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Endosialidase NF appears to bind polySia DP5 in a helical conformation.
Chembiochem
December 2006
Institute for Glycomics, Griffith University (Gold Coast Campus), PMB 50 Gold Coast Mail Centre, Queensland 9726, Australia.
The genome of bacteriophage K1F, a T7-like phage that has acquired the ability to replicate on K1 strains of Escherichia coli.
J Bacteriol
December 2005
National Institutes of Mental Health, National Institutes of Health, Building 49, Room B1B20, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Bacteriophage K1F specifically infects Escherichia coli strains that produce the K1 polysaccharide capsule. Like several other K1 capsule-specific phages, K1F encodes an endo-neuraminidase (endosialidase) that is part of the tail structure which allows the phage to recognize and degrade the polysaccharide capsule. The complete nucleotide sequence of the K1F genome reveals that it is closely related to bacteriophage T7 in both genome organization and sequence similarity.
View Article and Find Full Text PDFEvidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization.
Eur J Biochem
April 1998
Research Institute, The Hospital for Sick Children, Department of Biochemistry, University of Toronto, Ontario, Canada.
We have investigated the possibility that the intestinal mucin rat Muc2 forms dimers during biosynthesis via intermolecular disulphide bridging of its C-terminal domains. Since the cysteine alignment of RMuc2 (and other secretory mucins) is similar to that of human von Willebrand factor, a similar C-tail to C-tail dimerization may occur in mucins. The C-terminal domain of RMuc2 (534 amino acids) was expressed in COS-1 cells, and the products monitored by SDS/PAGE and western blotting with three antibodies to different regions of the C-terminal domain.
View Article and Find Full Text PDFCellular site of synthesis and dynamics of cell surface re-expression of polysialic acid of the neural cell adhesion molecule.
Eur J Biochem
November 1994
Department of Pathology, University of Zürich, Switzerland.
Homopolymers of alpha-2,8-ketosidically linked sialic acid (polysialic acid) represent a posttranslational modification which, in mammals, appears to be unique for the neural cell adhesion molecule and the alpha subunit of sodium channels in brain. Under steady-state conditions, polysialic acid is detectable in the plasma membrane of different cell types but not in the cytoplasm. We have studied the site of synthesis and the cell surface re-expression of polysialic acid in a clonal subline of small cell lung carcinoma using the monoclonal antibody 735 and bacteriophage endosialidase, both specific reagents for polysialic acid.
View Article and Find Full Text PDFDevelopmental expression of trout egg polysialoglycoproteins and the prerequisite alpha 2,6-, and alpha 2,8-sialyl and alpha 2,8-polysialyltransferase activities required for their synthesis during oogenesis.
J Biol Chem
April 1994
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
The developmental expression of the alpha 2,6- and alpha 2,8-linked sialic acid (Sia) residues in trout egg polysialoglycoproteins (PSGPs) was studied by correlating the temporal expression of these sugar residues, and the prerequisite sialyltransferases responsible for their synthesis, during oogenesis. The following new findings are reported. 1) Disialylated glycoproteins were identified in ovaries 4-6 months prior to ovulation.
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