ArticleBiochemical and biophysical research communications2020
Multi-domain unfolding of the Fab fragment of a humanized anti-cocaine mAb characterized by non-reducing SDS-PAGE.
Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- Isothermal titration calorimetry determination of thermodynamics of binding of cocaine and its metabolites to humanized h2E2 anti-cocaine mAb.Biochemistry and biophysics reports · 2022Article
- Tyrosine nitration of a humanized anti-cocaine mAb differentially affects ligand binding of cocaine and its metabolites.Biochemistry and biophysics reports · 2022Article
- Cocaine binding to the Fab fragment of a humanized anti-cocaine mAb quantitated by dye absorption and fluorescence spectroscopy.Journal of immunological methods · 2021Article
- Ligand binding to a humanized anti-cocaine mAb measured by dye absorption spectroscopy.Biochemical and biophysical research communications · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Monoclonal antibodies and their fragments are widely used for research and therapy. Fab fragments are useful since they retain antigen binding specificity, but being smaller proteins, are better able to penetrate biological compartments and tumors, and do not induce Fc-dependent immunological system activation. Our laboratory developed an anti-cocaine mAb (named h2E2) for the treatment of cocaine use disorders, which is currently in advanced pre-clinical development. We are also interested in the Fab fragment of this mAb for potential therapy of acute cocaine overdose. Previously, we showed that this mAb and its F(ab')
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Registered trials
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