Other Publications (1)
Articles by Carolyn Sinow in JoVE
A Step Beyond BRET: Fluorescens av Unbound Eksitasjon fra luminescens (drivstoff) Joseph Dragavon1, Carolyn Sinow2, Alexandra D. Holland1, Abdessalem Rekiki1, Ioanna Theodorou3, Chelsea Samson4, Samantha Blazquez1, Kelly L. Rogers5, Régis Tournebize1,6,7, Spencer L. Shorte1 1Plate-Forme d'Imagerie Dynamique, Imagopole, Institut Pasteur, 2Department of Radiation Oncology, Stanford School of Medicine, 3Service Hospitalier Frédéric Joliot, Institut d'Imagerie Biomédicale, 4Vanderbilt School of Medicine, 5The Walter & Eliza Hall Institute of Medical Research, 6Unité INSERM U786, Institut Pasteur, 7Unité de Pathogénie Microbienne Moléculaire, Institut Pasteur Utvide grunnlaget og anvendbarhet av fluorescens ved Unbound Eksitasjon fra luminescens (drivstoff) med å kartlegge de relevante prinsipper og demonstrere sin kompatibilitet med en rekke fluoroforene og antistoff-målrettet forhold.
Other articles by Carolyn Sinow on PubMed
Insulin-like Growth Factor II Peptide Fusion Enables Uptake and Lysosomal Delivery of α-N-acetylglucosaminidase to Mucopolysaccharidosis Type IIIB Fibroblasts The Biochemical Journal. Mar, 2014 | Pubmed ID: 24266751 Enzyme replacement therapy for MPS IIIB (mucopolysaccharidosis type IIIB; also known as Sanfilippo B syndrome) has been hindered by inadequate mannose 6 phosphorylation and cellular uptake of rhNAGLU (recombinant human α-N-acetylglucosaminidase). We expressed and characterized a modified rhNAGLU fused to the receptor-binding motif of IGF-II (insulin-like growth factor 2) (rhNAGLU-IGF-II) to enhance its ability to enter cells using the cation-independent mannose 6-phosphate receptor, which is also the receptor for IGF-II (at a different binding site). RhNAGLU-IGF-II was stably expressed in CHO (Chinese-hamster ovary) cells, secreted and purified to apparent homogeneity. The Km and pH optimum of the fusion enzyme was similar to those reported for rhNAGLU. Both intracellular uptake and confocal microscopy suggested that MPS IIIB fibroblasts readily take up the fusion enzyme via receptor-mediated endocytosis that was inhibited significantly (P