Evidence map›Paper›PMID 19081058›Full record

ArticleStructure (London, England : 1993)2008

Structural basis for calcium sensing by GCaMP2.

Qi Wang, Bo Shui, Michael I Kotlikoff, Holger Sondermann

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

92 citing papers in PubMed, 176 citations in OpenAlex.

  1. Guidelines for evaluating endothelial function in vascular tissue.American journal of physiology. Heart and circulatory physiology · 2026
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  5. State-dependent motion of a genetically encoded fluorescent biosensor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Review
  8. Review
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  10. Article
  11. A blue-shifted genetically encoded CabioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

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

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.

Qi WangDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Bo Shui
Michael I Kotlikoff
Holger Sondermann
Cornell University · US

Funding

Smooth Muscle Ca Release in RYR and FKBP transgenic miceR01HL045239 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI KOTLIKOFF, MICHAEL I. · 1990 to 2006
$2.2M
Transgenic Mice- Recomb., Fate-Mapping,and Ca2+signalingR01DK065992 · NIDDK · CORNELL UNIVERSITY ITHACA · PI KOTLIKOFF, MICHAEL I. · 2004 to 2008
$1.9M
RNA Aptamers to Green Fluorescent Protein for Cell ImagingR21EB006782 · NIBIB · CORNELL UNIVERSITY · PI KOTLIKOFF, MICHAEL I. · 2007 to 2008
$419k
NHLBI NIH HHS HL45239NHLBI NIH HHS R01 HL045239NIBIB NIH HHS EB006782NIBIB NIH HHS R21 EB006782NIDDK NIH HHS DK65992NIDDK NIH HHS R01 DK065992
6 · The paper itself

Abstract

Genetically encoded Ca(2+) indicators are important tools that enable the measurement of Ca(2+) dynamics in a physiologically relevant context. GCaMP2, one of the most robust indicators, is a circularly permutated EGFP (cpEGFP)/M13/calmodulin (CaM) fusion protein that has been successfully used for studying Ca(2+) fluxes in vivo in the heart and vasculature of transgenic mice. Here we describe crystal structures of bright and dim states of GCaMP2 that reveal a sophisticated molecular mechanism for Ca(2+) sensing. In the bright state, CaM stabilizes the fluorophore in an ionized state similar to that observed in EGFP. Mutational analysis confirmed critical interactions between the fluorophore and elements of the fused peptides. Solution scattering studies indicate that the Ca(2+)-free form of GCaMP2 is a compact, predocked state, suggesting a molecular basis for the relatively rapid signaling kinetics reported for this indicator. These studies provide a structural basis for the rational design of improved Ca(2+)-sensitive probes.

Indexed as

Calcium SignalingCalmodulinCrystallizationCrystallography, X-RayFluorescent DyesGreen Fluorescent ProteinsHydrogen BondingKineticsLightModels, MolecularMyosin Light ChainsProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsScattering, Small AngleCalmodulinFluorescent DyesGreen Fluorescent ProteinsMyosin Light ChainsRecombinant Fusion ProteinsWater

Identifiers

PMID19081058
PMCPMC2614139
OpenAlexW2010694064

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.