Evidence map›Paper›PMID 12160466›Full record

ArticleThe Biochemical journal2002

Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases.

Pompea Del Vecchio, Giuseppe Graziano, Vincenzo Granata, Guido Barone, Luigi Mandrich, Mosè Rossi, Giuseppe Manco

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 65 citations in OpenAlex.

  1. Buttressing ligand-binding pockets in de novo designed NTF2-like domains.Protein science : a publication of the Protein Society · 2025
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  16. Carboxylic ester hydrolases from hyperthermophiles.Extremophiles : life under extreme conditions · 2009
    Review
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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 3 institutions in 1 country.

Pompea Del VecchioDepartment of Chemistry, University of Naples Federico II, Via Cintia, 45-80126 Naples, Italy. delvecchio@chemistry.unina.it
Giuseppe Graziano
Vincenzo Granata
Guido Barone
Luigi Mandrich
Mosè Rossi
Giuseppe Manco
Institute of Protein Biochemistry · ITUniversity of Naples Federico II · ITUniversity of Sannio · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The stability of two thermophilic esterases, AFEST from Archaeoglobus fulgidus and EST2 from Alicyclobacillus acidocaldarius, against the denaturing action of urea and guanidine hydrochloride has been investigated by means of steady-state fluorescence and circular dichroism measurements. Experimental results indicate that the two enzymes, even though very resistant to temperature and urea, show a resistance to guanidine hydrochloride weaker than expected on the basis of data collected so far for a large set of globular proteins. Structural information available for AFEST and EST2 and ideas that emerged from studies on the molecular origin of the greater thermal stability of thermophiles allow the suggestion of a reliable rationale. The present results may be an indication that the optimization of charge-charge interactions on the protein surface is a key factor for the stability of the two esterases.

Indexed as

ArchaeoglobusBacillusCircular DichroismEsterasesGuanidineProtein DenaturationSpectrometry, FluorescenceUreaEsterasesGuanidineUrea

Identifiers

PMID12160466
PMCPMC1222942
OpenAlexW2132834378

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.