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Richard I. Near
Researcher at Boston Medical Center
Publications - 41
Citations - 1613
Richard I. Near is an academic researcher from Boston Medical Center. The author has contributed to research in topics: Antibody & BCAR3. The author has an hindex of 23, co-authored 40 publications receiving 1576 citations. Previous affiliations of Richard I. Near include Massachusetts Institute of Technology & University of Washington.
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Journal ArticleDOI
Expression of a hybrid immunoglobulin-T cell receptor protein in transgenic mice.
Michael L.B. Becker,Richard I. Near,Meredith Mudgett-Hunter,Michael N. Margolies,Ralph T. Kubo,Jonathan Kaye,Stephen M. Hedrick +6 more
TL;DR: It is shown that the hybrid VDJH-C alpha protein forms part of a functional TCR complex by the criteria of coprecipitation and comodulation of CD3 and TCR beta chain components and T cell activation with anti-idiotypic antibodies or digoxin.
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Expression of the aryl hydrocarbon receptor/transcription factor (AhR) and AhR-regulated CYP1
Anthony F. Trombino,Richard I. Near,Raymond A. Matulka,Shi Yang,Laurie J. Hafer,Paul Toselli,Dong W. Kim,Adrianne E. Rogers,Gail E. Sonenshein,David H. Sherr +9 more
TL;DR: It is implied that AhR and CYP1B1 hyper-expression represent molecular biomarkers for, at least, PAH-induced mammary cell transformation, and mechanisms through which the AhR may contribute to carcinogenesis well after exogenous AhR ligands have been eliminated are suggested.
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The molecular evolution of the immune response
TL;DR: In this article Tim Manser and his colleagues seek to explain how genetically identical individuals generate widely diverse immune responses to the same antigen and some antigens reproducibly elicit similar immune responses (recurrent idiotypes) in all individuals.
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Efficient Production of a Functional Single-Chain Antidigoxin Antibody via an Engineered Bacillus subtilis Expression-Secretion System
TL;DR: N-terminal sequence determination indicated that the protein has the expected N-terminus with the signal peptide properly processed, and Affinity and ligand specificity studies demonstrated that the engineered antidigoxin SCA has almost identical properties as those of the parental monoclonal antibody.
Journal ArticleDOI
Modulation of antibody affinity by a non‐contact residue
J. F. Schillbach,Richard I. Near,Robert E. Bruccoleri,Edgar Haber,Philip D. Jeffrey,Jiri Novotny,Steven Sheriff,Michael N. Margolies +7 more
TL;DR: The mutagenesis and modeling results suggest that even conservative replacements of non‐contact residues can alter affinity indirectly through their impact on contact residue placement.