Davy Waterschoot
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Davy Waterschoot has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
- Christophe Ampe
Ghent University
2 shared publications - Joël Vandekerckhove
VIB and Ghent University
2 shared publications - Anja Lambrechts
Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium
1 shared publication - Bruno Constantin
Institut de Physiologie et Biologie Cellulaire, UMR CNRS/Université de Poitiers 6187, Pôle Biologie Santé, 86022 Poitiers cedex, France
1 shared publication - Davina Tondeleir
Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, A. Baertsoenkaai 3, Gent, Belgium
1 shared publication - Drieke Vandamme
Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, A. Baertsoenkaai 3, Gent, Belgium
1 shared publication
Latest Publications
- Open Access
- 1 January 2010
- Published by Springer Nature in BMC Molecular Biology
- Vol. 11 (1) , 45
Identification and expression analysis of splice variants of mouse enabled homologue during development and in adult tissues
The Enabled/Vasodilator stimulated phosphoprotein (Ena/VASP) gene family comprises three genes in vertebrates: Vasp, Enabled homologue (Enah) and Ena-VASP like (Evl). Enah has the most complex gene structure. It has extra alternatively included exons compared to Vasp and Evl, and possibly one alternatively excluded intron S. The aim of this mapping study was to probe the occurrence of combinations of exon usage in Enah thereby identifying possible vertebrate ENAH splice variants. We investigated this via an in silico analysis and by performing a reverse transcription-polymerase chain reaction (RT-PCR) screen on mouse samples. We further probed the expression pattern of mouse Enah splice variants during development and in a selection of mouse adult tissues and mouse cell lines.
- 1 January 2010
- Published by Springer Nature in BMC Molecular Biology
- Vol. 11 (1) , 45
Open AccessIdentification and expression analysis of splice variants of mouse enabled homologue during development and in adult tissues
The Enabled/Vasodilator stimulated phosphoprotein (Ena/VASP) gene family comprises three genes in vertebrates: Vasp, Enabled homologue (Enah) and Ena-VASP like (Evl). Enah has the most complex gene structure. It has extra alternatively included exons compared to Vasp and Evl, and possibly one alternatively excluded intron S. The aim of this mapping study was to probe the occurrence of combinations of exon usage in Enah thereby identifying possible vertebrate ENAH splice variants. We investigated this via an in silico analysis and by performing a reverse transcription-polymerase chain reaction (RT-PCR) screen on mouse samples. We further probed the expression pattern of mouse Enah splice variants during development and in a selection of mouse adult tissues and mouse cell lines.
- Open Access
- 1 January 2009
- Published by Springer Nature in BMC Research Notes
- Vol. 2 (1) , 40
Phenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes
Nemaline myopathy is a neuromuscular disorder characterized by the presence of nemaline bodies in patient muscles. 20% of the cases are associated with α-skeletal muscle actin mutations. We previously showed that actin mutations can cause four different biochemical phenotypes and that expression of NM associated actin mutants in fibroblasts, myoblasts and myotubes induces a range of cellular defects.
- 1 January 2009
- Published by Springer Nature in BMC Research Notes
- Vol. 2 (1) , 40
Open AccessPhenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes
Nemaline myopathy is a neuromuscular disorder characterized by the presence of nemaline bodies in patient muscles. 20% of the cases are associated with α-skeletal muscle actin mutations. We previously showed that actin mutations can cause four different biochemical phenotypes and that expression of NM associated actin mutants in fibroblasts, myoblasts and myotubes induces a range of cellular defects.