Evidence map›Paper›PMID 33513970›Full record

ArticleMarine drugs2021

An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate

Guang Yang, Matteo Mozzicafreddo, Patrizia Ballarini, Sandra Pucciarelli, Cristina Miceli

Open access · goldAbstract readComparative Study
In one paragraph

Article in Marine drugs, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. 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

5 authors at 1 institution in 1 country.

Guang YangSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino (MC), Italy.
Matteo MozzicafreddoSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino (MC), Italy.ORCID 0000-0001-9835-8446
Patrizia BallariniSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino (MC), Italy.
Sandra PucciarelliSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino (MC), Italy.ORCID 0000-0003-4178-2689
Cristina MiceliSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino (MC), Italy.ORCID 0000-0002-7829-8471
Università di Camerino · IT

Funding

FP7 People: Marie-Curie Actions BM1102
6 · The paper itself

Abstract

Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic

Indexed as

Cold TemperatureComputer SimulationAdaptation, PhysiologicalAmino Acid SequenceEuplotesLipaseProtein Structure, SecondaryLipaseamino acid compositionbioinformaticscold-adaptationhydrolytic enzymessecondary structure

Identifiers

PMID33513970
PMCPMC7912073
OpenAlexW3121276040

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.