Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Daisy Dewitte"'
Autor:
Daisy Dewitte, David Bourry, Frans Borremans, José C. Martins, Stefaan Rossenu, Christophe Ampe, Marleen Van Troys, Joël Vandekerckhove, W Vermeulen, Marc Goethals
Publikováno v:
Journal of Molecular Biology. 359:1277-1292
The HeadPiece (HP) domain, present in several F-actin-binding multi-domain proteins, features a well-conserved, solvent-exposed PXWK motif in its C-terminal subdomain. The latter is an autonomously folding subunit comprised of three alpha-helices org
Autor:
Daisy Dewitte, Joël Vandekerckhove, Natalie De Ruyck, Kanako Ono, Christophe Ampe, Shoichiro Ono, Veronique Jonckheere, Marleen Van Troys
Publikováno v:
Molecular Biology of the Cell. 15:4735-4748
Generating specific actin structures via controlled actin polymerization is a prerequisite for eukaryote development and reproduction. We here report on an essential Caenorhabditis elegans protein tetraThymosinbeta expressed in developing neurons and
Autor:
Daisy Dewitte, Stefaan Rossenu, Marleen Van Troys, Joël Vandekerckhove, Danny Peelaers, Shirley Leyman, Christophe Ampe, Veronique Jonckheere
Publikováno v:
Journal of Biological Chemistry. 278:16642-16650
We propose phage display combined with enzyme-linked immunosorbent assay as a tool for the systematic analysis of protein-protein interactions by investigating the binding behavior of variants to a partner protein. Via enzyme-linked immunosorbent ass
Autor:
Marleen Van Troys, Daisy Dewitte, M Goethals, Christophe Ampe, Jean-Luc Verschelde, Joël Vandekerckhove
Publikováno v:
Journal of Biological Chemistry. 272:32750-32758
Cofilin is representative for a family of low molecular weight actin filament binding and depolymerizing proteins. Recently the three-dimensional structure of yeast cofilin and of the cofilin homologs destrin and actophorin were resolved, and a strik
Publikováno v:
Journal of Protein Chemistry. 16:499-503
Phage display is a technique in which a foreign protein or peptide is presented at the surface of a (filamentous) bacteriophage. This system, developed by Smith [(1985), Science 228, 1315-1317], was originally used to create large libraries of antibo
Autor:
Christophe Ampe, Olivier Debeir, Christine Decaestecker, Daisy Dewitte, Robert J. Eddy, John S. Condeelis, Marleen Van Troys, Shirley Leyman, Laila Ritsma, Jacco van Rheenen, Davy Waterschoot, Joël Vandekerckhove, Mazen Sidani
Publikováno v:
Molecular biology of the cell, 20 (21
Molecular Biology of the Cell, 20(21), 4509-4523. American Society for Cell Biology
Molecular Biology of the Cell, 20(21), 4509-4523. American Society for Cell Biology
Cofilin is a key player in actin dynamics during cell migration. Its activity is regulated by (de)phosphorylation, pH, and binding to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P(2)]. Here, we here use a human cofilin-1 (D122K) mutant with increas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b46c211a408ea1d1c9673aa052e10a0
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52937
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52937
Autor:
Stefaan, Rossenu, Shirley, Leyman, Daisy, Dewitte, Danny, Peelaers, Veronique, Jonckheere, Marleen, Van Troys, Joel, Vandekerckhove, Christophe, Ampe
Publikováno v:
The Journal of biological chemistry. 278(19)
We propose phage display combined with enzyme-linked immunosorbent assay as a tool for the systematic analysis of protein-protein interactions by investigating the binding behavior of variants to a partner protein. Via enzyme-linked immunosorbent ass
Autor:
Daisy Dewitte, Christophe Ampe, Marleen Van Troys, Jean-Luc Verschelde, Marc Goethals, Joël Vandekerckhove
Publikováno v:
Biochemistry. 39(40)
We studied the effect of mutations in an alpha-helical region of actophorin (residues 91-108) on F-actin and PIP(2) binding. As in cofilin, residues in the NH(2)-terminal half of this region are involved in F-actin binding. We show here also that bas
We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants. The N-terminal part (residues 1-16) and a hexapeptide motif (residues 17-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91f9d01acffe9fccaa11f824b102267f
https://europepmc.org/articles/PMC449934/
https://europepmc.org/articles/PMC449934/
Publikováno v:
BMC Biochemistry. 3:12
Profilin is a small cytoskeletal protein which interacts with actin, proline-rich proteins and phosphatidylinositol 4,5-bisphosphate (PI(4,5)-P2). Crystallography, NMR and mutagenesis of vertebrate profilins have revealed the amino acid residues that