Evidence map›Paper›PMID 31877740›Full record

ArticleInternational journal of molecular sciences2019

Characterization and Immobilization of a Novel SGNH Family Esterase (

Ly Thi Huong Luu Le, Wanki Yoo, Sangeun Jeon, Kyeong Kyu Kim, T Doohun Kim

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Antiwrinkle and Antimelanogenesis Effects of TyndallizedInternational journal of molecular sciences · 2020
    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.

Ly Thi Huong Luu LeDepartment of Chemistry, College of Natural Science, Sookmyung Women's University, Seoul 04310, Korea.
Wanki YooDepartment of Chemistry, College of Natural Science, Sookmyung Women's University, Seoul 04310, Korea.
Sangeun JeonDepartment of Chemistry, College of Natural Science, Sookmyung Women's University, Seoul 04310, Korea.
Kyeong Kyu KimDepartment of Precision Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
T Doohun KimDepartment of Chemistry, College of Natural Science, Sookmyung Women's University, Seoul 04310, Korea.

Funding

National Research Foundation of Korea NRF-2018R1D1A1B07044447
6 · The paper itself

Abstract

The SGNH family esterases are highly effective biocatalysts due to their strong catalytic efficiencies, great stabilities, relatively small sizes, and ease of immobilization. Here, a novel SGNH family esterase (

Indexed as

Bacterial ProteinsBinding SitesConserved SequenceEnzymes, ImmobilizedEnzyme StabilityLactobacillus acidophilusPhospholipasesProtein BindingSubstrate SpecificityBacterial ProteinsEnzymes, ImmobilizedPhospholipasescrosslinked enzyme aggregatesimmobilizationLactobacillus acidophilusLaSGNH1SGNH family esterases

Identifiers

PMID31877740
PMCPMC6981805

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.