Evidence map›Paper›PMID 25643035›Full record

ArticlePloS one2015

N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interaction.

Giuliana Papoff, Nadia Trivieri, Sonia Marsilio, Roberta Crielesi, Cristiana Lalli, Loriana Castellani, Edward M Balog, Giovina Ruberti

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

8 authors at 3 institutions in 2 countries.

Giuliana PapoffNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
Nadia TrivieriNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
Sonia MarsilioNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
Roberta CrielesiNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
Cristiana LalliNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
Loriana CastellaniNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy; Department of Human Sciences, Society and Health, University of Cassino, Cassino, Italy.
Edward M BalogSchool of Applied Physiology, Georgia Institute of Technology, Atlanta, Georgia, United States of America.
Giovina RubertiNational Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
National Research Council · ITInstitute of Cell Biology and Neurobiology · ITGeorgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FADD (Fas-associated death domain) and TRADD (Tumor Necrosis Factor Receptor 1-associated death domain) proteins are important regulators of cell fate in mammalian cells. They are both involved in death receptors mediated signaling pathways and have been linked to the Toll-like receptor family and innate immunity. Here we identify and characterize by database search analysis, mutagenesis and calmodulin (CaM) pull-down assays a calcium-dependent CaM binding site in the α-helices 1-2 of TRADD death domain. We also show that oxidation of CaM methionines drastically reduces CaM affinity for FADD and TRADD suggesting that oxidation might regulate CaM-FADD and CaM-TRADD interactions. Finally, using Met-to-Leu CaM mutants and binding assays we show that both the N- and C-terminal domains of CaM are important for binding.

Indexed as

Amino Acid SequenceBinding SitesCalciumCalmodulinCell LineFas-Associated Death Domain ProteinHumansMethionineMethionine Sulfoxide ReductasesMolecular Sequence DataMutationOxidation-ReductionProtein BindingProtein Structure, TertiaryTNF Receptor-Associated Death Domain ProteinCalciumCalmodulinFADD protein, humanFas-Associated Death Domain ProteinMethioninemethionine sulfoxide reductaseMethionine Sulfoxide ReductasesTNF Receptor-Associated Death Domain Protein

Identifiers

PMID25643035
PMCPMC4313936
OpenAlexW2062383639

What OpenQuestion holds

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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.