Beyond Expansion: Structural Studies on the Transport Roles of Human Serum Albumin

@article{Curry2002BeyondES,
  title={Beyond Expansion: Structural Studies on the Transport Roles of Human Serum Albumin},
  author={Stephen Curry},
  journal={Vox Sanguinis},
  year={2002},
  volume={83}
}
  • S. Curry
  • Published 1 August 2002
  • Chemistry, Biology
  • Vox Sanguinis
Introduction Clinically, human serum albumin (HSA) is best known as a volume expander but its prominent role in this capacity perhaps overshadows the protein’s other major talent: transport. As a plasma transporter molecule HSA displays truly bewildering binding capabilities. Its primary physiological ligands are non-esterified long-chain fatty acids but HSA also binds toxic metabolites such as bilirubin and CMPF, steroid hormones, thyroxine, tryptophan and several vitamins and metal ions… 
Lessons from the crystallographic analysis of small molecule binding to human serum albumin.
  • S. Curry
  • Biology, Chemistry
    Drug metabolism and pharmacokinetics
  • 2009
TLDR
Since further progress is likely to benefit from increased structural scrutiny of HSA, methodological developments instrumental to the success of crystallographic analysis of the protein are discussed in some detail.
Structural basis of drug recognition by human serum albumin.
TLDR
The modulation of ligand binding to HSA is relevant not only under physiological conditions, but also in the pharmacological therapy management as several factors can modulate drug binding.
Serum Albumin: A Multifaced Enzyme
TLDR
An overview of the intrinsic and metal dependent (pseudo-)enzymatic properties of HSA is reported to highlight the roles played by this multifaced protein.
The extraordinary ligand binding properties of human serum albumin
TLDR
The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins.
Human serum albumin: from bench to bedside.
Human plasma lipocalins and serum albumin: Plasma alternative carriers?
Heme-based catalytic properties of human serum albumin
TLDR
Under physiological and pathological conditions, HSA has a pivotal role in heme scavenging transferring the metal-macrocycle from high- and low-density lipoproteins to hemopexin, thus acquiring globin-like reactivity.
Heme impairs allosterically drug binding to human serum albumin Sudlow's site I.
Modulation of heme and myristate binding to human serum albumin by anti‐HIV drugs
TLDR
The binding of Fe(III)heme to HSA in the presence of three representative anti‐HIV drugs and myristate is investigated, providing a foundation for the comprehension of the complex network of links modulating HSA‐binding properties.
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TLDR
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TLDR
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TLDR
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TLDR
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