Evidence map›Paper›PMID 30559593›Full record

ArticleEvolutionary bioinformatics online2018

Putative Interaction Proteins of the Ubiquitin Ligase Hrd1 in

Haolang Jiang, Lianyu Lin, Wei Tang, Xuehang Chen, Qiaojia Zheng, Jun Huang, Tao Yang, Li Su, Yanhan Dong, Baohua Wang and 1 more

Open access · goldAbstract read
In one paragraph

Article in Evolutionary bioinformatics online, 2018. 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 50% 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, 4 citations in OpenAlex.

  1. Article
  2. 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

11 authors at 3 institutions in 1 country.

Haolang JiangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Lianyu LinFujian University Key Laboratory for Plant-Microbe Interaction and College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, China.
Wei TangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Xuehang ChenFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Qiaojia ZhengFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Jun HuangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Tao YangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Li SuFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Yanhan DongQingdao University, Qingdao, China.
Baohua WangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Zonghua WangFujian University Key Laboratory for Plant-Microbe Interaction and College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, China.
Fujian Agriculture and Forestry University · CNMinjiang University · CNQingdao University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the entry portal of the conventional secretory pathway where the newly synthesized polypeptides fold, modify, and assemble. The ER responses to the unfolded proteins in its lumen (ER stress) by triggering intracellular signal transduction pathways include the ER-associated degradation (ERAD) pathway and the unfolded protein response (UPR) pathway. In yeast and mammals, the ubiquitin ligase Hrd1 is indispensable for the ERAD pathway, and also Hrd1-mediated ERAD pathway plays a crucial role in maintaining homeostasis and metabolism of human beings. However, the underlying physiological roles and regulatory mechanism of the Hrd1-involved ERAD pathway in the plant pathogenic fungi are still unclear. Here, we identified the Hrd1 orthologous proteins from 9 different fungi and noticed that these Hrd1 orthologs are conserved. Through identification of MoHrd1 putative interacting proteins by co-immunoprecipitation assays and enrichment analysis, we found that MoHrd1 is involved in the secretory pathway, energy synthesis, and metabolism. Taken together, our results suggest that MoHrd1 is conserved among fungi and play an important role in cellular metabolism and infection-related development. Our finding helps uncover the mechanism of Hrd1-involved ERAD pathway in fungi and sheds a new light to understand the pathogenic mechanism of

Indexed as

endoplasmic reticulum–associated degradation (ERAD)Magnaporthe oryzaemass spectrometrythe ubiquitin ligase Hrd1

Identifiers

PMID30559593
PMCPMC6291861
OpenAlexW2904529581

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.