase-4 covers topics such as Protease which are related to areas like Cell biology. Her Enzyme research integrates issues from Dipeptidyl Peptidase 9, Dipeptidyl peptidase 8, Chemical synthesis and Stereochemistry.
Ingrid De Meester mainly focuses on Immunology, Dipeptidyl peptidase, Internal medicine, Fibroblast activation protein, alpha and Dipeptidyl peptidase-4. Her Immunology research incorporates themes from Proteases, Disease and Transplantation. Her research in Dipeptidyl peptidase intersects with topics in Cancer research, CXCL10, Extracellular matrix, Structure–activity relationship and Type 2 diabetes.
Ingrid De Meester combines subjects such as Gastroenterology and Diabetes mellitus, Endocrinology with her study of Internal medicine. Her Dipeptidyl peptidase-4 research includes elements of Porphyromonas gingivalis, Pharmacokinetics, In vitro and Microbiology. Her Serine protease research is included under the broader classification of Biochemistry.
Her primary areas of study are Dipeptidyl peptidase, Immunology, Dipeptidyl peptidase-4, In vitro and Antibody. Ingrid De Meester combines subjects such as Cancer research and Type 2 diabetes with her study of Dipeptidyl peptidase. Her Immunology research incorporates elements of Disease and Transplantation.
Her Dipeptidyl peptidase-4 study integrates concerns from other disciplines, such as Interleukin 6, Oligopeptidase, Structure–activity relationship and Macrophage. Her Oligopeptidase study is concerned with the field of Biochemistry as a whole. Her In vitro research includes themes of Porphyromonas gingivalis, Periodontitis and Microbiology.
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Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV.
Anne-Marie Lambeir;Christine Durinx;Simon Scharpé;Ingrid De Meester.
Critical Reviews in Clinical Laboratory Sciences (2003)
The effects of psychological stress on humans: increased production of pro-inflammatory cytokines and a Th1-like response in stress-induced anxiety
Michael Maes;Cai Song;Aihua Lin;Raf De Jongh.
CD26, let it cut or cut it down
Ingrid De Meester;Stephan Korom;Stephan Korom;Jo Van Damme;Simon Scharpé.
Immunology Today (1999)
Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection.
Paul Proost;Ingrid De Meester;Dominique Schols;Sofie Struyf.
Journal of Biological Chemistry (1998)
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides.
Christine Durinx;Anne-Marie Lambeir;Eugène Bosmans;Jean-Bernard Falmagne.
FEBS Journal (2000)
Kinetic Investigation of Chemokine Truncation by CD26/Dipeptidyl Peptidase IV Reveals a Striking Selectivity within the Chemokine Family
Anne-Marie Lambeir;Paul Proost;Christine Durinx;Gunther Bal.
Journal of Biological Chemistry (2001)
Processing by CD26/dipeptidyl-peptidase IV reduces the chemotactic and anti-HIV-1 activity of stromal-cell-derived factor-1α
Paul Proost;Sofie Struyf;Dominique Schols;Christine Durinx.
FEBS Letters (1998)
Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form.
Inger Brandt;Anne-Marie Lambeir;Jean-Marie Ketelslegers;Marc Vanderheyden.
Clinical Chemistry (2006)
Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78beta into a most efficient monocyte attractant and CCR1 agonist.
Paul Proost;Patricia Menten;Sofie Struyf;Evemie Schutyser.
Natural truncation of RANTES abolishes signaling through the CC chemokine receptors CCR1 and CCR3, impairs its chemotactic potency and generates a CC chemokine inhibitor.
Sofie Struyf;Ingrid De Meester;Simon Scharpé;Jean-Pierre Lenaerts.
European Journal of Immunology (1998)
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