V
Viswanathan Shankar
Researcher at University of Oklahoma Health Sciences Center
Publications - 12
Citations - 807
Viswanathan Shankar is an academic researcher from University of Oklahoma Health Sciences Center. The author has contributed to research in topics: Mucin & Complementary DNA. The author has an hindex of 7, co-authored 12 publications receiving 785 citations. Previous affiliations of Viswanathan Shankar include University of Oklahoma.
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Infection-Derived Enterococcus faecalis Strains Are Enriched in esp, a Gene Encoding a Novel Surface Protein
TL;DR: The deduced primary structure of the Esp protein from strain MMH594, inferred to be 1,873 amino acids with a predicted mass of ∼202 kDa, reveals a core region consisting of repeat units that make up 50% of the protein, which bears global organizational similarity to the Rib and C alpha proteins of group B streptococci.
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Chromosomal Localization of a Human Mucin Gene (MUC8) and Cloning of the cDNA Corresponding to the Carboxy Terminus
Viswanathan Shankar,Prabhasankar Pichan,Roger L. Eddy,Vijay Tonk,Norma J. Nowak,Sheila N.J. Sait,Thomas B. Shows,Roger E. Schultz,Garrett Gotway,Ronald C. Elkins,Michael S. Gilmore,Goverdhan P. Sachdev +11 more
TL;DR: An additional new sequence derived by 3'-rapid amplification of cDNA ends technique represents the extreme carboxy terminus of MUC8, a major airway mucin glycoprotein with novel tandem repetitive sequence that was mapped to chromosome 12 using DNA from a panel of human-mouse somatic cell hybrids.
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A novel human airway mucin cDNA encodes a protein with unique tandem-repeat organization.
TL;DR: The data indicate that mucin encoded by clone pAM1 represents a unique type of peptide organization which has not been described in mucin cDNAs reported thus far.
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Evidence of hydrophobic domains in human respiratory mucins. Effect of sodium chloride on hydrophobic binding properties.
TL;DR: Hydrophobic binding properties of purified human respiratory mucins were studied by the fluorescence probe technique using mansylphenylalanine (Mns-Phe) as the fluorescent probe, showing that the binding sites are on the nonglycosylated, Pronase-sensitive portion of the mucin molecules.
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Macromolecular properties and polymeric structure of canine tracheal mucins.
TL;DR: Two high-Mr mucus glycoproteins (mucins), C TM-A and CTM-B, were highly purified from canine tracheal pouch secretions, and their macromolecular properties as well as polymeric structure were investigated.