Evidence map›Paper›PMID 11827162›Full record

ArticleMolecular and cellular biochemistry2001

Distinctive features of plant protein kinase CK2.

M Riera, G Peracchia, M Pagès

Abstract read
PubMed
In one paragraph

Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

10 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Specific characteristics of CK2β regulatory subunits in plants.Molecular and cellular biochemistry · 2011
    Article
  6. CK2α is essential for embryonic morphogenesis.Molecular and cellular biochemistry · 2011
    Article
  7. Article
  8. Article
  9. Article
  10. 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

3 authors at 1 institution in 1 country.

M RieraDepartament de Genètica Molecular, Institut de Biologia Molecular de Barcelona, Centre d'Investigació i Desenvolupament, C.S.I.C., Spain.
G Peracchia
M Pagès
Institut de Biologia Molecular de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, protein kinase CK2 is involved in different processes that control many aspects of metabolism and development. In mammals and yeast the enzyme is a heterotetramer composed of two types of subunits. During years the subunit composition of the maize protein kinase CK2 enzyme has been a source of controversy. We have recently characterized the maize holoenzyme subunits. Our results show that multiple catalytic and regulatory subunits are expressed in maize and are able to specifically interact with other alpha and beta subunits suggesting a high level of heterogeneity in the typical heterotetrameric structure. Here, we summarize data available on plant CK2 enzymes, in order to clarify the distinctive features and functions of plant protein kinase CK2.

Indexed as

Amino Acid SequenceCasein Kinase IICatalytic DomainDimerizationDNA, ComplementaryGene LibraryHumansModels, BiologicalMolecular Sequence DataPlantsProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiaeSequence Homology, Amino AcidTwo-Hybrid System TechniquesZea maysCasein Kinase IIDNA, ComplementaryProtein Serine-Threonine Kinases

Identifiers

PMID11827162
OpenAlexW1550919387

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.