Evidence map›Paper›PMID 15840729›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Scanning the human proteome for calmodulin-binding proteins.

Xinchun Shen, C Alexander Valencia, Jack W Szostak, Jack Szostak, Biao Dong, Rihe Liu

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
–field-weighted citation impact
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

89 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. CaBiomolecules · 2023
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Calmodulin inMicroorganisms · 2022
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. How Functional Genomics Can Keep Pace With VUS Identification.Frontiers in cardiovascular medicine · 2022
    Review

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

4 · The record

Corrections and comments

  • Erratum issued
    Szostak, Jack [corrected to Szostak, Jack W]
5 · Who and what money

Authors and funding

6 authors.

Xinchun ShenDivision of Medicinal Chemistry and Natural Products, School of Pharmacy, and Carolina Center for Genome Sciences, University of North Carolina, Chapel Hill, NC 27599, USA.
C Alexander Valencia
Jack W Szostak
Jack Szostak
Biao Dong
Rihe Liu

Funding

IN VITRO SELECTION AND EVOLUTION OF NEW RIBOZYMESR01GM053936 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI SZOSTAK, JACK W · 1996 to 2003
$864k
NIGMS NIH HHS GM53936NIGMS NIH HHS R01 GM053936
6 · The paper itself

Abstract

The calcium ion (Ca(2+)) is a ubiquitous second messenger that is crucial for the regulation of a wide variety of cellular processes. The diverse transient signals transduced by Ca(2+) are mediated by intracellular Ca(2+)-binding proteins, also known as Ca(2+) sensors. A key obstacle to studying many Ca(2+)-sensing proteins is the difficulty in identifying the numerous downstream target interactions that respond to Ca(2+)-induced conformational changes. Among a number of Ca(2+) sensors in the eukaryotic cell, calmodulin (CaM) is the most widespread and the best studied. Employing the mRNA display technique, we have scanned the human proteome for CaM-binding proteins and have identified and characterized a large number of both known and previously uncharacterized proteins that interact with CaM in a Ca(2+)-dependent manner. The interactions of several identified proteins with Ca(2+)/CaM were confirmed by using pull-down assays and coimmunoprecipitation. Many of the CaM-binding proteins identified belong to protein families such as the DEAD/H box proteins, ribosomal proteins, proteasome 26S subunits, and deubiquitinating enzymes, suggesting the possible involvement of Ca(2+)/CaM in different signaling pathways. The selection method described herein could be used to identify the binding partners of other calcium sensors on the proteome-wide scale.

Indexed as

Binding SitesCalmodulin-Binding ProteinsCloning, MolecularHeLa CellsHumansProteomeCalmodulin-Binding ProteinsProteome

Identifiers

PMID15840729
PMCPMC1087907

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.