Evidence map›Paper›PMID 10212491›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences1999

Processing of ARIA and release from isolated nerve terminals.

B Han, G D Fischbach

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 47% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Multiple personalities of neuregulin gene family members.The Journal of comparative neurology · 2004
    Review
  6. Back signaling by the Nrg-1 intracellular domain.The Journal of cell biology · 2003
    Article
  7. Article
  8. Mechanisms of the release of anterogradely transported neurotrophin-3 from axon terminals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  9. The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

2 authors at 1 institution in 1 country.

B HanHarvard Medical School, Department of Neurobiology, Boston, MA 02115, USA.
G D Fischbach
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuromuscular junction is a specialized synapse in that every action potential in the presynaptic nerve terminal results in an action potential in the postsynaptic membrane, unlike most interneuronal synapses where a single presynaptic input makes only a small contribution to the population postsynaptic response. The postsynaptic membrane at the neuromuscular junction contains a high density of neurotransmitter (acetylcholine) receptors and a high density of voltage-gated Na+ channels. Thus, the large acetylcholine activated current occurs at the same site where the threshold for action potential generation is low. Acetylcholine receptor inducing activity (ARIA), a 42 kD protein, that stimulates synthesis of acetylcholine receptors and voltage-gated Na+ channels in cultured myotubes, probably plays the same roles at developing and mature motor endplates in vivo. ARIA is synthesized as part of a larger, transmembrane, precursor protein called proARIA. Delivery of ARIA from motor neuron cell bodies in the spinal cord to the target endplates involves several steps, including proteolytic cleavage of proARIA. ARIA is also expressed in the central nervous system and it is abundant in the molecular layer of the cerebellum. In this paper we describe our first experiments on the processing and release of ARIA from subcellular fractions containing synaptosomes from the chick cerebellum as a model system.

Indexed as

Avian ProteinsAnimalsCerebellumChick EmbryoGlycoproteinsIn Vitro TechniquesMembrane PotentialsMiceModels, NeurologicalNerve Tissue ProteinsNeuregulin-1NeuregulinsNeuromuscular JunctionProtein Processing, Post-TranslationalSynaptosomesAvian ProteinsGlycoproteinsNerve Tissue ProteinsNeuregulin-1NeuregulinsNRG1 protein, Gallus gallusNrg1 protein, mouse

Identifiers

PMID10212491
PMCPMC1692493
OpenAlexW2100300408

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.