Evidence map›Paper›PMID 22694836›Full record

ReviewTrends in plant science2012

ABC1K atypical kinases in plants: filling the organellar kinase void.

Peter K Lundquist, Jerrold I Davis, Klaas J van Wijk

Abstract readReview
In one paragraph

Review in Trends in plant science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 72 citations in OpenAlex.

  1. Plant-fungi interactions inProceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Coenzyme Q biochemistry and biosynthesis.Trends in biochemical sciences · 2023
    Review
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  10. Bean and Pea Plastoglobules Change in Response to Chilling Stress.International journal of molecular sciences · 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

3 authors at 1 institution in 1 country.

Peter K LundquistDepartment of Plant Biology, Cornell University, Ithaca, NY 14853, USA.
Jerrold I Davis
Klaas J van Wijk
Cornell University · US

Funding

CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
NIGMS NIH HHS 5T32GM008500NIGMS NIH HHS T32 GM008500
6 · The paper itself

Abstract

Surprisingly few protein kinases have been demonstrated in chloroplasts or mitochondria. Here, we discuss the activity of bc(1) complex kinase (ABC1K) protein family, which we suggest locate in mitochondria and plastids, thus filling the kinase void. The ABC1Ks are atypical protein kinases and their ancestral function is the regulation of quinone synthesis. ABC1Ks have proliferated from one or two members in non-photosynthetic organisms to more than 16 members in algae and higher plants. In this review, we reconstruct the evolutionary history of the ABC1K family, provide a functional domain analysis for angiosperms and a nomenclature for ABC1Ks in Arabidopsis (Arabidopsis thaliana), rice (Oryza sativa) and maize (Zea mays). Finally, we hypothesize that targets of ABC1Ks include enzymes of prenyl-lipid metabolism as well as components of the organellar gene expression machineries.

Indexed as

Amino Acid MotifsBenzoquinonesEvolution, MolecularGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMagnoliopsidaMitochondriaMultigene FamilyPhylogenyPlant ProteinsPlastidsProtein KinasesProtein Structure, TertiaryYeastsBenzoquinonesPlant ProteinsProtein Kinasesquinone

Identifiers

PMID22694836
PMCPMC3926664
OpenAlexW2007958560

What OpenQuestion holds

Textmetadata
LicenceTDM
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.