ArticleStructure (London, England : 1993)2014
Molecular mechanism of antibody-mediated activation of β-galactosidase.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 26 citations in OpenAlex.
- Antibody-mediated enzyme formation: Its legacy at age fifty-four.Journal of molecular recognition : JMR · 2021Review
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- Sparseness and Smoothness Regularized Imaging for improving the resolution of Cryo-EM single-particle reconstruction.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Measuring the effects of particle orientation to improve the efficiency of electron cryomicroscopy.Nature communications · 2017Article
- High-resolution cryo-EM proteasome structures in drug development.Acta crystallographica. Section D, Structural biology · 2017Article
- The potential use of single-particle electron microscopy as a tool for structure-based inhibitor design.Acta crystallographica. Section D, Structural biology · 2017Article
- Membrane protein structures without crystals, by single particle electron cryomicroscopy.Current opinion in structural biology · 2015Review
- Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.Nature communications · 2015Article
- Seeing tobacco mosaic virus through direct electron detectors.Journal of structural biology · 2015Article
- Semi-automated selection of cryo-EM particles in RELION-1.3.Journal of structural biology · 2015Article
- The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.Biochimica et biophysica acta · 2015Article
- Comparison of optimal performance at 300keV of three direct electron detectors for use in low dose electron microscopy.Ultramicroscopy · 2014Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Binding of a single-chain Fv antibody to Escherichia coli β-galactosidase (β-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated enzyme formation mutants. To understand the nature of this activation, we have determined by electron cryo-microscopy the structure of the complex between β-gal and the antibody scFv13R4. Our structure localizes the scFv13R4 binding site to the crevice between domains 1 and 3 in each β-gal subunit. The mutations that scFv13R4 counteracts are located between the antibody binding site and the active site of β-gal, at one end of the TIM-barrel that forms domain 3 where the substrate lactose is hydrolyzed. The mode of binding suggests how scFv stabilizes both the active site of β-gal and the tetrameric state.
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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.