Evidence map›Paper›PMID 28449373›Full record

ArticleJournal of molecular recognition : JMR2017

Biophysical analysis of the dynamics of calmodulin interactions with neurogranin and Ca

Christian Seeger, Vladimir O Talibov, U Helena Danielson

Abstract read
In one paragraph

Article in Journal of molecular recognition : JMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Calcium/Calmodulin-Dependent Serine Protein Kinase (Animals : an open access journal from MDPI · 2023
    Article
  4. Article
  5. Calmodulin as CaInternational journal of molecular sciences · 2021
    Article
  6. Article
  7. 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.

Christian SeegerDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.
Vladimir O TalibovDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.
U Helena DanielsonDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0003-2728-0340

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM) functions depend on interactions with CaM-binding proteins, regulated by Ca2+. Induced structural changes influence the affinity, kinetics, and specificities of the interactions. The dynamics of CaM interactions with neurogranin (Ng) and the CaM-binding region of Ca2+/calmodulin-dependent kinase II (CaMKII

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalmodulinCations, DivalentCattleGene ExpressionHumansKineticsNeurograninProtein BindingProtein Interaction Domains and MotifsProteinsRecombinant ProteinsSequence AlignmentCalciumCalmodulinCAMK2N1 protein, humanCations, DivalentNeurograninProteinsRecombinant Proteinscalmodulincalmodulin-dependent kinasemicroscale thermophoresisneurograninsurface plasmon resonance

Identifiers

PMID28449373
PMCPMC5518211

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.