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Ghislain Opdenakker

Researcher at Rega Institute for Medical Research

Publications -  561
Citations -  35678

Ghislain Opdenakker is an academic researcher from Rega Institute for Medical Research. The author has contributed to research in topics: Chemokine & Matrix metalloproteinase. The author has an hindex of 95, co-authored 547 publications receiving 32815 citations. Previous affiliations of Ghislain Opdenakker include The Catholic University of America & University of Oxford.

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Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)

TL;DR: The ability of gelatinase B to degrade components of the extracellular matrix and to regulate the activity of a number of soluble proteins confers an important role in various physiological and pathological processes, including reproduction, growth, development, inflammation, and vascular and proliferative diseases.
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Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases

TL;DR: This Review compares the major classes of MMP inhibitors and advocates that future drug discovery should be based on crucial insights into the differential roles of specific MMPs in pathophysiology obtained with animal models, including knockout studies.
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Concepts and Principles of O-Linked Glycosylation

TL;DR: The biosynthesis, structures, and functions of O-glycosylation, as a complex posttranslational event, is reviewed and compared and the recent development of novel technologies for glycan analysis promises to yield new insights in the factors that determine site occupancy, structure-function relationship, and the contribution of O -linked sugars to physiological and pathological processes.
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Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact

TL;DR: A better understanding of regulator (IL-8) and effector molecules (gelatinase B) of neutrophils and of mechanisms underlying leukocytosis, shock syndromes, and stem cell mobilization by IL-8 is led to.