Evidence map›Paper›PMID 28860196›Full record

ArticleThe Journal of biological chemistry2017

Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from

Olga Otrusinová, Gabriel Demo, Petr Padrta, Zuzana Jaseňáková, Blanka Pekárová, Zuzana Gelová, Agnieszka Szmitkowska, Pavel Kadeřávek, Séverine Jansen, Milan Zachrdla and 8 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. The structure of B-ARR reveals the molecular basis of transcriptional activation by cytokinin.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Modeling of Protein⁻Protein Interactions in Cytokinin Signal Transduction.International journal of molecular sciences · 2019
    Article
  5. Article
  6. 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

18 authors at 3 institutions in 3 countries.

Olga OtrusinováFrom the Central European Institute of Technology and.
Gabriel DemoFrom the Central European Institute of Technology and.
Petr PadrtaFrom the Central European Institute of Technology and.
Zuzana JaseňákováFrom the Central European Institute of Technology and.
Blanka PekárováFrom the Central European Institute of Technology and.
Zuzana GelováFrom the Central European Institute of Technology and.
Agnieszka SzmitkowskaFrom the Central European Institute of Technology and.
Pavel KadeřávekFrom the Central European Institute of Technology and.
Séverine JansenFrom the Central European Institute of Technology and.
Milan ZachrdlaFrom the Central European Institute of Technology and.
Tomáš KlumplerFrom the Central European Institute of Technology and.
Jaromír MarekFrom the Central European Institute of Technology and.
Jozef HritzFrom the Central European Institute of Technology and.
Lubomír JandaFrom the Central European Institute of Technology and.
Hideo Iwaïthe Institute of Biotechnology, University of Helsinki, Viikinkaari 1 (P. O. Box 65), 00014 Helsinki, Finland.
Michaela WimmerováFrom the Central European Institute of Technology and.
Jan HejátkoFrom the Central European Institute of Technology and.
Lukáš ŽídekFrom the Central European Institute of Technology and lzidek@chemi.muni.cz.
Central European Institute of Technology · ATMasaryk University · CZUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multistep phosphorelay (MSP) cascades mediate responses to a wide spectrum of stimuli, including plant hormonal signaling, but several aspects of MSP await elucidation. Here, we provide first insight into the key step of MSP-mediated phosphotransfer in a eukaryotic system, the phosphorylation of the receiver domain of the histidine kinase CYTOKININ-INDEPENDENT 1 (CKI1

Indexed as

ArabidopsisArabidopsis ProteinsCrystallography, X-RayNuclear Magnetic Resonance, BiomolecularProtein DomainsProtein KinasesProtein Structure, SecondaryReceptors, Cell SurfaceArabidopsis ProteinsCKI1 protein, ArabidopsisETR1 protein, ArabidopsisProtein KinasesReceptors, Cell Surfacehistidine kinasenuclear magnetic resonance (NMR)protein dynamicprotein phosphorylationreceiver domainrelaxation dispersionX-ray crystallography

Identifiers

PMID28860196
PMCPMC5655527
OpenAlexW2751303376

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.