Evidence map›Paper›PMID 32312753›Full record

ArticleThe Journal of biological chemistry2020

The acetyltransferase Eco1 elicits cohesin dimerization during S phase.

Di Shi, Shuaijun Zhao, Mei-Qing Zuo, Jingjing Zhang, Wenya Hou, Meng-Qiu Dong, Qinhong Cao, Huiqiang Lou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Role of chromosomal cohesion and separation in aneuploidy and tumorigenesis.Cellular and molecular life sciences : CMLS · 2024
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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

8 authors at 2 institutions in 1 country.

Di ShiState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China.
Shuaijun ZhaoState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China.
Mei-Qing ZuoNational Institute of Biological Sciences, Beijing 102206, China.
Jingjing ZhangState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China.
Wenya HouState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing 102206, China.ORCID 0000-0002-6094-1182
Qinhong CaoState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China.
Huiqiang LouState Key Laboratory of Agro-Biotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, No. 2 Yuan-Ming-Yuan West Road, Beijing 100193, China lou@cau.edu.cn.
China Agricultural University · CNNational Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cohesin is a DNA-associated protein complex that forms a tripartite ring controlling sister chromatid cohesion, chromosome segregation and organization, DNA replication, and gene expression. Sister chromatid cohesion is established by the protein acetyltransferase Eco1, which acetylates two conserved lysine residues on the cohesin subunit Smc3 and thereby ensures correct chromatid separation in yeast (

Indexed as

AcetyltransferasesCell Cycle ProteinsChromatidsChromosomal Proteins, Non-HistoneChromosomes, FungalCohesinsHistone DemethylasesHumansNuclear ProteinsProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsS PhaseAcetyltransferasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsECO1 protein, S cerevisiaeHistone DemethylasesHOS1 protein, S cerevisiaeIRR1 protein, S cerevisiaeMCD1 protein, S cerevisiaeNuclear ProteinsRAD61 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsacetylationacetyltransferasecell cyclechromatid cohesioncohesindimerizationDNA replicationdouble ring modelEco1protein acetylationself-interaction

Identifiers

PMID32312753
PMCPMC7261783
OpenAlexW3016762722

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.