Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 49, 2012, Pages 19971-19976

  Davies, Douglas R ^a   Gelinas, Amy D ^b   Zhang, Chi ^b   Rohloff, John C ^b   Carter, Jeffrey D ^b   O'Connell, Daniel ^b,c   Waugh, Sheela M ^b   Wolk, Steven K ^b   Mayfield, Wesley S ^b   Burgin, Alex B ^a   Edwards, Thomas E ^a   Stewart, Lance J ^a   Gold, Larry ^b   Janjic, Nebojsa ^b   Jarvis, Thale C ^b  

^a Emerald BioStructures Inc   (United States)

^b SomaLogic Inc   (United States)

^c St Andrews School   (United States)

Author keywords

Modified nucleotide; Pseudoknot; SELEX

Indexed keywords

APTAMER; PLATELET DERIVED GROWTH FACTOR BB;

ARTICLE; CRYSTAL STRUCTURE; DNA BINDING MOTIF; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN MODIFICATION; PROTEIN TARGETING;

AMINO ACID MOTIFS; APTAMERS, NUCLEOTIDE; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHOSPHORYLATION; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-SIS; SELEX APTAMER TECHNIQUE; SEQUENCE ANALYSIS, DNA; TRANSITION TEMPERATURE;

EID: 84870579370     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1213933109     Document Type: Article

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