Results 211 to 220 of about 200,545 (260)
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EPITOPE TAGGING

Annual Review of Genetics, 1998
▪ Abstract  Epitope tagging is a recombinant DNA method by which a protein encoded by a cloned gene is made immunoreactive to a known antibody. This review discusses the major advantages and limitations of epitope tagging and describes a number of recent applications.
J W, Jarvik, C A, Telmer
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Non-Neutralizing Epitopes Shade Neutralizing Epitopes against Omicron in a Multiple Epitope-Based Vaccine

ACS Infectious Diseases, 2022
The ongoing coronavirus disease 2019 pandemic has raised concerns about the risk of re-infection. Non-neutralizing epitopes are one of the major reasons for antibody-dependent enhancement. Past studies on the ancestral severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have revealed an infectivity-enhancing site on the ancestral SARS-CoV-2 ...
Hua-Rui Gong   +5 more
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Epitope Mapping

Molecular Biotechnology, 1994
Monoclonal antibodies (MAbs) are specific immunological tools because they bind to a precise determinant (the epitope) on the surface of a protein. The procedure of identifying the binding site of a MAb is often termed "epitope mapping."
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Epitope Mapping

1998
Epitope mapping can be used to identify areas of a protein that an antibody recognizes and binds to. Monoclonal antibodies are easier to characterize, but epitope maps can also be produced for polyclonal antisera.
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Hypervariable epitope constructs as a means of accounting for epitope variability

Vaccine, 1994
Epitope variability is one of the greatest obstacles to development of synthetic peptide vaccines. Based on a recently described hypervariable epitope (aa 414-434) on the envelope glycoprotein (gp130) to simian immunodeficiency virus (SIVmac142), we have developed a novel approach to account for epitope variability.
D E, Anderson   +4 more
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An Overview of Epitopes and Methods for Antibody Epitope Mapping

Antibodies are protein molecules indispensable for many therapeutic, diagnostic, and research purposes due to their exquisite ability to selectively recognize and bind a given antigen. The particular area of the antigen recognized by the antibody is called the epitope, and mapping of such epitopes can provide important mechanistic insights and indicate
Johan, Nilvebrant   +3 more
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Predefined spacers between epitopes on a recombinant epitope-peptide impacted epitope-specific antibody response

Immunology Letters, 2005
We have developed a widely applicable method to construct epitope-peptide gene for epitope-vaccine strategy recently. In this study, we wanted to know whether the predefined spacers between epitopes on a recombinant epitope-peptide impacted the production of epitope-specific antibodies.
Zuqiang, Liu   +2 more
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Immunoglobulin Epitopes in Primates

Vox Sanguinis, 1979
Abstract. Non‐human primate sera were investigated for the presence of various human immunoglobulin epitopes including allotypes of ϰ‐, γ1‐, γ2‐, γ3‐ and α2‐chains, isotypes of ϰ‐, γ1‐, γ2‐, γ3‐, γ4‐, α1‐, α2‐ and μ‐chains and iso‐allotypes. The non‐human primate sera comprised representatives of several species of apes, Old World monkeys, New World ...
E, van Loghem, G, de Lange
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Distinct epitopes on amiloride

American Journal of Physiology-Cell Physiology, 1989
Most Na(+)-selective transport proteins are inhibited by the drug amiloride. Studies using amiloride analogues suggest that specific regions of amiloride might participate in binding to receptors on these transport proteins. To determine whether certain domains of this drug are recognized as distinct epitopes, amiloride was coupled to albumin through ...
T R, Kleyman   +4 more
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Epitopes on Rh Proteins

Vox Sanguinis, 2000
Analyses of the reactions of monoclonal anti‐D with Rh D variant red cells have shown that there are at least 24 different epitopes of the Rh D antigen. Similar studies Of Rh E variant red cells with monoclonal anti‐E indicate that there are at least 4 epitopes of the Rh E antigen.
M L, Scott   +4 more
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