Journal ArticleDOI
Serum heme-albumin: An allosteric protein
Paolo Ascenzi,Mauro Fasano +1 more
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TLDR
Heme scavenging by plasma proteins, including serum albumin (SA), provides protection against free‐heme oxidative damage, limits access by pathogens to the heme, and contributes to iron homeostasis by recycling theHeme iron.Abstract:
Heme scavenging by plasma proteins, including serum albumin (SA), provides protection against free-heme oxidative damage, limits access by pathogens to the heme, and contributes to iron homeostasis by recycling the heme iron. In turn, serum heme-albumin (SA-heme) acquires heme-based ligand-binding and (pseudo-)enzymatic properties. Heme binding to SA and SA-heme reactivity are allosterically and competitively modulated by endogenous and exogenous third components, this being relevant in pharmacotherapy management.read more
Citations
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Journal ArticleDOI
Human serum albumin: from bench to bedside.
TL;DR: HSA is a valuable biomarker of many diseases, including cancer, rheumatoid arthritis, ischemia, post-menopausal obesity, severe acute graft-versus-host disease, and diseases that need monitoring of the glycemic control.
Journal ArticleDOI
Allostery in a monomeric protein: the case of human serum albumin.
Paolo Ascenzi,Mauro Fasano +1 more
TL;DR: Both functional and structural aspects of the allosteric modulation of heme and drug binding to HSA and of the drug-dependent reactivity of HSA-heme are reviewed.
Journal ArticleDOI
Flavonoid binding to human serum albumin.
TL;DR: Present data indicate a novel role of fatty acids as allosteric inhibitors of flavonoid bioavailability, and appear to be relevant in rationalizing the interference between dietary compounds, food supplements, and drugs.
Journal ArticleDOI
Heme: Modulator of Plasma Systems in Hemolytic Diseases
Lubka T. Roumenina,Lubka T. Roumenina,Lubka T. Roumenina,Julie Rayes,Sébastien Lacroix-Desmazes,Sébastien Lacroix-Desmazes,Sébastien Lacroix-Desmazes,Jordan D. Dimitrov,Jordan D. Dimitrov,Jordan D. Dimitrov +9 more
TL;DR: This review analyzes heme interactions with coagulation, complement, and immunoglobulins to better understand the complex pathogenesis of hemolytic diseases.
Journal ArticleDOI
An overview of albumin and alpha-1-acid glycoprotein main characteristics: highlighting the roles of amino acids in binding kinetics and molecular interactions
TL;DR: This review summarizes the common knowledge about the structural and molecular characteristics of both ALB and AGP in humans, and about the most involved amino acids in their high-affinity binding pockets, and is useful for the design of new drug entities with high-binding characteristics.
References
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Journal ArticleDOI
The Protein Data Bank
Helen M. Berman,John D. Westbrook,Zukang Feng,Gary L. Gilliland,Talapady N. Bhat,Helge Weissig,Ilya N. Shindyalov,Philip E. Bourne +7 more
TL;DR: The goals of the PDB are described, the systems in place for data deposition and access, how to obtain further information and plans for the future development of the resource are described.
Journal ArticleDOI
SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.
Nicolas Guex,Manuel C. Peitsch +1 more
TL;DR: An environment for comparative protein modeling is developed that consists of SWISS‐MODEL, a server for automated comparativeprotein modeling and of the SWiss‐PdbViewer, a sequence to structure workbench that provides a large selection of structure analysis and display tools.
Book ChapterDOI
Structure of serum albumin.
Daniel C. Carter,Joseph X. Ho +1 more
TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Book
All About Albumin: Biochemistry, Genetics, and Medical Applications
TL;DR: The Albumin Molecule: Its Structure and Chemical Properties and Practical Aspects: Albumin in the Laboratory.
Journal ArticleDOI
Structural Basis of the Drug-Binding Specificity of Human Serum Albumin.
TL;DR: Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation.