Evidence map›Paper›PMID 10590166›Full record

ArticleThe Plant cell1999

Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis.

J Shi, K N Kim, O Ritz, V Albrecht, R Gupta, K Harter, S Luan, J Kudla

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed, 1 pooled it
12.7field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 1 synthesis or guideline pooled it, 308 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Genome-Wide Identification of Members of the SoybeanPlants (Basel, Switzerland) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Genome-Wide Identification, Characterization and Expression Analysis of theInternational journal of molecular sciences · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. The CBL-CIPK Pathway in Plant Response to Stress Signals.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. Frontiers in plant science · 2020
    Article

51 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

J ShiDepartment of Plant and Microbial Biology, University of California, Berkeley, California 94720, USA.
K N Kim
O Ritz
V Albrecht
R Gupta
K Harter
S Luan
J Kudla
University of California, Berkeley · USUniversität Ulm · DEUniversity of Freiburg · DE

Funding

IMMUNOPHILINS AND THEIR FUNCTION IN HIGHER PLANTSR29GM052826 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI LUAN, SHENG · 1995 to 1999
–
NIGMS NIH HHS GM52826
6 · The paper itself

Abstract

Members of the Arabidopsis calcineurin B-like Ca(2)+ binding protein (AtCBL) family are differentially regulated by stress conditions. One AtCBL plays a role in salt stress; another is implicated in response to other stress signals, including drought, cold, and wounding. In this study, we identified a group of novel protein kinases specifically associated with AtCBL-type Ca(2)+ sensors. In addition to a typical protein kinase domain, they all contain a unique C-terminal region that is both required and sufficient for interaction with the AtCBL-type but not calmodulin-type Ca(2)+ binding proteins from plants. Interactions between the kinases and AtCBLs require micromolar concentrations of Ca(2)+, suggesting that increases in cellular Ca(2)+ concentrations may trigger the formation of AtCBL-kinase complexes in vivo. Unlike most serine/threonine kinases, the AtCBL-interacting kinase efficiently uses Mn(2)+ to Mg(2)+ as a cofactor and may function as a Mn(2)+ binding protein in the cell. These findings link a new type of Ca(2)+ sensors to a group of novel protein kinases, providing the molecular basis for a unique Ca(2)+ signaling machinery in plant cells.

Indexed as

Arabidopsis ProteinsAmino Acid SequenceArabidopsisBinding SitesCalcineurinCalciumCalcium-Binding ProteinsCalcium SignalingMolecular Sequence DataPhosphorylationProtein KinasesRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidArabidopsis ProteinsCalcineurinCalciumCalcium-Binding ProteinsCBL protein, ArabidopsisProtein KinasesRecombinant Proteins

Identifiers

PMID10590166
PMCPMC144142
OpenAlexW2115595638

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.