Evidence map›Paper›PMID 25159857›Full record

ReviewCell calcium2014

Toward a high-resolution structure of IP₃R channel.

Irina I Serysheva

Open access · greenAbstract readReview
In one paragraph

Review in Cell calcium, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Wound Repair and CaCells · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. MERCs. The Novel Assistant to Neurotransmission?Frontiers in neuroscience · 2020
    Review
  14. IPCellular and molecular life sciences : CMLS · 2017
    Review
  15. Structure of IPCurrent opinion in structural biology · 2017
    Review
  16. Review
  17. Review
  18. Article
  19. Regulation of cardiomyocyte autophagy by calcium.American journal of physiology. Endocrinology and metabolism · 2016
    Review
  20. Coupling all-atom molecular dynamics simulations of ions in water with Brownian dynamics.Proceedings. Mathematical, physical, and engineering sciences · 2016
    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

1 author at 1 institution in 1 country.

Irina I SeryshevaDepartment of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston, 6431 Fannin Street, Houston, TX 77030, USA. Electronic address: irina.i.serysheva@uth.tmc.edu.
The University of Texas Health Science Center at Houston · US

Funding

Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
Structure-Function Studies Of IP3R ChannelsR01GM072804 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SERYSHEVA, IRINA I · 2005 to 2023
$4.8M
Structural Studies of RyR ChannelR21AR063255 · NIAMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SERYSHEVA, IRINA I · 2013 to 2014
$368k
NIAMS NIH HHS R21 AR063255NIAMS NIH HHS R21AR063255NIGMS NIH HHS R01 GM072804NIGMS NIH HHS R01GM072804NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01GM079429
6 · The paper itself

Abstract

The ability of cells to maintain low levels of Ca(2+) under resting conditions and to create rapid and transient increases in Ca(2+) upon stimulation is a fundamental property of cellular Ca(2+) signaling mechanism. An increase of cytosolic Ca(2+) level in response to diverse stimuli is largely accounted for by the inositol 1,4,5-trisphosphate receptor (IP3R) present in the endoplasmic reticulum membranes of virtually all eukaryotic cells. Extensive information is currently available on the function of IP3Rs and their interaction with modulators. Very little, however, is known about their molecular architecture and therefore most critical issues surrounding gating of IP3R channels are still ambiguous, including the central question of how opening of the IP3R pore is initiated by IP3 and Ca(2+). Membrane proteins such as IP3R channels have proven to be exceptionally difficult targets for structural analysis due to their large size, their location in the membrane environment, and their dynamic nature. To date, a 3D structure of complete IP3R channel is determined by single-particle cryo-EM at intermediate resolution, and the best crystal structures of IP3R are limited to a soluble portion of the cytoplasmic region representing ∼15% of the entire channel protein. Together these efforts provide the important structural information for this class of ion channels and serve as the basis for further studies aiming at understanding of the IP3R function.

Indexed as

AnimalsCalciumHumansInositol 1,4,5-Trisphosphate ReceptorsIon Channel GatingProtein ConformationSignal TransductionCalciumInositol 1,4,5-Trisphosphate Receptors3D structureCalcium signalingElectron cryomicroscopyIP(3)RSingle-particle reconstruction

Identifiers

PMID25159857
PMCPMC4162860
OpenAlexW2066425541

What OpenQuestion holds

Textmetadata
LicenceTDM
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.