Evidence map›Paper›PMID 12160464›Full record

ArticleThe Biochemical journal2002

Molecular and biochemical characterization of a calcium/calmodulin-binding protein kinase from rice.

Lei Zhang, Bi-Feng Liu, Shuping Liang, Russell L Jones, Ying-Tang Lu

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Genome-Wide Investigation ofInternational journal of molecular sciences · 2025
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  3. Review
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  6. Article
  7. Activation of CaMKIIδA promotes CaActa pharmacologica Sinica · 2018
    Article
  8. Article
  9. Functional Analysis of theInternational journal of molecular sciences · 2018
    Article
  10. Article
  11. Review
  12. Article
  13. Review
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  15. Article
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Lei ZhangThe Key Lab of MOE for Plant Developmental Biology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Bi-Feng Liu
Shuping Liang
Russell L Jones
Ying-Tang Lu
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A Ca2+/calmodulin (CaM)-binding protein kinase from rice ( Oryza sativa ), OsCBK, has been characterized that lacks Ca2+-binding EF hands and has Ca2+/CaM-independent autophosphorylation and substrate-phosphorylation activity. OsCBK has all 11 subdomains of a kinase catalytic domain and a putative CaM-binding domain, and shares high identity with Ca2+-dependent-protein-kinase ('CDPK')-related protein kinases in plants. OsCBK bound CaM in a Ca2+-dependent manner as previously reported for Ca2+/calmodulin-dependent protein kinases in animals, but autophosphorylation and phosphorylation of histone IIIs were Ca2+/CaM-independent. Surface plasmon resonance analysis showed that OsCBK specifically bound CaM with high affinity ( K (D)=30 nM). Capillary electrophoresis showed that phosphorylation of OsCBK occurred on serine and threonine residues. These data show that OsCBK is a serine/threonine protein kinase that binds Ca2+/CaM, but whose enzymic activity is independent of Ca2+/CaM. In situ hybridization showed that OsCBK is expressed in reproductive and vegetative tissues of rice and shows temporal and spatial changes during plant growth and development. OsCBK is highly expressed in zones of cell division and it is particularly abundant in sporogenous cells of the anther at meiosis.

Indexed as

Amino Acid SequenceBase SequenceCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCloning, MolecularDNA, ComplementaryDNA, PlantHydrogen-Ion ConcentrationMagnesiumMolecular Sequence DataOryzaPhosphorylationProtein Structure, TertiarySaltsSequence Homology, Amino AcidCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinDNA, ComplementaryDNA, PlantMagnesiumSalts

Identifiers

PMID12160464
PMCPMC1222965
OpenAlexW2038021289

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.