Publications by authors named "M V Pellanda"
Article Synopsis
- The study examines three OST isoforms (STT3A, STT3B, and STT3C) to understand their glycan and polypeptide substrate specificities using genetic tools and glycoproteomics in yeast.
- Results show that STT3A has a broader acceptance of glycan structures, while STT3B needs more complex ones, and STT3C has no specific preference, with distinct regions of the protein influencing their substrate interactions.
Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel.
View Article and Find Full Text PDFThe proportion of peritoneal dialysis (PD) patients on automated peritoneal dialysis (APD) has been steadily increasing over the past decade. In the US, the percentage of PD patients on APD has steadily risen from 9% in 1993 to 54% in 2000. In continuous ambulatory peritoneal dialysis (CAPD), PD exchanges are performed manually, while in APD a mechanical device to assist the delivery and drainage of dialysate is employed.
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