A Receptor-Mediated Mechanism to Support Clinical Observation of Altered Albumin Variants
Author:
Affiliation:
1. Department of Molecular, Biosciences, University of Oslo, Oslo, Norway
Funder
Molecular Biology, Biotechnology and Bioinformatics
University of Oslo
The Norwegian Cancer Society
Publisher
Oxford University Press (OUP)
Subject
Biochemistry (medical),Clinical Biochemistry
Link
http://academic.oup.com/clinchem/article-pdf/53/12/2216/32689793/clinchem2216.pdf
Reference5 articles.
1. Dolcini L, Caridi G, Dagnino M, Sala A, Gokce S, Sokucu S, et al. Analbuminemia produced by a novel splicing mutation. Clin Chem2007;53:1549-1552.
2. The Albumin Website. http://www.albumin.org (accessed August 2007)..
3. Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol2007;7:715-725.
4. Anderson CL, Chaudhury C, Kim J, Bronson CL, Wani MA, Mohanty S. Perspective—FcRn transports albumin: relevance to immunology and medicine. Trends Immunol2006;27:343-348.
5. Andersen JT, Dee Qian J, Sandlie I. The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin. Eur J Immunol2006;36:3044-3051.
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2. Unraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based Therapeutics;Frontiers in Immunology;2015-01-26
3. Human serum albumin: From bench to bedside;Molecular Aspects of Medicine;2012-06
4. A novel splicing mutation causes analbuminemia in a Portuguese boy;Molecular Genetics and Metabolism;2012-03
5. Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor;Nature Communications;2012-01
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