C
C. Subasinghe
Researcher at Georgetown University Medical Center
Publications - 10
Citations - 2333
C. Subasinghe is an academic researcher from Georgetown University Medical Center. The author has contributed to research in topics: Oligonucleotide & Cell culture. The author has an hindex of 9, co-authored 10 publications receiving 2312 citations.
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Journal ArticleDOI
Characterization of oligonucleotide transport into living cells
S.L. Loke,Cy A. Stein,X. H. Zhang,K. Mori,M Nakanishi,C. Subasinghe,Jack S. Cohen,L.M. Neckers +7 more
TL;DR: This work has investigated the mechanism by which oligonucleotides enter living cells and identified an 80-kDa surface protein that may mediate transport.
Journal ArticleDOI
Physicochemical properties of phosphorothioate oligodeoxynucleotides.
TL;DR: The syntheses, melting temperatures, and nuclease susceptibilities of a series of phosphorothioate ODN analogs are reported, providing a rational basis for the S-dC/G sequences as potential effective anti-AIDS agents.
Journal Article
Antisense-mediated Inhibition of BCL2 Protooncogene Expression and Leukemic Cell Growth and Survival: Comparisons of Phosphodiester and Phosphorothioate Oligodeoxynucleotides
TL;DR: Data indicate that PO and PS oligodeoxynucleotides targeted against the human BCL2 protooncogene can be sequence-specific inhibitors of leukemic cell growth and survival.
Journal ArticleDOI
Comparative inhibition of rabbit globin mRNA translation by modified antisense oligodeoxynucleotides
Christian Cazenave,C. A. Stein,N. Loreau,Nguyen Thanh Thuong,L.M. Neckers,C. Subasinghe,Claude Hélène,Jack S. Cohen,Jean-Jacques Toulmé +8 more
TL;DR: Phosphorothioate oligodeoxyribonucleotides were shown to be non-specific inhibitors of protein translation, at concentrations in the micromolar range, in both cell-free systems and oocytes.
Journal ArticleDOI
Phosphorothioate and normal oligodeoxyribonucleotides with 5'-linked acridine: characterization and preliminary kinetics of cellular uptake.
TL;DR: Reports of melting temperatures (Tm) of a series of S-oligos compared with those of the corresponding normal oligomers and the uptake of these fluorescently labeled oligos into HL60 cells suggest an energy-dependent process, and a possible membrane receptor for oligos.