Evidence map›Paper›PMID 24713697›Full record

ArticleThe Journal of biological chemistry2014

Neurogranin alters the structure and calcium binding properties of calmodulin.

Laurel Hoffman, Anuja Chandrasekar, Xu Wang, John A Putkey, M Neal Waxham

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 13% 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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Neurogranin Promotes Neuronal Maturation and Network Activity Through CaInternational journal of molecular sciences · 2026
    Article
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  6. Review
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  19. Physiologically Relevant Free CaJournal of molecular biology · 2021
    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

5 authors at 1 institution in 1 country.

Laurel HoffmanFrom the Departments of Neurobiology and Anatomy and.
Anuja ChandrasekarFrom the Departments of Neurobiology and Anatomy and.
Xu WangBiochemistry and Molecular Biology, University of Texas Medical School at Houston, Houston, Texas 77030.
John A PutkeyBiochemistry and Molecular Biology, University of Texas Medical School at Houston, Houston, Texas 77030.
M Neal WaxhamFrom the Departments of Neurobiology and Anatomy and m.n.waxham@uth.tmc.edu.
Institute of Neurobiology · BG

Funding

Principles for Tuning Target Selectivity in Signaling ProteinsR01GM097553 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHEUNG, MARGARET SHUN · 2011 to 2022
$2.7M
Regulators of Calcium SignalingR01GM104290 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PUTKEY, JOHN ANTHONY · 2013 to 2016
$1.2M
NIGMS NIH HHS GM097553NIGMS NIH HHS GM104290NIGMS NIH HHS R01 GM097553NIGMS NIH HHS R01 GM104290
6 · The paper itself

Abstract

Neurogranin (Ng) is a member of the IQ motif class of calmodulin (CaM)-binding proteins, and interactions with CaM are its only known biological function. In this report we demonstrate that the binding affinity of Ng for CaM is weakened by Ca(2+) but to a lesser extent (2-3-fold) than that previously suggested from qualitative observations. We also show that Ng induced a >10-fold decrease in the affinity of Ca(2+) binding to the C-terminal domain of CaM with an associated increase in the Ca(2+) dissociation rate. We also discovered a modest, but potentially important, increase in the cooperativity in Ca(2+) binding to the C-lobe of CaM in the presence of Ng, thus sharpening the threshold for the C-domain to become Ca(2+)-saturated. Domain mapping using synthetic peptides indicated that the IQ motif of Ng is a poor mimetic of the intact protein and that the acidic sequence just N-terminal to the IQ motif plays an important role in reproducing Ng-mediated decreases in the Ca(2+) binding affinity of CaM. Using NMR, full-length Ng was shown to make contacts largely with residues in the C-domain of CaM, although contacts were also detected in residues in the N-terminal domain. Together, our results can be consolidated into a model where Ng contacts residues in the N- and C-lobes of both apo- and Ca(2+)-bound CaM and that although Ca(2+) binding weakens Ng interactions with CaM, the most dramatic biochemical effect is the impact of Ng on Ca(2+) binding to the C-terminal lobe of CaM.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding, CompetitiveBinding SitesBlotting, WesternCalciumCalmodulinCalorimetryHumansKineticsMagnetic Resonance SpectroscopyMolecular Sequence DataNeurograninProtein BindingCalciumCalmodulinNeurograninCalciumCalmodulinCell SignalingIntrinsically Disordered ProteinsIsothermal Titration CalorimetryKineticsNuclear Magnetic ResonanceProtein-Protein InteractionsProtein StructureSignal Transduction

Identifiers

PMID24713697
PMCPMC4031520
OpenAlexW2054856526

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.