Evidence map›Paper›PMID 31598788›Full record

ArticleJournal of molecular modeling2019

Molecular simulation of PcCel45A protein expressed from Aspergillus nidulans to understand its structure, dynamics, and thermostability.

Mehmet Altay Unal, Bahadir Boyacioglu, Huseyin Unver, Ayhan Elmali

Abstract read
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In one paragraph

Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. 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.

Mehmet Altay UnalStem Cell Institute, Ankara University, 06520, Cevizlidere-Ankara, Turkey. altay.unal@ankara.edu.tr.ORCID http://orcid.org/0000-0001-8607-5043
Bahadir BoyaciogluVocational School of Health Services, Ankara University, 06290, Kecioren-Ankara, Turkey.
Huseyin UnverFaculty of Sciences, Department of Physics, Ankara University, 06100, Besevler Ankara, Turkey.
Ayhan ElmaliDepartment of Physics Engineering, Faculty of Engineering, Ankara University, 06100, Besevler Ankara, Turkey.
Ankara University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PACS and mathematical subject classification numbers as needed. Molecular dynamic simulation is a very usable tool to understand various factors, including structure temperature dependence, dynamics, and stability for protein structure. The three main components, namely endoglucanase, exoglucanase, and β-glucosidase, effectively convert lignocellulosic biomass into fermentable sugar. Cellulose is the major component of plant cell walls and is the most abundant organic compound on the earth. Somewhat organisms can use cellulose as a food source, possessing cellulases (cellobiohydrolases and endoglucanases) that can catalyze the hydrolysis of the β-(1,4) glycosidic bonds. In this work, we investigated conformational and structural properties of PcCel45A protein by changing at temperatures with 300 K, 333 K, and 352 K. We found that the ASN92 residue was the major contributor to the stability of structure; some other residues correlated significantly with thermal stability. We also compared the theoretical results of the current study with the experimental ones published in previous studies.

Indexed as

Aspergillus nidulansbeta-GlucosidaseBiomassCatalysisCellulaseCelluloseFungal ProteinsHydrolysisMolecular Dynamics SimulationTemperaturebeta-GlucosidaseCellulaseCelluloseFungal ProteinsMolecular dynamicsPCcel45A

Identifiers

PMID31598788
OpenAlexW2979872002

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.