Evidence map›Paper›PMID 34638659›Full record

ReviewInternational journal of molecular sciences2021

Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties.

Daria A Belinskaia, Polina A Voronina, Vladimir I Shmurak, Richard O Jenkins, Nikolay V Goncharov

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 217 papers, 5 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
217citing papers in PubMed, 5 pooled it
14.3field-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

217 citing papers in PubMed, 5 syntheses or guidelines pooled it, 335 citations in OpenAlex.

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157 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

5 authors at 2 institutions in 2 countries.

Daria A BelinskaiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez 44, 194223 St. Petersburg, Russia.
Polina A VoroninaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez 44, 194223 St. Petersburg, Russia.
Vladimir I ShmurakSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez 44, 194223 St. Petersburg, Russia.
Richard O JenkinsLeicester School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK.
Nikolay V GoncharovSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez 44, 194223 St. Petersburg, Russia.
Institute of Evolutionary Physiology and Biochemistry · RUDe Montfort University · GB

Funding

the State assignment AAAA-A18-118012290142-9
6 · The paper itself

Abstract

Being one of the main proteins in the human body and many animal species, albumin plays a decisive role in the transport of various ions-electrically neutral and charged molecules-and in maintaining the colloidal osmotic pressure of the blood. Albumin is able to bind to almost all known drugs, as well as many nutraceuticals and toxic substances, largely determining their pharmaco- and toxicokinetics. Albumin of humans and respective representatives in cattle and rodents have their own structural features that determine species differences in functional properties. However, albumin is not only passive, but also an active participant of pharmacokinetic and toxicokinetic processes, possessing a number of enzymatic activities. Numerous experiments have shown esterase or pseudoesterase activity of albumin towards a number of endogeneous and exogeneous esters. Due to the free thiol group of Cys34, albumin can serve as a trap for reactive oxygen and nitrogen species, thus participating in redox processes. Glycated albumin makes a significant contribution to the pathogenesis of diabetes and other diseases. The interaction of albumin with blood cells, blood vessels and tissue cells outside the vascular bed is of great importance. Interactions with endothelial glycocalyx and vascular endothelial cells largely determine the integrative role of albumin. This review considers the esterase, antioxidant, transporting and signaling properties of albumin, as well as its structural and functional modifications and their significance in the pathogenesis of certain diseases.

Indexed as

AnimalsAntioxidantsEsterasesHumansOxidation-ReductionProtein TransportSerum AlbuminSignal TransductionAntioxidantsEsterasesSerum Albuminadvanced glycation end productsalbuminendotheliumesterasesglycocalyxoxidative stresspathogenesistranscytosistransport

Identifiers

PMID34638659
PMCPMC8508759
OpenAlexW3202291377

What Socratic 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 Socratic graph.