Evidence map›Paper›PMID 22973849›Full record

ArticleProtein and peptide letters2013

Functional and structural analysis of the conserved EFhd2 protein.

Yancy Ferrer-Acosta, Eva N Rodríguez Cruz, Ana del C Vaquer, Irving E Vega

Abstract read
In one paragraph

Article in Protein and peptide letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Getting cells into shape by calcium-dependent actin cross-linking proteins.Frontiers in cell and developmental biology · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. EFhd2 Affects Tau Liquid-Liquid Phase Separation.Frontiers in neuroscience · 2019
    Article
  13. Article
  14. Structural implications of CaScientific reports · 2016
    Article
  15. Review
  16. Review
  17. Article
  18. Cdk5 phosphorylation of EFhd2 at S74 affects its calcium binding activity.Protein science : a publication of the Protein Society · 2014
    Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Yancy Ferrer-AcostaDepartment of Biology, University of Puerto Rico-Rio Piedras Campus, San Juan, PR 00931, USA.
Eva N Rodríguez Cruz
Ana del C Vaquer
Irving E Vega
University of Puerto Rico at Río Piedras · PR

Funding

Upgrade Laboratories Facilities at UPR-Rio PiedrasR25GM061151 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI CARBALLEIRA, NESTOR MANUEL · 2001 to 2023
$32.5M
RIO PIEDRAS MARC U*STAR DEVELOPMENT PROGRAMT34GM007821 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI CARBALLEIRA, NESTOR MANUEL · 1985 to 2020
$20.3M
The role of a novel tau-associated protein in neurodegenerationSC1NS066988 · NINDS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI VEGA, IRVING E · 2009 to 2012
$972k
NIGMS NIH HHS 5R25GM061151NIGMS NIH HHS 5T34GM007821NIGMS NIH HHS R25 GM061151NIGMS NIH HHS T34 GM007821NINDS NIH HHS 1SC1NS066988NINDS NIH HHS SC1 NS066988
6 · The paper itself

Abstract

EFhd2 is a novel protein conserved from C. elegans to H. sapiens. This novel protein was originally identified in cells of the immune and central nervous systems. However, it is most abundant in the central nervous system, where it has been found associated with pathological forms of the microtubule-associated protein tau. The physiological or pathological roles of EFhd2 are poorly understood. In this study, a functional and structural analysis was carried to characterize the molecular requirements for EFhd2's calcium binding activity. The results showed that mutations of a conserved aspartate on either EF-hand motif disrupted the calcium binding activity, indicating that these motifs work in pair as a functional calcium binding domain. Furthermore, characterization of an identified single-nucleotide polymorphisms (SNP) that introduced a missense mutation indicates the importance of a conserved phenylalanine on EFhd2 calcium binding activity. Structural analysis revealed that EFhd2 is predominantly composed of alpha helix and random coil structures and that this novel protein is thermostable. EFhd2's thermo stability depends on its N-terminus. In the absence of the N-terminus, calcium binding restored EFhd2's thermal stability. Overall, these studies contribute to our understanding on EFhd2 functional and structural properties, and introduce it into the family of canonical EF-hand domain containing proteins.

Indexed as

Amino Acid SequenceAnimalsCalciumCalcium-Binding ProteinsHumansMiceModels, MolecularMolecular Sequence DataMutation, MissensePolymorphism, Single NucleotideProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSequence AlignmentCalciumCalcium-Binding ProteinsEFHD2 protein, mouseRecombinant Proteins

Identifiers

PMID22973849
PMCPMC3633529
OpenAlexW1997214903

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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.