Article Abstract:
Neurexin IV (NRX IV) has recently been isolated in Drosophila and classified as a new member of the neurexin family of cell surface proteins that are thought to be involved in cellular interactions and target recognition. NRX IV has been determined to mediate cell-cell interaction by providing a link between the extracellular environment and the intracellular components of septate junctions. NRX IV has also been found to exhibit significant amino acid sequence homology with human and rat Caspr, indicating that NRX IV is the Drosophila counterpart of Caspr. The observed structural similarity between NRX IV and Caspr also implies a conserved mechanism for cellular interactions.
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Article Abstract:
A study was undertaken to evaluate the DNA binding properties of the BV1 and BC1 proteins of the bean dwarf mosaic geminivirus to correlate them to the maintenance of the viral genome size during systemic infection. BV1 and BC1 are considered as movement proteins since the former moves viral DNA out of the nucleus and the latter influences DNA transport through plasmodesmata. Results revealed that the two proteins were capable of recognizing DNA on the basis of genome size and form and manifested protein-nucleic acid interaction.
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Article Abstract:
The binding of proteoglycans to growth factors induces a regulatory role on the growth factors. The binding of the proteoglycan, heparin, to the fibroblast growth factor (FGF) is necessary for FGF-induced biological activity. Proteoglycans are proteins containing carbohydrates and are low affinity receptors. The binding of the low affinity receptors appears to be necessary for reducing the dimensionality of ligand binding from three to two dimensions.
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