Evidence map›Paper›PMID 15454427›Full record

ArticleBiophysical journal2004

Osmophobic effect of glycerol on irreversible thermal denaturation of rabbit creatine kinase.

Fan-Guo Meng, Yuan-Kai Hong, Hua-Wei He, Arkadii E Lyubarev, Boris I Kurganov, Yong-Bin Yan, Hai-Meng Zhou

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-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

11 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Refolding of Lysozyme in Glycerol as Studied by Fast Scanning Calorimetry.International journal of molecular sciences · 2022
    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

7 authors at 2 institutions in 2 countries.

Fan-Guo MengDepartment of Biological Sciences and Biotechnology, Tsinghua University, Beijing, China.
Yuan-Kai Hong
Hua-Wei He
Arkadii E Lyubarev
Boris I Kurganov
Yong-Bin Yan
Hai-Meng Zhou
Tsinghua University · CNA N Bach Institute of Biochemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein stability plays an extremely important role not only in its biological function but also in medical science and protein engineering. Osmolytes provide a general method to protect proteins from the unfolding and aggregation induced by extreme environmental stress. In this study, the effect of glycerol on protection of the model enzyme creatine kinase (CK) against heat stress was investigated by a combination of spectroscopic method and thermodynamic analysis. Glycerol could prevent CK from thermal inactivation and aggregation in a concentration-dependent manner. The spectroscopic measurements suggested that the protective effect of glycerol was a result of enhancing the structural stability of native CK. A further thermodynamic analysis using the activated-complex theory suggested that the effect of glycerol on preventing CK against aggregation was consistent with those previously established mechanisms in reversible systems. The osmophobic effect of glycerol, which preferentially raised the free energy of the activated complex, shifted the equilibrium between the native state and the activated complex in favor of the native state. A comparison of the inactivation rate and the denaturation rate suggested that the protection of enzyme activity by glycerol should be attributed to the enhancement of the structural stability of the whole protein rather than the flexible active site.

Indexed as

Hot TemperatureModels, ChemicalAnimalsCreatine KinaseEnergy TransferEnzyme ActivationEnzyme StabilityGlycerolHydrophobic and Hydrophilic InteractionsKineticsMultiprotein ComplexesMuscle, SkeletalOsmosisProtein DenaturationRabbitsTemperatureCreatine KinaseGlycerolMultiprotein Complexes

Identifiers

PMID15454427
PMCPMC1304650
OpenAlexW2141791707

What OpenQuestion holds

Textmetadata
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.