Evidence map›Paper›PMID 35518265›Full record

ArticleRSC advances2020

Thermal resilience of ensilicated lysozyme

A Doekhie, M N Slade, L Cliff, L Weaver, R Castaing, J Paulin, Y-C Chen, K J Edler, F Koumanov, K J Marchbank and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Thermal Stabilisation of Lysozyme through Ensilication.Molecules (Basel, Switzerland) · 2024
    Article
  2. Review
  3. Article
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

12 authors at 3 institutions in 2 countries.

A DoekhieDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.ORCID https://orcid.org/0000-0002-9612-7588
M N SladeDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.ORCID https://orcid.org/0000-0002-0948-0317
L CliffDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.
L WeaverDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.
R CastaingMaterial and Chemical Characterisation Facility, University of Bath Claverton Down Bath BA2 7AY UK.
J PaulinThe Medical School, Framlington Place, Newcastle University Newcastle upon Tyne NE2 4HH UK.
Y-C ChenDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.
K J EdlerDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.ORCID https://orcid.org/0000-0001-5822-0127
F KoumanovDepartment for Health, University of Bath Claverton Down Bath BA2 7AY UK.ORCID https://orcid.org/0000-0002-9029-3390
K J MarchbankThe Medical School, Framlington Place, Newcastle University Newcastle upon Tyne NE2 4HH UK.ORCID https://orcid.org/0000-0003-1312-5411
J M H van den ElsenDepartment of Biology and Biochemistry, University of Bath Claverton Down Bath BA2 7AY UK.
A SartbaevaDepartment of Chemistry, University of Bath Claverton Down Bath BA2 7AY UK a.doekhie@bath.ac.uk.ORCID https://orcid.org/0000-0003-1017-0161
University of Bath · GBNewcastle upon Tyne Hospital · GBNational Centre for Compositional Characterisation of Materials · IN

Funding

Medical Research Council MC_PC_15030Medical Research Council MR/P002927/1
6 · The paper itself

Abstract

Ensilication is a novel method of protein thermal stabilisation using silica. It uses a modified sol-gel process which tailor fits a protective silica shell around the solvent accessible protein surface. This, electrostatically attached, shell has been found to protect the protein against thermal influences and retains its native structure and function after release. Here, we report the calorimetric analysis of an ensilicated model protein, hen egg-white lysozyme (HEWL) under several ensilication conditions. DSC, TGA-DTA-MS, CD, were used to determine unfolding temperatures of native, released and ensilicated lysozyme to verify the thermal resilience of the ensilicated material. Our findings indicate that ensilication protects against thermal fluctuations even at low concentrations of silica used for ensilication. Secondly, the thermal stabilisation is comparable to lyophilisation, and in some cases is even greater than lyophilisation. Additionally, we performed a mouse

Identifiers

PMID35518265
PMCPMC9056174
OpenAlexW3047087306

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.