Evidence map›Paper›PMID 31842334›Full record

ArticleBiomolecules2019

Critical Factors in Human Antizymes that Determine the Differential Binding, Inhibition, and Degradation of Human Ornithine Decarboxylase.

Ju-Yi Hsieh, Yen-Chin Liu, I-Ting Cheng, Chu-Ju Lee, Yu-Hsuan Wang, Yi-Shiuan Fang, Yi-Liang Liu, Guang-Yaw Liu, Hui-Chih Hung

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Protein degradation of antizyme depends on the N-terminal degrons.Protein science : a publication of the Protein Society · 2024
    Article
  3. Biomolecules · 2023
    Article
  4. 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

9 authors at 2 institutions in 1 country.

Ju-Yi HsiehDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Yen-Chin LiuDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
I-Ting ChengDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Chu-Ju LeeDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Yu-Hsuan WangDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Yi-Shiuan FangDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Yi-Liang LiuDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.
Guang-Yaw LiuInstitute of Biochemistry, Microbiology & Immunology, Chung Shan Medical University, Taichung 40201, Taiwan.
Hui-Chih HungDepartment of Life Sciences and Institute of Genomics & Bioinformatics, National Chung Hsing University, Taichung 40227, Taiwan.ORCID 0000-0003-0180-1822
National Chung Hsing University · TWChung Shan Medical University Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antizyme (AZ) is a protein that negatively regulates ornithine decarboxylase (ODC). AZ achieves this inhibition by binding to ODC to produce AZ-ODC heterodimers, abolishing enzyme activity and targeting ODC for degradation by the 26S proteasome. In this study, we focused on the biomolecular interactions between the C-terminal domain of AZ (AZ

Indexed as

Binding SitesHumansOrnithine DecarboxylaseOrnithine Decarboxylase InhibitorsProteinsProteolysisOrnithine Decarboxylaseornithine decarboxylase antizymeOrnithine Decarboxylase InhibitorsProteinsAZ isoformbinding affinityprotein–protein interactionubiquitin-independent degradation

Identifiers

PMID31842334
PMCPMC6995573
OpenAlexW2996105183

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.