ArticleThe Journal of biological chemistry2009
High resolution NMR-based model for the structure of a scFv-IL-1beta complex: potential for NMR as a key tool in therapeutic antibody design and development.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
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- Dimeric Ankyrin with Inverted Module Promotes Bifunctional Property in Capturing Capsid to Impede HIV-1 Replication.International journal of molecular sciences · 2023Article
- Chemical Diversification of Simple Synthetic Antibodies.ACS chemical biology · 2021Article
- Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein.PLoS pathogens · 2020Article
- VProteins · 2020Article
- Discrete analysis of camelid variable domains: sequences, structures, and in-silico structure prediction.PeerJ · 2020Article
- Article
- Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition.Structure (London, England : 1993) · 2018Article
- Anti-ROR1 scFv-EndoG as a Novel Anti-Cancer Therapeutic DrugAsian Pacific journal of cancer prevention : APJCP · 2018Article
- Production of Single-Chain Fv Antibodies Specific for GA-Pyridine, an Advanced Glycation End-Product (AGE), with Reduced Inter-Domain Motion.Molecules (Basel, Switzerland) · 2017Article
- The intervening removable affinity tag (iRAT) production system facilitates Fv antibody fragment-mediated crystallography.Protein science : a publication of the Protein Society · 2016Article
- Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif.Nature communications · 2015Article
- Structural basis for epitope masking and strain specificity of a conserved epitope in an intrinsically disordered malaria vaccine candidate.Scientific reports · 2015Article
- Characterization of an anti-Bla g 1 scFv: epitope mapping and cross-reactivity.Molecular immunology · 2014Article
- Antibody neutralization of retargeted measles viruses.Virology · 2014Article
- Conformational heterogeneity in antibody-protein antigen recognition: implications for high affinity protein complex formation.The Journal of biological chemistry · 2014Article
- TanCAR: A Novel Bispecific Chimeric Antigen Receptor for Cancer Immunotherapy.Molecular therapy. Nucleic acids · 2013Article
- Structure and interactions of the human programmed cell death 1 receptor.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Monoclonal antibodies have recently started to deliver on their promise as highly specific and active drugs; however, a more effective, knowledge-based approach to the selection, design, and optimization of potential therapeutic antibodies is currently limited by the surprising lack of detailed structural information for complexes formed with target proteins. Here we show that complexes formed with minimal antigen binding single chain variable fragments (scFv) reliably reflect all the features of the binding interface present in larger Fab fragments, which are commonly used as therapeutics, and report the development of a robust, reliable, and relatively rapid approach to the determination of high resolution models for scFv-target protein complexes. This NMR spectroscopy-based approach combines experimental determination of the interaction surfaces and relative orientations of the scFv and target protein, with NMR restraint-driven, semiflexible docking of the proteins to produce a reliable and highly informative model of the complex. Experience with scFvs and Fabs targeted at a number of secreted regulatory proteins suggests that the approach will be applicable to many therapeutic antibodies targeted at proteins, and its application is illustrated for a potential therapeutic antibody targeted at the cytokine IL-1beta. The detailed structural information that can be obtained by this approach has the potential to have a major impact on the rational design and development of an increasingly important class of biological pharmaceuticals.
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What OpenQuestion holds
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.