Zobrazeno 1 - 10
of 35
pro vyhledávání: '"E A, Padlan"'
Publikováno v:
The Journal of Immunology. 153:1161-1170
We are studying murine mAbs against two carbohydrate epitopes, 3-fucosyllactosamine (Le(x), CD15) and galactosylgloboside. The VH domains of both panels of Ab are encoded by VH441, a member of the X24 family of Ig genes. To evaluate the contribution
Publikováno v:
Scopus-Elsevier
The Journal of Experimental Medicine
The Journal of Experimental Medicine
To gain insight into the rules that govern the binding of endogenous and viral peptides to a given major histocompatibility complex (MHC) class I molecule, we characterized the amino acid sequences of a set of self peptides bound by a soluble analogu
Publikováno v:
The Journal of Immunology. 144:2620-2626
The reactivity of 23 mouse monoclonal Ig with a rabbit polyclonal antiserum to VH of anti-alpha(1----6)dextran 19.22.1 and with a monoclonal anti-VH of anti-DNP MOPC315, when correlated with amino acid sequence, identified several residues in the fir
Generation and characterization of a single gene-encoded single-chain-tetravalent antitumor antibody
Publikováno v:
Clinical cancer research : an official journal of the American Association for Cancer Research. 5
Monoclonal antibody (mAb) CC49, a murine IgG1, reacts with the tumor-associated glycoprotein-72 expressed on a variety of carcinomas. In clinical trials, radiolabeled CC49 has shown excellent tumor localization to a variety of carcinomas. To minimize
Publikováno v:
Journal of molecular biology. 289(5)
We describe here the structure of a murine T cell receptor (TCR) Valpha2.6Jalpha38 (TCRAV2S6J38) domain, derived from a T cell hybridoma with specificity for the H-2Ddmajor histocompatibility complex class I molecule bound to a decamer peptide, P18-I
Publikováno v:
Allergy. 53
Autor:
A D, Santos, E A, Padlan
Publikováno v:
Progress in nucleic acid research and molecular biology. 60
Two procedures for improving the efficacy of medically important antibodies are described. The first procedure is designed to reduce the immunogenicity of nonhuman antibodies to the barest minimum--the "humanization" is accomplished by transplanting
Publikováno v:
The Journal of biological chemistry. 271(21)
The three-dimensional structure of the Fab of TR1.9, a high-affinity IgG1, kappa human autoantibody to thyroid peroxidase, was determined crystallographically to a resolution of 2.0 A. The combining site was found to be relatively flat, like other an
Publikováno v:
Human antibodies and hybridomas. 7(3)
A murine monoclonal antibody H67 was characterized for the binding specificity, which showed that H67 recognizes a disulfide-bond-dependent conformational epitope of common a antigenic determinant on the hepatitis B surface antigen. The result sugges
Autor:
E A, Padlan
Publikováno v:
Advances in protein chemistry. 49