Structural analysis and fatty acid-binding properties of two Croatian variants of human serum albumin

Author:

Kragh-Hansen Ulrich,Campagnoli Monica,Dodig Slavica,Nielsen Henning,Benko Bojan,Raos Miljenko,Cesati Roberto,Sala Alberto,Galliano Monica,Minchiotti Lorenzo

Publisher

Elsevier BV

Subject

Biochemistry, medical,Clinical Biochemistry,Biochemistry,General Medicine

Reference16 articles.

1. All about albumin: biochemistry, genetics and medical applications;Peters,1996

2. Genetic variants showing apparent hot-spots in the human serum albumin gene;Galliano;Clin. Chim. Acta,1999

3. Bisalbuminemia in two Croatian families;Dodig;Arch. Med. Res.,2000

4. Structural study of the glycosylated and unglycosylated forms of a genetic variant of human serum albumin (63Asp→Asn);Sakamoto;Biochim. Biophys. Acta,1995

5. Structural characterization of a chain termination mutant of human serum albumin;Galliano;J. Biol. Chem.,1986

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1. Role of Herborn (K240E) and Milano Slow (D375H) human serum albumin variants towards binding of phenylbutazone and ibuprofen;International Journal of Biological Macromolecules;2019-08

2. Human plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2018-04

3. Intrinsically Disordered Regions in Serum Albumin: What Are They For?;Cell Biochemistry and Biophysics;2017-03-10

4. Human serum albumin isoforms: Genetic and molecular aspects and functional consequences;Biochimica et Biophysica Acta (BBA) - General Subjects;2013-12

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