Evidence map›Paper›PMID 29475950›Full record

ArticleThe Journal of biological chemistry2018

A chemical genetic approach to engineer phototropin kinases for substrate labeling.

Jonathan Schnabel, Peter Hombach, Thomas Waksman, Giovanni Giuriani, Jan Petersen, John M Christie

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. 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
2.4field-weighted citation impact, top 11% 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, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. CIPK23 regulates blue light-dependent stomatal opening in Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2020
    Article
  9. The continuing arc toward phototropic enlightenment.Journal of experimental botany · 2020
    Article
  10. Review
  11. 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

6 authors at 1 institution in 2 countries.

Jonathan SchnabelFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and.
Peter HombachFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and.
Thomas WaksmanFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and.
Giovanni GiurianiFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and.
Jan PetersenFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and.
John M ChristieFrom the Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom and john.christie@glasgow.ac.uk.
University of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J016047/1Biotechnology and Biological Sciences Research Council BB/M002128/1
6 · The paper itself

Abstract

Protein kinases (PKs) control many aspects of plant physiology by regulating signaling networks through protein phosphorylation. Phototropins (phots) are plasma membrane-associated serine/threonine PKs that control a range of physiological processes that collectively serve to optimize photosynthetic efficiency in plants. These include phototropism, leaf positioning and flattening, chloroplast movement, and stomatal opening. Despite their identification over two decades ago, only a handful of substrates have been identified for these PKs. Progress in this area has been hampered by the lack of a convenient means to confirm the identity of potential substrate candidates. Here we demonstrate that the kinase domain of

Indexed as

Amino Acid SubstitutionArabidopsisArabidopsis ProteinsMutation, MissensePhosphoproteinsStaining and LabelingAdenosine TriphosphateProtein DomainsProtein Serine-Threonine KinasesAdenosine TriphosphateArabidopsis ProteinsNPH1 protein, ArabidopsisPhosphoproteinsPHOT2 protein, ArabidopsisProtein Serine-Threonine KinasesArabidopsisATPchemical geneticsgatekeeperphotobiologyphotoreceptorprotein engineeringprotein kinase

Identifiers

PMID29475950
PMCPMC5900772
OpenAlexW2790052416

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.