Publications
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Identification of the CD163 protein domains involved in infection of the porcine reproductive and respiratory syndrome virus Ghent University
Quantifying information transfer by protein domains: Analysis of the Fyn SH2 domain structure Vrije Universiteit Brussel
Background
Efficient communication between distant sites within a protein is essential for cooperative biological response. Although often associated with large allosteric movements, more subtle changes in protein dynamics can also induce long-range correlations. However, an appropriate formalism that directly relates protein structural dynamics to information exchange between functional sites is still lacking.
Results
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Efficient communication between distant sites within a protein is essential for cooperative biological response. Although often associated with large allosteric movements, more subtle changes in protein dynamics can also induce long-range correlations. However, an appropriate formalism that directly relates protein structural dynamics to information exchange between functional sites is still lacking.
Results
...
Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants? Ghent University
The plant-specific family of DNA-binding proteins containing three HMG-box domains interacts with mitotic and meiotic chromosomes Ghent University University of Antwerp
PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores KU Leuven
Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. Prion-like conversion underlies important biological processes but is also connected to human disease. Yeast prions are the best understood transmissible amyloids. In these proteins, prion formation from an initially soluble state involves a structural conversion, driven, in many cases, by specific domains enriched in glutamine/asparagine (Q/N) ...
Amaranthin-like proteins with aerolysin domains in plants Ghent University
Functional and immunological characterization of a Duffy binding-like alpha domain from Plasmodium falciparum erythrocyte membrane protein 1 that mediates rosetting Institute of Tropical Medicine
The Duffy binding-like (DBL) domains are common adhesion modules present in Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) variants, which are responsible for immune evasion and cytoadherence. Knowledge about how immune responses are acquired against polymorphic DBL domains of PfEMP1 can aid in the development of vaccines for malaria. A recombinant DBLalpha domain, encoded by R29 var1, which binds complement receptor 1 to ...
The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose carbohydrates Vrije Universiteit Brussel
Saccharomyces cerevisiae cells possess a remarkable capacity to adhere to other yeast cells, which is called
flocculation. Flocculation is defined as the phenomenon wherein yeast cells adhere in clumps and sediment
rapidly from the medium in which they are suspended. These cell-cell interactions are mediated by a class of
specific cell wall proteins, called flocculins, that stick out of the cell walls of flocculent cells. The ...
flocculation. Flocculation is defined as the phenomenon wherein yeast cells adhere in clumps and sediment
rapidly from the medium in which they are suspended. These cell-cell interactions are mediated by a class of
specific cell wall proteins, called flocculins, that stick out of the cell walls of flocculent cells. The ...
The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose binding activity. Vrije Universiteit Brussel
The expression of the Flo11 flocculin in Saccharomyces cerevisiae offers the cell a wide range of phenotypes, depending on the strain and the environmental conditions. The most important are pseudohyphae development, invasive growth and flocculation. The mechanism of cellular adhesion mediated by Flo11p is not well understood. Therefore, the N-terminal domain of Flo11p was purified and studied. Although its amino acid sequence shows less ...