Evidence map›Paper›PMID 33799517›Full record

ArticleBiomolecules2021

Trehalose Restrains the Fibril Load towards α-Lactalbumin Aggregation and Halts Fibrillation in a Concentration-Dependent Manner.

Sania Bashir, Ishfaq Ahmad Ahanger, Anas Shamsi, Mohamed F Alajmi, Afzal Hussain, Hani Choudhry, Faizan Ahmad, Md Imtaiyaz Hassan, Asimul Islam

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

4 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
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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

9 authors at 3 institutions in 2 countries.

Sania BashirCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.ORCID 0000-0002-8775-2592
Ishfaq Ahmad AhangerCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.ORCID 0000-0001-9088-4257
Anas ShamsiCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.ORCID 0000-0001-7055-7056
Mohamed F AlajmiDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia.
Afzal HussainDepartment of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia.ORCID 0000-0001-9769-2557
Hani ChoudhryDepartment of Biochemistry, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia.ORCID 0000-0003-0401-6619
Faizan AhmadCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.
Md Imtaiyaz HassanCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.ORCID 0000-0002-3663-4940
Asimul IslamCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.ORCID 0000-0001-9060-7970
Jamia Millia Islamia · INKing Saud University · SAKing Abdulaziz University · SA

Funding

Deanship of Scientific Research, King Saud University (Grant number RSP-2019-122)Indian Council of Medical Research (ICMR) BIC/12(16)/2014
6 · The paper itself

Abstract

Protein aggregation and misfolding are some of the most challenging obstacles, customarily studied for their association with amyloid pathologies. The mechanism of amyloid fibrillation development is a dynamic phenomenon involving various factors such as the intrinsic properties of protein and the physical and chemical environmental conditions. The purpose of this study was to see the thermal aggregation profile of alpha-lactalbumin (α-LA) and to delineate the effect of trehalose on its aggregation profile. α-LA was subjected to thermal aggregation at high concentrations. UV-Vis spectroscopy, a turbidity assay, intrinsic fluorescence, Rayleigh scattering and a thioflavin T (ThT) assay explained the steady outcomes that 1 M trehalose repressed α-LA aggregation in the most effective way followed by 0.75 M and 0.5 M and to a significantly lesser degree by 0.25 M. Multi spectroscopic obser Sania

Indexed as

Protein AggregatesAnimalsBenzothiazolesCattleLactalbuminMolecular Docking SimulationNephelometry and TurbidimetryProtein BindingScattering, RadiationSpectrometry, FluorescenceSpectrophotometry, UltravioletTemperatureTrehaloseBenzothiazolesLactalbuminProtein Aggregatesthioflavin TTrehalosemolecular dockingprotein aggregationspectroscopytransmission electron microscopytrehalose

Identifiers

PMID33799517
PMCPMC8001226
OpenAlexW3133605594

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.