Evidence map›Paper›PMID 30347699›Full record

ArticleMicroorganisms2018

Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 from

María-Efigenia Álvarez-Cao, Roberto González, María A Pernas, María Luisa Rúa

Open access · goldAbstract read
In one paragraph

Article in Microorganisms, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. 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

4 authors at 1 institution in 1 country.

María-Efigenia Álvarez-CaoDepartment of Food and Analytical Chemistry, Sciences Faculty of Ourense, University of Vigo, As Lagoas s/n, 32004 Ourense, Spain. mariaealvarez@uvigo.es.
Roberto GonzálezDepartment of Food and Analytical Chemistry, Sciences Faculty of Ourense, University of Vigo, As Lagoas s/n, 32004 Ourense, Spain. robergg@uvigo.es.
María A PernasDepartment of Food and Analytical Chemistry, Sciences Faculty of Ourense, University of Vigo, As Lagoas s/n, 32004 Ourense, Spain. mapernas@mundo-r.com.
María Luisa RúaDepartment of Food and Analytical Chemistry, Sciences Faculty of Ourense, University of Vigo, As Lagoas s/n, 32004 Ourense, Spain. mlrua@uvigo.es.ORCID 0000-0001-5952-2442
Universidade de Vigo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermophilic proteins have evolved different strategies to maintain structure and function at high temperatures; they have large, hydrophobic cores, and feature increased electrostatic interactions, with disulfide bonds, salt-bridging, and surface charges. Oligomerization is also recognized as a mechanism for protein stabilization to confer a thermophilic adaptation. Mesophilic proteins are less thermostable than their thermophilic homologs, but oligomerization plays an important role in biological processes on a wide variety of mesophilic enzymes, including thermostabilization. The mesophilic yeast

Indexed as

Candida rugosadimerizationinhibitioninterfacial activationkineticlipasestructure

Identifiers

PMID30347699
PMCPMC6313406
OpenAlexW2896670604

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.