Evidence map›Paper›PMID 26445900›Full record

ArticleScientific reports2015

Cutoff lensing: predicting catalytic sites in enzymes.

Simon Aubailly, Francesco Piazza

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

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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

2 citing papers in PubMed.

  1. 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

2 authors.

Simon AubaillyUniversité d'Orléans, Centre de Biophysique Moléculaire, CNRS-UPR4301, Rue C. Sadron, 45071, Orléans, France.
Francesco PiazzaUniversité d'Orléans, Centre de Biophysique Moléculaire, CNRS-UPR4301, Rue C. Sadron, 45071, Orléans, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Predicting function-related amino acids in proteins with unknown function or unknown allosteric binding sites in drug-targeted proteins is a task of paramount importance in molecular biomedicine. In this paper we introduce a simple, light and computationally inexpensive structure-based method to identify catalytic sites in enzymes. Our method, termed cutoff lensing, is a general procedure consisting in letting the cutoff used to build an elastic network model increase to large values. A validation of our method against a large database of annotated enzymes shows that optimal values of the cutoff exist such that three different structure-based indicators allow one to recover a maximum of the known catalytic sites. Interestingly, we find that the larger the structures the greater the predictive power afforded by our method. Possible ways to combine the three indicators into a single figure of merit and into a specific sequential analysis are suggested and discussed with reference to the classic case of HIV-protease. Our method could be used as a complement to other sequence- and/or structure-based methods to narrow the results of large-scale screenings.

Indexed as

Models, StatisticalAllosteric SiteAmidinotransferasesAmino AcidsArginine KinaseCatalytic DomainComputer SimulationDatabases, ProteinHIV-1HIV ProteaseHumansAmidinotransferasesAmino AcidsArginine Kinaseglycine amidinotransferaseHIV Protease

Identifiers

PMID26445900
PMCPMC4597221

What OpenQuestion holds

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Registered trials

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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.