ArticleMolecules (Basel, Switzerland)2017
NMR Detection of Semi-Specific Antibody Interactions in Serum Environments.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
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.
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.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it, 13 citations in OpenAlex.
- Preoperative neutrophil-to-lymphocyte ratio and systemic immune-inflammation index as prognostic biomarkers for postoperative pneumonia and pulmonary complications after thoracic surgery: a systematic review and meta-analysis.Frontiers in medicine · 2026Pooled it
- Negative interference with antibody-dependent cellular cytotoxicity mediated by rituximab from its interactions with human serum proteins.Frontiers in immunology · 2023Article
- Role of NMR in High Ordered Structure Characterization of Monoclonal Antibodies.International journal of molecular sciences · 2020Review
- Biophysical characterization of dynamic structures of immunoglobulin G.Biophysical reviews · 2020Review
- Review
- Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems.Journal of biomolecular NMR · 2018Article
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 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although antibody functions are executed in heterogeneous blood streams characterized by molecular crowding and promiscuous intermolecular interaction, detailed structural characterizations of antibody interactions have thus far been performed under homogeneous in vitro conditions. NMR spectroscopy potentially has the ability to study protein structures in heterogeneous environments, assuming that the target protein can be labeled with NMR-active isotopes. Based on our successful development of isotope labeling of antibody glycoproteins, here we apply NMR spectroscopy to characterize antibody interactions in heterogeneous extracellular environments using mouse IgG-Fc as a test molecule. In human serum, many of the HSQC peaks originating from the Fc backbone exhibited attenuation in intensity of various magnitudes. Similar spectral changes were induced by the Fab fragment of polyclonal IgG isolated from the serum, but not by serum albumin, indicating that a subset of antibodies reactive with mouse IgG-Fc exists in human serum without preimmunization. The
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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.