Evidence map›Paper›PMID 34109551›Full record

ArticleMolecular biotechnology2021

Improvement Thermal Stability of D-Lactate Dehydrogenase by Hydrophobin-1 and in Silico Prediction of Protein-Protein Interactions.

Mehri Mokhtari-Abpangoui, Azadeh Lohrasbi-Nejad, Jafar Zolala, Masoud Torkzadeh-Mahani, Saba Ghanbari

Abstract read
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Article in Molecular biotechnology, 2021. 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
0.1field-weighted citation impact, top 67% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Microorganisms · 2022
    Review
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 2 institutions in 1 country.

Mehri Mokhtari-AbpangouiDepartment of Agricultural Biotechnology, Shahid Bahonar University of Kerman, Kerman, Iran.
Azadeh Lohrasbi-NejadDepartment of Agricultural Biotechnology, Shahid Bahonar University of Kerman, Kerman, Iran. a.lohrasbi@uk.ac.ir.ORCID http://orcid.org/0000-0003-3269-437X
Jafar ZolalaDepartment of Agricultural Biotechnology, Shahid Bahonar University of Kerman, Kerman, Iran.
Masoud Torkzadeh-MahaniDepartment of Biotechnology, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran.
Saba GhanbariDepartment of Biotechnology, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran.
Shahid Bahonar University of Kerman · IRGraduate University of Advanced Technology · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrophobins are small surface-active proteins. They can connect to hydrophobic or hydrophilic regions and oligomerize in solution to form massive construction. In nature, these proteins are produced by filamentous fungi at different stages of growth. So far, researchers have used them in various fields of biotechnology. In this study, recombinant hydrophobin-1 (rHFB1, 7.5 kDa) was used to stabilize recombinant D-lactate dehydrogenase (rD-LDH, 35 kDa). rD-LDH is a sensitive enzyme deactivated and oxidized by external agents such as O

Indexed as

Enzyme StabilityFungal ProteinsHydrophobic and Hydrophilic InteractionsLactate DehydrogenasesModels, MolecularMolecular Docking SimulationProtein BindingProtein ConformationRecombinant ProteinsThermodynamicsD-lactate dehydrogenaseFungal ProteinsLactate DehydrogenasesRecombinant ProteinsD-lactate dehydrogenaseDockingHydrophobin-1Kinetic parametersProtein–protein interactionThermodynamic parametersThermostability

Identifiers

PMID34109551
OpenAlexW3169495406

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.