ArticleStructure (London, England : 1993)2011
Flexible architecture of IP3R1 by Cryo-EM.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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.
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.
Who cites it
50 citing papers in PubMed, 80 citations in OpenAlex.
- Understanding IPCell calcium · 2023Review
- Conformational motions and ligand-binding underlying gating and regulation in IPNature communications · 2022Article
- Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- High value-added application of a renewable bioresource as acaricide: Investigation the mechanism of action of scoparone againstJournal of advanced research · 2022Article
- Communications between Mitochondria and Endoplasmic Reticulum in the Regulation of Metabolic Homeostasis.Cells · 2021Review
- A Comparative Perspective on Functionally-Related, Intracellular Calcium Channels: The Insect Ryanodine and Inositol 1,4,5-Trisphosphate Receptors.Biomolecules · 2021Review
- Cryo-EM structure of type 1 IPCommunications biology · 2021Article
- Allosteric response to ligand binding: Molecular dynamics study of the N-terminal domains in IPBiophysics and physicobiology · 2019Article
- Cryo-EM reveals ligand induced allostery underlying InsPCell research · 2018Article
- Membrane protein structural biology in the era of single particle cryo-EM.Current opinion in structural biology · 2018Review
- Article
- PLC and IPThe Journal of general physiology · 2018Article
- Endoplasmic Reticulum-Mitochondrial Contactology: Structure and Signaling Functions.Trends in cell biology · 2018Review
- Article
- Single-particle cryo-EM-Improved ab initio 3D reconstruction with SIMPLE/PRIME.Protein science : a publication of the Protein Society · 2018Article
- IPCellular and molecular life sciences : CMLS · 2017Review
- Structure of IPCurrent opinion in structural biology · 2017Review
- IPProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crystal structures of the TRIC trimeric intracellular cation channel orthologues.Cell research · 2016Article
- Synthesis of dimeric analogs of adenophostin A that potently evoke CaRSC advances · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Inositol 1,4,5-trisphosphate receptors (IP3Rs) play a fundamental role in generating Ca2+ signals that trigger many cellular processes in virtually all eukaryotic cells. Thus far, the three-dimensional (3D) structure of these channels has remained extremely controversial. Here, we report a subnanometer resolution electron cryomicroscopy (cryo-EM) structure of a fully functional type 1 IP3R from cerebellum in the closed state. The transmembrane region reveals a twisted bundle of four α helices, one from each subunit, that form a funnel shaped structure around the 4-fold symmetry axis, strikingly similar to the ion-conduction pore of K+ channels. The lumenal face of IP3R1 has prominent densities that surround the pore entrance and similar to the highly structured turrets of Kir channels. 3D statistical analysis of the cryo-EM density map identifies high variance in the cytoplasmic region. This structural variation could be attributed to genuine structural flexibility of IP3R1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.