ReviewBiophysical reviews2018
Heat denaturation of the antibody, a multi-domain protein.
Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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
33 citing papers in PubMed, 82 citations in OpenAlex.
- Article
- Development of a Novel Engineered Antibody Format for PSMA-Targeted Radionuclide Therapy.Molecular pharmaceutics · 2025Article
- Detection of canine distemper virus (CDV) neutralising antibodies in small ruminants during peste-des-petits-ruminants virus (PPRV) surveillance in Zambia.BMC veterinary research · 2025Article
- Article
- Accelerated protein retention expansion microscopy using microwave radiation.Cell reports methods · 2024Article
- Heat-induced structural and chemical changes to a computationally designed miniprotein.Protein science : a publication of the Protein Society · 2024Article
- Developing a synergistic rate-retarding polymeric implant for controlling monoclonal antibody delivery in minimally invasive glaucoma surgery.International journal of biological macromolecules · 2024Article
- Study of Monoclonal Antibody Aggregation at the Air-Liquid Interface under Flow by ATR-FTIR Spectroscopic Imaging.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- The effect of temperature on the synthesis of magnetite nanoparticles by the coprecipitation method.Heliyon · 2024Article
- Impact of Urea on Monoclonal Antibodies: Multiple Destabilization and Aggregation Effects for Therapeutic Immunoglobulin G Proteins.ACS omega · 2024Article
- An electrochemical immunosensor based on a carboxylated multiwalled carbon nanotube-silver nanoparticle-chitosan functional layer for the detection of fipronil.Nanoscale advances · 2023Article
- In vivo deglycosylation of recombinant glycoproteins in tobacco BY-2 cells.Plant biotechnology journal · 2023Article
- Design of an alternate antibody fragment format that can be produced in the cytoplasm of Escherichia coli.Scientific reports · 2023Article
- Toward the rapid diagnosis of sepsis: dendritic copper nanostructure functionalized diazonium salt modified screen-printed graphene electrode for IL-6 detection.Mikrochimica acta · 2023Article
- Quantum Cascade Laser Based Infrared Spectroscopy: A New Paradigm for Protein Secondary Structure Measurement.Pharmaceutical research · 2023Article
- Radiolabeled GPVI-Fc for PET Imaging of Multiple Extracellular Matrix Fibers: A New Look into Pulmonary Fibrosis Progression.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2023Article
- Point-of-care detection of Japanese encephalitis virus biomarker in clinical samples using a portable smartphone-enabled electrochemical "Sensit" device.Bioengineering & translational medicine · 2023Article
- Increasing temperature denatures canine IgG reducing its ability to inhibit heartworm antigen detection.Parasites & vectors · 2023Article
- Tear nanoDSF Denaturation Profile Is Predictive of Glaucoma.International journal of molecular sciences · 2023Article
- Recent advances and challenges in temperature monitoring and control in microfluidic devices.Electrophoresis · 2023Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antibody is one of the most well-studied multi-domain proteins because of its abundance and physiological importance. In this article, we describe the effect of the complex, multi-domain structure of the antibody on its denaturation by heat. Natural antibodies are composed of 6 to 70 immunoglobulin fold domains, and are irreversibly denatured at high temperatures. Although the separated single immunoglobulin fold domain can be refolded after heat denaturation, denaturation of pairs of such domains is irreversible. Each antibody subclass exhibits a distinct heat tolerance, and IgE is especially known to be heat-labile. IgE starts unfolding at a lower temperature compared to other antibodies, because of the low stability of its CH3 domain. Each immunoglobulin domain starts unfolding at different temperatures. For instance, the CH3 domain of IgG unfolds at a higher temperature than its CH2 domain. Thus, the antibody has a mixture of folded and unfolded structures at a certain temperature. Co-existence of these folded and unfolded domains in a single polypeptide chain may increase the tendency to aggregate which causes the inactivation of the antibody.
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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.