[HTML][HTML] A computational tool to predict the evolutionarily conserved protein–protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - FEBS letters, 2014 - Elsevier
Identifying hot-spot residues–residues that are critical to protein–protein binding–can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …
A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - 2013 - dspace.mit.edu
Identifying hot-spot residues–residues that are critical to protein–protein binding–can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …
[PDF][PDF] A computational tool to predict the evolutionarily conserved protein–protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - FEBS Letters, 2014 - core.ac.uk
abstract Identifying hot-spot residues–residues that are critical to protein–protein binding–
can help to elucidate a protein's function and assist in designing therapeutic molecules to …
can help to elucidate a protein's function and assist in designing therapeutic molecules to …
A computational tool to predict the evolutionarily conserved protein–protein interaction hot‐spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - FEBS Letters, 2014 - Wiley Online Library
Identifying hot‐spot residues–residues that are critical to protein–protein binding–can help
to elucidate a protein's function and assist in designing therapeutic molecules to target those …
to elucidate a protein's function and assist in designing therapeutic molecules to target those …
A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - FEBS letters, 2014 - pubmed.ncbi.nlm.nih.gov
Identifying hot-spot residues-residues that are critical to protein-protein binding-can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …
A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein.
NJ Agrawal, B Helk, BL Trout - FEBS Letters, 2013 - europepmc.org
Identifying hot-spot residues-residues that are critical to protein-protein binding-can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …
A computational tool to predict the evolutionarily conserved protein–protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - FEBS Letters, 2014 - ui.adsabs.harvard.edu
Identifying hot-spot residues–residues that are critical to protein–protein binding–can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …
[PDF][PDF] A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein
NJ Agrawal, B Helk, BL Trout - core.ac.uk
Identifying hot-spot residues-residues that are critical to protein-protein binding-can help to
elucidate a protein's function and assist in designing therapeutic molecules to target those …
elucidate a protein's function and assist in designing therapeutic molecules to target those …