Evidence map›Paper›PMID 32088832›Full record

ArticlePlant molecular biology2020

A mutation near the active site of S-RNase causes self-compatibility in S-RNase-based self-incompatible plants.

Yang Li, Junkai Wu, Chuanbao Wu, Jie Yu, Chunsheng Liu, Wenqi Fan, Tianzhong Li, Wei Li

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

7 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  5. Downregulated expression of SHorticulture research · 2021
    Article
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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.

Yang LiLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China.
Junkai WuCollege of Horticulture Science and Technology, Hebei Normal University of Science & Technology, Hebei, China.
Chuanbao WuLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China.
Jie YuLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China.
Chunsheng LiuLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China.
Wenqi FanLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China.
Tianzhong LiLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China. litianzhong1535@163.com.ORCID http://orcid.org/0000-0003-4076-231X
Wei LiLaboratory of Fruit Cell and Molecular Breeding, China Agricultural University, Beijing, 100193, China. Jason870613@126.com.
China Agricultural University · CNHebei Normal University of Science and Technology · CN

Funding

Key Laboratory of Highway Construction and Maintenance Technology in the Loess Region of Shanxi Transportation Research Institute (CN) CEFF-PXM2019_014207_000032Key Programme 31630066National Natural Science Foundation of China 2018YFD1000107
6 · The paper itself

Abstract

key messageThe structurally simplest amino acid glycine could make contribution to nuclease activity of S-RNase and self-incompatibility in S-RNase-based plants. S-RNase is regarded as inhibitor of self-pollen tube in S-RNase-based self-incompatibility plants. Certain residues like histidine are necessary for RNase activity and self-incompatibility; however, it is unknown whether any other residues contribute to this. Previously, we identified an association between the self-compatible Chinese pear (Pyrus × bretschneideri) cultivar 'Yanzhuang' (YZ) and a mutation causing a residue shift (glycine-to-valine) in the 2nd conserved region (C2) of S

Indexed as

Self-Incompatibility in Flowering PlantsCatalytic DomainConserved SequenceGlycineMutationPlant BreedingPollen TubePyrusRibonucleasesGlycineribonuclease SRibonucleasesConserved residuePearRNase activitySelf-compatibilitySNPS-RNase mutation

Identifiers

PMID32088832
OpenAlexW3007694013

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.