ArticleJournal of molecular biology2011
Site-specific coupling and sterically controlled formation of multimeric antibody fab fragments with unnatural amino acids.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 70 citations in OpenAlex.
- Efficiency landscape of bioorthogonal click reactions producing bispecific antibody conjugates.Cell reports methods · 2026Article
- Noncanonical amino acid-aided synthesis of anti-PD-L1 bispecific nanobody for colon cancer immunotherapy.Communications biology · 2025Article
- Methods for Conjugating Antibodies with Quantum Dots.Molecules (Basel, Switzerland) · 2025Review
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023Review
- Bioorthogonal PEGylation Prolongs the Elimination Half-Life of N-TIMP2 While Retaining MMP Inhibition.Bioconjugate chemistry · 2022Article
- Article
- An overview of chemo- and site-selectivity aspects in the chemical conjugation of proteins.Royal Society open science · 2022Article
- Palladium-Protein Oxidative Addition Complexes by Amine-Selective Acylation.Journal of the American Chemical Society · 2020Article
- Mutually Orthogonal Nonsense-Suppression Systems and Conjugation Chemistries for Precise Protein Labeling at up to Three Distinct Sites.Journal of the American Chemical Society · 2019Article
- Active Targeting of Cancer Cells by Nanobody Decorated Polypeptide Micelle with Bio-orthogonally Conjugated Drug.Nano letters · 2019Article
- Playing with the Molecules of Life.ACS chemical biology · 2018Review
- A Chemoselective Rapid Azo-Coupling Reaction (CRACR) for Unclickable Bioconjugation.Journal of the American Chemical Society · 2017Article
- Improving theranostics in pancreatic cancer.Journal of surgical oncology · 2017Review
- Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex.Scientific reports · 2016Article
- Synthesis and incorporation of a caged tyrosine amino acid possessing a bioorthogonal handle.Tetrahedron letters · 2016Article
- Site-Specifically Labeled Immunoconjugates for Molecular Imaging--Part 2: Peptide Tags and Unnatural Amino Acids.Molecular imaging and biology · 2016Review
- Fc-Small Molecule Antibody Mimetics.Bioconjugate chemistry · 2015Article
- Bacterial secretion of soluble and functional trivalent scFv-based N-terminal trimerbodies.AMB Express · 2015Article
- Synthesis and Incorporation of Unnatural Amino Acids To Probe and Optimize Protein Bioconjugations.Bioconjugate chemistry · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Immunoconjugates and multispecific antibodies are rapidly emerging as highly potent experimental therapeutics against cancer. We have developed a method to incorporate an unnatural amino acid, p-acetylphenylalanine (pAcPhe) into an antibody antigen binding fragment (Fab) targeting HER2 (human epidermal growth factor receptor 2), allowing site-specific labeling without disrupting antigen binding. Expression levels of the pAcPhe-containing proteins were comparable to that of wild-type protein in shake-flask and fermentation preparations. The pAcPhe-Fabs were labeled by reaction with hydroxylamine dye and biotin species to produce well-defined, singly conjugated Fabs. We then coupled a hydroxylamine biotin to the pAcPhe-Fab and demonstrated controlled assembly of Fabs in the presence of the tetrameric biotin-binding protein, NeutrAvidin. The position of Fab biotinylation dictates the geometry of multimer assembly, producing unique multimeric Fab structures. These assembled Fab multimers differentially attenuate Her2 phosphorylation in breast cancer cells that overexpress the Her2 receptor. Thus, an encoded unnatural amino acid produces a chemical "handle" by which immunoconjugates and multimers can be engineered.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.