Evidence map›Paper›PMID 32744250›Full record

ArticleActa crystallographica. Section F, Structural biology communications2020

Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.

Hong Chen, Yanqiong Kong, Jia Chen, Lan Li, Xiushan Li, Feng Yu, Zhenhua Ming

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2020. 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
0.7field-weighted citation impact, top 21% 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. 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 3 institutions in 1 country.

Hong ChenState Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, People's Republic of China.
Yanqiong KongState Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi University, Nanning 530004, People's Republic of China.
Jia ChenState Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, People's Republic of China.
Lan LiState Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, People's Republic of China.
Xiushan LiState Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, People's Republic of China.
Feng YuState Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, People's Republic of China.
Zhenhua MingState Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi University, Nanning 530004, People's Republic of China.
State Key Laboratory of Chemobiosensing and ChemometricsState Key Laboratory For Conservation and Utilization of Subtropical Agro-BioresourcesHunan University · CN

Funding

National Natural Science Foundation of China 31571444National Natural Science Foundation of China 31700052National Natural Science Foundation of China 31871396National Natural Science Foundation of China 31900867State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources SKLCUSA-a201806
6 · The paper itself

Abstract

Transmembrane kinases (TMKs) are members of the plant receptor-like kinase (RLK) family. TMKs are characterized by an extracellular leucine-rich-repeat (LRR) domain, a single transmembrane region and a cytoplasmic kinase domain. TMKs have been shown to act as critical modulators of cell expansion and cell proliferation. Here, the crystal structure of the extracellular domain of TMK3 (TMK3-ECD) was determined to a resolution of 2.06 Å, with an R

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCloning, MolecularCrystallography, X-RayDisulfidesEscherichia coliGene ExpressionGenetic VectorsIsoenzymesModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsArabidopsis ProteinsAT1G66150 protein, ArabidopsisDisulfidesIsoenzymesProtein Serine-Threonine KinasesRecombinant Proteinsextracellular domainLRR-RLKsnon-LRR regionprotein crystallographyTMK3transmembrane kinases

Identifiers

PMID32744250
PMCPMC7397464
OpenAlexW3046606571

What OpenQuestion holds

Textmetadata
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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.