J
Johannes M. F. G. Aerts
Researcher at Leiden University
Publications - 447
Citations - 23448
Johannes M. F. G. Aerts is an academic researcher from Leiden University. The author has contributed to research in topics: Glucocerebrosidase & Enzyme replacement therapy. The author has an hindex of 79, co-authored 432 publications receiving 21413 citations. Previous affiliations of Johannes M. F. G. Aerts include University of California, Los Angeles & Academic Medical Center.
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Journal ArticleDOI
Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease.
TL;DR: It is concluded that plasma chitotriosidase levels can serve as a new diagnostic hallmark of GD and should prove to be useful in assessing whether clinical manifestations of GD are present and for monitoring the efficacy of therapeutic intervention.
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Novel oral treatment of Gaucher's disease with N-butyldeoxynojirimycin (OGT 918) to decrease substrate biosynthesis
Timothy M. Cox,Robin H. Lachmann,C. E. M. Hollak,Johannes M. F. G. Aerts,S. van Weely,M. Hrebicek,Frances M. Platt,Terry D. Butters,Raymond A. Dwek,C. Moyses,I. Gow,Deborah Elstein,Ari Zimran +12 more
TL;DR: Reducing the rate of substrate formation by OGT 918 improves key clinical features of non-neuronopathic Gaucher's disease and justifies further trials in this and other glycosphingolipid storage disorders.
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Elevated globotriaosylsphingosine is a hallmark of Fabry disease
Johannes M. F. G. Aerts,Johanna E. M. Groener,Sijmen Kuiper,Wilma E. Donker-Koopman,Anneke Strijland,Roelof Ottenhoff,Cindy P. A. A. van Roomen,Mina Mirzaian,Frits A. Wijburg,Gabor E. Linthorst,Anouk C. Vedder,Saskia M. Rombach,Josanne Cox-Brinkman,Pentti Somerharju,Rolf G. Boot,Carla E. M. Hollak,Roscoe O. Brady,Ben J. H. M. Poorthuis +17 more
TL;DR: It is shown that globotriaosylsphingosine is an inhibitor of α-galactosidase A activity and the increased intima-media thickness in Fabry patients therefore may be related to the presence of this metabolite.
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Identification of a novel acidic mammalian chitinase distinct from chitotriosidase
Rolf G. Boot,E. F. C. Blommaart,Erwin Swart,K. Ghauharali-Van der Vlugt,Nora Bijl,C. Moe,Allen R. Place,Johannes M. F. G. Aerts +7 more
TL;DR: The study has revealed the existence of a chitinolytic enzyme in the gastrointestinal tract and lung that may play a role in digestion and/or defense.
Journal ArticleDOI
Cloning of a cDNA Encoding Chitotriosidase, a Human Chitinase Produced by Macrophages
TL;DR: The results show that, in contrast to previous beliefs, human macrophages can synthesize a functional chitinase, a highly conserved enzyme with a strongly regulated expression that may play a role in the degradation of chitIn-containing pathogens and can be used as a marker for specific disease states.