Evidence map›Paper›PMID 34576249›Full record

ReviewInternational journal of molecular sciences2021

Serum Albumin: A Multifaced Enzyme.

Giovanna De Simone, Alessandra di Masi, Paolo Ascenzi

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 1 pooled it
11.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

106 citing papers in PubMed, 1 synthesis or guideline pooled it, 203 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Disease Modulating Agents in Cirrhosis.Clinics in liver disease · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Observational
  18. Article
  19. Human Serum Albumin: 3D Insight on Protein Hydration.International journal of molecular sciences · 2025
    Article
  20. Article

46 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Giovanna De SimoneDipartimento di Scienze, Università degli Studi Roma Tre, Viale Marconi 446, 00146 Roma, Italy.ORCID 0000-0002-9358-9891
Alessandra di MasiDipartimento di Scienze, Università degli Studi Roma Tre, Viale Marconi 446, 00146 Roma, Italy.ORCID 0000-0002-1122-8663
Paolo AscenziLaboratorio Interdipartimentale di Microscopia Elettronica, Università degli Studi Roma Tre, Via della Vasca Navale 79, 00146 Roma, Italy.ORCID 0000-0002-6449-2150
Roma Tre University · IT

Funding

Ministero degli Affari Esteri e della Cooperazione Internazionale MAMBOMinistero dell'Istruzione, dell'Università e della Ricerca Dipartimenti di Eccellenza, MIUR (Legge 232/2016, Articolo 1, Comma 314-337)
6 · The paper itself

Abstract

Human serum albumin (HSA) is the most abundant protein in plasma, contributing actively to oncotic pressure maintenance and fluid distribution between body compartments. HSA acts as the main carrier of fatty acids, recognizes metal ions, affects pharmacokinetics of many drugs, provides the metabolic modification of some ligands, renders potential toxins harmless, accounts for most of the anti-oxidant capacity of human plasma, and displays esterase, enolase, glucuronidase, and peroxidase (pseudo)-enzymatic activities. HSA-based catalysis is physiologically relevant, affecting the metabolism of endogenous and exogenous compounds including proteins, lipids, cholesterol, reactive oxygen species (ROS), and drugs. Catalytic properties of HSA are modulated by allosteric effectors, competitive inhibitors, chemical modifications, pathological conditions, and aging. HSA displays anti-oxidant properties and is critical for plasma detoxification from toxic agents and for pro-drugs activation. The enzymatic properties of HSA can be also exploited by chemical industries as a scaffold to produce libraries of catalysts with improved proficiency and stereoselectivity for water decontamination from poisonous agents and environmental contaminants, in the so called "green chemistry" field. Here, an overview of the intrinsic and metal dependent (pseudo-)enzymatic properties of HSA is reported to highlight the roles played by this multifaced protein.

Indexed as

Green Chemistry TechnologyReactive Oxygen SpeciesAnimalsAntioxidantsAspirinBiomarkersCatalysisFructose-Bisphosphate AldolaseGlucuronidaseHemeHumansIonsLigandsLipid PeroxidationMolecular ConformationPhosphopyruvate HydrataseAntioxidantsAspirinBiomarkersFructose-Bisphosphate AldolaseGlucuronidaseHemeIonsLigandsPhosphopyruvate HydrataseReactive Oxygen SpeciesSerum Albumin, Humanaldolase activityanti-oxidant activityenolase activityenzymatic propertiesesterase activityglucuronidase activityhuman serum albuminhuman serum heme-albuminperoxidase activity

Identifiers

PMID34576249
PMCPMC8466385
OpenAlexW3198921728

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.