AbstractWe report that, contrary to common belief, polypeptides fused to the carboxy-terminus of the M13 gene-3 minor coat protein are functionally displayed on the phage surface. In a phagemid display system, carboxy-terminal fusion through optimized linker sequences resulted in display levels comparable to those achieved with conventional amino-terminal fusions. These findings are of considerable importance to phage display technology because they enable investigations not suited to amino-terminal display, including the study of protein–protein interactions requiring free carboxy-termini, functional cDNA cloning efforts, and the display of intracellular proteins
We have reported variants of the M13 bacteriophage major coat protein (P8) that enable high copy dis...
BACKGROUND: Phage display is a platform for selection of specific binding molecules and this is a cl...
Bacteriophage display systems have been developed to allow the selection of a protein or peptide bas...
AbstractWe report that, contrary to common belief, polypeptides fused to the carboxy-terminus of the...
The process of phage display utilizes manipulation of the bacteriophage genome to facilitate the pre...
M13 bacteriophage display presents polypeptides as fusions to phage coat proteins. Such phage-displa...
Phage display of proteins continues to be an important technology with a variety of applications. In...
Phage display is a platform for selection of specific binding molecules and this is a clear-cut moti...
M13 bacteriophage has been widely used as a display platform for a variety of peptides. This display...
Using the phage display technology, a protein can be displayed at the surface of bacteriophages as a...
We exploit bacterial sortases to attach a variety of moieties to the capsid proteins of M13 bacterio...
Background: Phage display is a leading technology for selection of binders with affinity for specifi...
Numerous examples of phage display applied to soluble proteins demonstrate the power of the techniqu...
Here we describe a phage vector for the display of single chain antibodies and polypeptides on the s...
We have reported variants of the M13 bacteriophage major coat protein ~P8! that enable high copy dis...
We have reported variants of the M13 bacteriophage major coat protein (P8) that enable high copy dis...
BACKGROUND: Phage display is a platform for selection of specific binding molecules and this is a cl...
Bacteriophage display systems have been developed to allow the selection of a protein or peptide bas...
AbstractWe report that, contrary to common belief, polypeptides fused to the carboxy-terminus of the...
The process of phage display utilizes manipulation of the bacteriophage genome to facilitate the pre...
M13 bacteriophage display presents polypeptides as fusions to phage coat proteins. Such phage-displa...
Phage display of proteins continues to be an important technology with a variety of applications. In...
Phage display is a platform for selection of specific binding molecules and this is a clear-cut moti...
M13 bacteriophage has been widely used as a display platform for a variety of peptides. This display...
Using the phage display technology, a protein can be displayed at the surface of bacteriophages as a...
We exploit bacterial sortases to attach a variety of moieties to the capsid proteins of M13 bacterio...
Background: Phage display is a leading technology for selection of binders with affinity for specifi...
Numerous examples of phage display applied to soluble proteins demonstrate the power of the techniqu...
Here we describe a phage vector for the display of single chain antibodies and polypeptides on the s...
We have reported variants of the M13 bacteriophage major coat protein ~P8! that enable high copy dis...
We have reported variants of the M13 bacteriophage major coat protein (P8) that enable high copy dis...
BACKGROUND: Phage display is a platform for selection of specific binding molecules and this is a cl...
Bacteriophage display systems have been developed to allow the selection of a protein or peptide bas...