Phage display for selection of novel binding peptides.

By Sachdev S. Sidhu, Henry B. Lowman, B. Cunningham, James A. Wells. 2000

420 citations recorded by the source corpus.

Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. O. Schueler‐Furman
2. Barak Raveh
3. Nir London
4. Lior Zimmerman
5. J. Wells
6. Christopher L. McClendon
7. Jeffrey J. Gray
8. Björn Wallner

In Radiology, Nuclear Medicine and Imaging

1. O. Schueler‐Furman
2. Paramjit S. Arora
3. Andrea L. Jochim

Citations in the corpus

• Reaching for high-hanging fruit in drug discovery at protein–protein interfaces (2007, background): “Moreover, peptides selected for binding to one of the partners in a protein–protein pair (by using phage display) often compete with the natural protein partner for binding to the hotspo”
• Rosetta FlexPepDock ab-initio: Simultaneous Folding, Docking and Refinement of Peptides onto Their Receptors (2011, background): “However, the number of available models solved in experiment represents only a small fraction of known peptideprotein interactions, while high-throughput methods for screening of peptide libraries such as peptide arrays [19] combinatorial phagedisplay [20,21,22] and yeast surface display [23,24,25] ”