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Robert Charles Ladner

Bio: Robert Charles Ladner is an academic researcher. The author has contributed to research in topics: Recombinant DNA & Binding selectivity. The author has an hindex of 5, co-authored 10 publications receiving 3791 citations.

Papers
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Patent
02 Sep 1987
TL;DR: In this article, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.
Abstract: The invention pertains to a single polypeptide chain binding molecule which has binding specificity and affinity substantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an antibody, to genetic sequences coding therefor, and to recombinant DNA methods of producing such molecule and uses for such molecule.

3,290 citations

Patent
01 Apr 1993
TL;DR: In this paper, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.
Abstract: The invention pertains to a single polypeptide chain binding molecule which has binding specificity and affinity substantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an antibody, to genetic sequences coding therefor, and to recombinant DNA methods of producing such molecule and uses for such molecule.

262 citations

Patent
02 Mar 1988
TL;DR: In this paper, a genetically engineered organism displaying the expression product of an inserted gene on its outer surface was presented, in a preferred embodiment, a single chain antibody was displayed on the outer surface of the genetically engineered microorganism.
Abstract: This invention comprises a genetically engineered organism displaying the expression product of an inserted gene on its outer surface. In a preferred embodiment, a single chain antibody is displayed on the outer surface of the genetically engineered microorganism.

154 citations

Patent
06 Jun 1995
TL;DR: In this article, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.
Abstract: The invention pertains to a single polypeptide chain binding molecule which has binding specificity and affinity substantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an antibody, to genetic sequences coding therefor, and to recombinant DNA methods of producing such molecule and uses for such molecule.

78 citations

Patent
02 Mar 1988
TL;DR: In this article, a genetically engineered organism displaying the expression product of an inserted gene on its outer surface was presented, in a preferred embodiment, a single chain antibody was displayed on the outer surface of the genetically engineered microorganism.
Abstract: This invention comprises a genetically engineered organism displaying the expression product of an inserted gene on its outer surface. In a preferred embodiment, a single chain antibody is displayed on the outer surface of the genetically engineered microorganism.

5 citations


Cited by
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Patent
02 Sep 1987
TL;DR: In this article, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.
Abstract: The invention pertains to a single polypeptide chain binding molecule which has binding specificity and affinity substantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an antibody, to genetic sequences coding therefor, and to recombinant DNA methods of producing such molecule and uses for such molecule.

3,290 citations

Patent
29 Jun 2001
TL;DR: In this article, a structural signal called for the display of the protein on the outer surface of a chosen bacterial cell, bacterial spore or phage (genetic package) is introduced into a genetic package.
Abstract: In order to obtain a novel binding protein against a chosen target, DNA molecules, each encoding a protein comprising one of a family of similar potential binding domains and a structural signal calling for the display of the protein on the outer surface of a chosen bacterial cell, bacterial spore or phage (genetic package) are introduced into a genetic package. The protein is expressed and the potential binding domain is displayed on the outer surface of the package. The cells or viruses bearing the binding domains which recognize the target molecule are isolated and amplified. The successful binding domains are then characterized. One or more of these successful binding domains is used as a model for the design of a new family of potential binding domains, and the process is repeated until a novel binding domain having a desired affinity for the target molecule is obtained. In one embodiment, the first family of potential binding domains is related to bovine pancreatic trypsin inhibitor, the genetic package is M13 phage, and the protein includes the outer surface transport signal of the M13 gene III protein.

3,093 citations

Patent
10 Jul 1991
TL;DR: In this paper, a member of a specific binding pair (sbp) is identified by expressing DNA encoding a genetically diverse population of such sbp members in recombinant host cells in which the sbps members are displayed in functional form at the surface of a secreted recombinant genetic display package (rgdp) containing DNA encoding the sbp member or a polypeptide component thereof.
Abstract: A member of a specific binding pair (sbp) is identified by expressing DNA encoding a genetically diverse population of such sbp members in recombinant host cells in which the sbp members are displayed in functional form at the surface of a secreted recombinant genetic display package (rgdp) containing DNA encoding the sbp member or a polypeptide component thereof, by virtue of the sbp member or a polypeptide component thereof being expressed as a fusion with a capsid component of the rgdp. The displayed sbps may be selected by affinity with a complementary sbp member, and the DNA recovered from selected rgdps for expression of the selected sbp members. Antibody sbp members may be thus obtained, with the different chains thereof expressed, one fused to the capsid component and the other in free form for association with the fusion partner polypeptide. A phagemid may be used as an expression vector, with said capsid fusion helping to package the phagemid DNA. Using this method libraries of DNA encoding respective chains of such multimeric sbp members may be combined, thereby obtaining a much greater genetic diversity in the sbp members than could easily be obtained by conventional methods.

2,740 citations

PatentDOI
28 Mar 1994-Science
TL;DR: In this article, a computer-assisted method for identifying protein sequences that fold into a known 3D structure was proposed, based on three key features of each residue's environment within the structure: (1) the total area of the residue's side-chain that is buried by other protein atoms, inaccessible to solvent; (2) the fraction of the side-chains area that is covered by polar atoms (O, N) or water; and (3) the local secondary structure.
Abstract: A computer-assisted method for identifying protein sequences that fold into a known three-dimensional structure. The method determines three key features of each residue's environment within the structure: (1) the total area of the residue's side-chain that is buried by other protein atoms, inaccessible to solvent; (2) the fraction of the side-chain area that is covered by polar atoms (O, N) or water, and (3) the local secondary structure. Based on these parameters, each residue position is categorized into an environment class. In this manner, a three-dimensional protein structure is converted into a one-dimensional environment string. A 3D structure profile table is then created containing score values that represent the frequency of finding any of the 20 common amino acids structures at each position of the environment string. These frequencies are determined from a database of known protein structures and aligned sequences.

2,530 citations

Patent
23 Sep 1992
TL;DR: In this paper, the authors describe methods for the production of antibodies, or antibody fragments, which have the same binding specificity as a parent antibody, but which have increased human characteristics.
Abstract: Methods are disclosed which may be used for the production of antibodies, or antibody fragments, which have the same binding specificity as a parent antibody but which have increased human characteristics. Humanised antibodies may be obtained by chain shuffling, perhaps using phage display technology. In one embodiment, a polypeptide comprising a heavy or light chain variable domain of a non-human antibody specific for an antigen of interest is combined with a repertoire of human complementary (light or heavy) chain variable domains. Hybrid pairings which are specific for the antigen of interest are selected. Human chains from the selected pairings may then be combined with a repertoire of human complementary variable domains (heavy or light) and humanised antibody polypeptide dimers can then be selected for binding specificity for antigen. The methods may be combined with CDR-imprinting. In another embodiment, component part of an antigen-binding site of a non-human antibody known to bind a particular antigen is combined with a repertoire of component parts of an antigen-binding site of human antibody, forming a library of antibody polypeptide dimers with antigen-binding sites. Hybrids selected from this library may be used in a second humanising shuffling step, or may already be of sufficient human character to be of value, perhaps after some modification to increase human character still further.

2,228 citations