ArticleProtein science : a publication of the Protein Society2019
Human serum albumin presents isoform variants with altered neonatal Fc receptor interactions.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Comparative Characterisation of Five Plasma-Derived Human Serum Albumin Preparations: Structural Integrity, Functional Properties, and Quality Attributes.Pharmaceuticals (Basel, Switzerland) · 2026Article
- A bioinformatic survey of RNA isoform diversity and expression across 9 GTEx tissues using long-read sequencing data.BMC genomics · 2025Article
- Enhanced plasma half-life and efficacy of engineered human albumin-fused GLP-1 despite enzymatic cleavage of its C-terminal end.Communications biology · 2025Article
- Computational Study of Molecular Mechanism for the Involvement of Human Serum Albumin in the Renin-Angiotensin-Aldosterone System.International journal of molecular sciences · 2024Article
- Albumin, an interesting and functionally diverse protein, varies from 'native' to 'effective' (Review).Molecular medicine reports · 2024Review
- Clinical Significance of Serum Albumin and Implications of FcRn Inhibitor Treatment in IgG-Mediated Autoimmune Disorders.Frontiers in immunology · 2022Review
- Biomonitoring of Ambient Outdoor Air Pollutant Exposure in Humans Using Targeted Serum Albumin Adductomics.Chemical research in toxicology · 2021Article
- Human serum albumin presents isoform variants with altered neonatal Fc receptor interactions.Protein science : a publication of the Protein Society · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin (HSA) is the most abundant protein in plasma and presents the particularity, with IgG, to have an extraordinary long serum half-life conferred by its interaction with the neonatal Fc receptor (FcRn). If the impact of IgG post-translational modifications (PTMs) on FcRn binding is well documented, it is far less reported for HSA despite numerous PTMs occurring on the protein in plasma. HSA is susceptible to numerous degradation reactions in plasma, because of aging, oxidative stress or liver and pancreas related pathologies. In the present study, we combined FcRn affinity chromatography and mass spectrometry to investigate the impact of HSA PTMs upon FcRn binding. This methodology presents the advantage to distinguish the effect of a single modification from a plasma HSA preparation made of a mixture of different isoforms. Cys
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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.