222725-68-0Relevant academic research and scientific papers
Bis 2′-5′-RR-(3′F-A)(3′F-A) cyclic dinucleotide compound and uses thereof
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, (2021/04/14)
The present invention provides the cyclic dinucleotide compound 2′2′-RR-(3′F-A)(3′F-A) as a highly active immune stimulator that activates DCs via the cytoplasmic receptor known as STING (Stimulator of Interferon Genes), and compositions and uses thereof.
DC-SIGN ANTIBODY CONJUGATES COMPRISING STING AGONISTS
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, (2020/05/29)
Provided herein are immunoconjugates comprising an anti-DC-SiGN antibody conjugated to a STING agonist. Also disclosed are methods of making the immunoconjugates and methods of treating cancer using the immunoconjugates.
LOCKED NUCLEIC ACID CYCLIC DINUCLEOTIDE COMPOUNDS AND USES THEREOF
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Paragraph 0548; 0553-0554, (2019/07/03)
The present invention provides highly active locked nucleic acid cyclic-dinucleotide (LNA-CDN) immune stimulators that activate DCs via the cytoplasmic receptor known as STING (Stimulator of Interferon Genes). In particular, the LNA-CDNs of the present in
COMPOSITIONS AND METHODS FOR ACTIVATING "STIMULATOR OF INTERFERON GENE"-DEPENDENT SIGNALLING
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, (2017/05/17)
The present invention provides highly active cyclic-di-nucleotide (CDN) immune stimulators that activate DCs via a recently discovered cytoplasmic receptor known as STING (Stimulator of Interferon Genes). In particular, the CDNs of the present invention are provided in the form of a composition comprising one or more cyclic purine dinucleotides induce human STING-dependent type I interferon production, wherein the cyclic purine dinuclotides present in the composition are 2'- or 3'-mono-fluoro substituted, or 2'3'-di-fluoro substituted mixed linkage 2',5' - 3',5' CDNs.
Nuclease resistant hammerhead motif: From '5-ribo' to '3-ribo' model
Matulic-Adamic, Jasenka,Daniher, Andrew T.,Gonzalez, Carolyn,Beigelman, Leonid
, p. 157 - 160 (2007/10/03)
Previously developed '5-ribo' nuclease stabilized hammerhead motif was further refined by systematic incorporation of 1-(β-D-xylofuranosyl) adenine (xA) and 1-(β-D-xylofuranosyl) guanine (xG) in the place of conserved ribopurine residues of the catalytic core. Modified ribozymes substituted with xA at positions A15.1 and A6 demonstrated catalytic activity close to the parent stabilized ribozyme. Analogous guanosine substitutions at positions G5, G8 and G12 substantially lowered catalytic rates.
