Evidence map›Paper›PMID 26264442›Full record

ReviewExperimental biology and medicine (Maywood, N.J.)2016

The neuronal porosome complex in health and disease.

Akshata R Naik, Kenneth T Lewis, Bhanu P Jena

Open access · greenAbstract readReview
In one paragraph

Review in Experimental biology and medicine (Maywood, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Hydrodynamics govern the pre-fusion docking time of synaptic vesicles.Journal of the Royal Society, Interface · 2018
    Article
  3. Fusion Pore: A Curious Case of Rediscovering Science.Discoveries (Craiova, Romania) · 2017
    Article
  4. 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 at 1 institution in 1 country.

Akshata R NaikDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Kenneth T LewisDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Bhanu P JenaDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA bjena@med.wayne.edu.
Wayne State University · US

Funding

UNDERSTANDING MEMBRANE FUSION A BIOENGINEERING APPROACHR01EB000303 · NIBIB · WAYNE STATE UNIVERSITY · PI JENA, BHANU P · 2002 to 2004
$1.2M
EXOCYTOSIS: USING NANOSURGERY AND BIOENGINEERINGR01DK056212 · NIDDK · YALE UNIVERSITY · PI JENA, BHANU P · 1999 to 2003
$1.1M
UNDERSTANDING MEMBRANE FUSION A BIOENGINEERING APPROACHR01NS039918 · NINDS · YALE UNIVERSITY · PI JENA, BHANU P · 2000 to 2001
$791k
NIBIB NIH HHS R01 EB000303NIDDK NIH HHS DK56212,NIDDK NIH HHS R01 DK056212NINDS NIH HHS NS39918NINDS NIH HHS R01 NS039918
6 · The paper itself

Abstract

Cup-shaped secretory portals at the cell plasma membrane called porosomes mediate the precision release of intravesicular material from cells. Membrane-bound secretory vesicles transiently dock and fuse at the base of porosomes facing the cytosol to expel pressurized intravesicular contents from the cell during secretion. The structure, isolation, composition, and functional reconstitution of the neuronal porosome complex have greatly progressed, providing a molecular understanding of its function in health and disease. Neuronal porosomes are 15 nm cup-shaped lipoprotein structures composed of nearly 40 proteins, compared to the 120 nm nuclear pore complex composed of >500 protein molecules. Membrane proteins compose the porosome complex, making it practically impossible to solve its atomic structure. However, atomic force microscopy and small-angle X-ray solution scattering studies have provided three-dimensional structural details of the native neuronal porosome at sub-nanometer resolution, providing insights into the molecular mechanism of its function. The participation of several porosome proteins previously implicated in neurotransmission and neurological disorders, further attest to the crosstalk between porosome proteins and their coordinated involvement in release of neurotransmitter at the synapse.

Indexed as

Synaptic TransmissionAnimalsCell Membrane StructuresHumansMacromolecular SubstancesMembrane ProteinsMicroscopy, Atomic ForceModels, BiologicalNeuronsProtein ConformationScattering, Small AngleMacromolecular SubstancesMembrane Proteinsneuronal diseaseNeuronal porosome complexneurotransmission

Identifiers

PMID26264442
PMCPMC4935393
OpenAlexW1862415835

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.