Publications by authors named "Christine Dovengerds"
Article Synopsis
- Dynamin-like proteins (DLPs) play key roles in membrane fusion and fission by polymerizing, with guanylate-binding proteins (GBPs) being a specific family involved in immune responses.
- Human guanylate-binding protein 1 (hGBP1) regulates cell adhesion and migration and is shown to interact with membranes in a GTP-dependent manner.
- The research demonstrates that hGBP1 functions as a molecular switch driven by nucleotide availability, which alters its interactions with membranes and its polymerization behavior, all without needing additional proteins.
Drosophila Ebony is a β-alanyl biogenic amine synthetase with proven function in cuticle and in glia of the nervous system. It is closely related to nonribosomal peptide synthetases (NRPSs), which typically consist of at least an adenylation, a peptidyl carrier protein and a peptide bond forming condensation domain. Besides its role in cuticle formation, Ebony is in most glia of the brain thought to convert biogenic amines to β-alanyl conjugates.
View Article and Find Full Text PDFHuman guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of large GTPases (LGs). In the course of GTP hydrolysis, the protein undergoes structural changes leading to self-assembly of the protein, which is a characteristic property of all family members. For self-assembly, the protein employs two distinct interaction sites, one of which is located within the LG domain of the protein located at the N-terminus, and the second is located in the C-terminal alpha-helical domain.
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