Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets
Journal Article
Overview
publication date
- December 4, 2012
has subject area
- Aptamers, Nucleotide
- Biochemical Phenomena - Molecular Structure
- Biochemical Phenomena - Phosphorylation
- Biochemical Phenomena - Protein Binding
- Biological Factors - Becaplermin
- Biological Factors - Proto-Oncogene Proteins c-sis
- Blood Proteins - Proto-Oncogene Proteins c-sis
- Chemical Phenomena - Molecular Structure
- Crystallography, X-Ray
- DNA-Binding Proteins - Becaplermin
- DNA-Binding Proteins - Proto-Oncogene Proteins c-sis
- Hydrophobic and Hydrophilic Interactions
- Investigative Techniques - SELEX Aptamer Technique
- Laboratory Chemicals - DNA Primers
- Metabolism - Phosphorylation
- Metabolism - Protein Binding
- Models, Molecular
- Molecular Sequence Data
- Oligodeoxyribonucleotides - DNA Primers
- Organic Chemistry Phenomena - Phosphorylation
- Peptides - Becaplermin
- Peptides - Proto-Oncogene Proteins c-sis
- Protein Structural Elements - Amino Acid Motifs
- Protein Structure, Secondary - Amino Acid Motifs
- Proteins - Becaplermin
- Proteins - Proto-Oncogene Proteins c-sis
- Proto-Oncogene Proteins - Proto-Oncogene Proteins c-sis
- Sequence Analysis, DNA
- Technology - SELEX Aptamer Technique
- Transition Temperature
has restriction
- green
Date in CU Experts
- September 9, 2013 10:30 AM
Full Author List
- Davies DR; Gelinas AD; Zhang C; Rohloff JC; Carter JD; O'Connell D; Waugh SM; Wolk SK; Mayfield WS; Burgin AB
author count
- 15
citation count
- 178
published in
Other Profiles
International Standard Serial Number (ISSN)
- 0027-8424
Digital Object Identifier (DOI)
Additional Document Info
start page
- 19971
end page
- 19976
volume
- 109
issue
- 49