Evidence map›Paper›PMID 29361797›Full record

ArticleMolecules (Basel, Switzerland)2018

Biochemical Analysis of the Role of Leucine-Rich Repeat Receptor-Like Kinases and the Carboxy-Terminus of Receptor Kinases in Regulating Kinase Activity in Arabidopsis thaliana and Brassica oleracea.

Eun-Seok Oh, Yeon Lee, Won Byoung Chae, Jana Jeevan Rameneni, Yong-Soon Park, Yong Pyo Lim, Man-Ho Oh

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 17% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. The Receptor-Like KinaseInternational journal of molecular sciences · 2021
    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

7 authors at 2 institutions in 1 country.

Eun-Seok OhDepartment of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 34134, Korea. oes0318@naver.com.
Yeon LeeDepartment of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 34134, Korea. yeonlee@cnu.ac.kr.
Won Byoung ChaeVegetable Research Division, National Institute of Horticultural and Herbal Science, RDA, Wanju 55365, Korea. chaeddang@korea.kr.
Jana Jeevan RameneniDepartment of Horticulture, College of Agriculture and Life Science, Chungnam National University, Daejeon 34134, Korea. saijeevan7@gmail.com.
Yong-Soon ParkDepartment of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 34134, Korea. yspark2005@gmail.com.
Yong Pyo LimDepartment of Horticulture, College of Agriculture and Life Science, Chungnam National University, Daejeon 34134, Korea. yplim@cnu.ac.kr.
Man-Ho OhDepartment of Biological Sciences, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 34134, Korea. manhooh@cnu.ac.kr.ORCID 0000-0002-6524-3252
Chungnam National University · KRRural Development Administration · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein post-translational modification by phosphorylation is essential for the activity and stability of proteins in higher plants and underlies their responses to diverse stimuli. There are more than 300 leucine-rich repeat receptor-like kinases (LRR-RLKs), a major group of receptor-like kinases (RLKs) that plays an important role in growth, development, and biotic stress responses in higher plants. To analyze auto- and transphosphorylation patterns and kinase activities in vitro, 43 full-length complementary DNA (cDNA) sequences were cloned from genes encoding LRR-RLKs. Autophosphorylation activity was found in the cytoplasmic domains (CDs) of 18 LRR-RLKs; 13 of these LRR-RLKs with autophosphorylation activity showed transphosphorylation in

Indexed as

Protein Interaction Domains and MotifsAmino Acid SequenceArabidopsisArabidopsis ProteinsBrassicaComputational BiologyMembrane ProteinsMutationPhosphorylationPhylogenyProtein Serine-Threonine KinasesRecombinant Fusion ProteinsArabidopsis ProteinsAT3g23750 protein, ArabidopsisMembrane ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsArabidopsis thalianaBrassica oleraceabrassinosteroidleucine-rich repeat receptor-like kinasesphosphorylation

Identifiers

PMID29361797
PMCPMC6017770
OpenAlexW2788789874

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.