Evidence map›Paper›PMID 8755532›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Real-time detection of the surface delivery of newly synthesized membrane proteins.

J S Andreose, G Fumagalli, F J Sigworth, M J Caplan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. 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
0.1field-weighted citation impact, top 56% 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, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Inhibition of axonal growth by brefeldin A in hippocampal neurons in culture.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997
    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

4 authors at 1 institution in 1 country.

J S AndreoseDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, USA.
G Fumagalli
F J Sigworth
M J Caplan
Yale University · US

Funding

FLUCTUATIONS IN IONIC CURRENT THROUGH MEMBRANE CHANNELSR01NS021501 · NINDS · YALE UNIVERSITY · PI SIGWORTH, FREDERICK J · 1985 to 2024
$10.9M
ION PUMPS IN POLARIZED EPITHELIA: SORTING AND FUNCTIONR01GM042136 · NIGMS · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 1989 to 2004
$1.7M
NIGMS NIH HHS GM-42136NINDS NIH HHS NS-21501
6 · The paper itself

Abstract

Newly synthesized membrane proteins travel from the Golgi complex to the cell surface in transport vesicles. We have exploited the ion channel properties of the nicotinic acetylcholine receptor (AChR) to observe in real time the constitutive delivery of newly synthesized AChR proteins to the plasma membrane in cultured muscle cells. Whole-cell voltage clamp was employed to monitor the current fluctuations induced by carbamylcholine upon the insertion into the plasma membrane of newly synthesized AChRs, following release from a 20 degrees C temperature block. We find that the transit of vesicles to the cell surface occurs within a few minutes after release of the block. The time course of electrical signals is consistent with many of the fusion events being instantaneous, although some appear to reveal the flickering of a fusion pore. AChR-containing vesicles can fuse individually or as conglomerates. Intracellular application of guanosine 5'-[gamma-thio]triphosphate inhibits the constitutive traffic of AChRs in most cells. Individual exocytotic vesicles carry between 10 and 300 AChR molecules, suggesting that AChRs may be packed extremely densely.

Indexed as

Protein Processing, Post-TranslationalAnimalsBungarotoxinsCell LineCell MembraneElectrophysiologyFourier AnalysisGolgi ApparatusGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateIon ChannelsKineticsMembrane PotentialsMembrane ProteinsMiceMuscle, SkeletalBungarotoxinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateIon ChannelsMembrane ProteinsReceptors, Nicotinic

Identifiers

PMID8755532
PMCPMC38803
OpenAlexW1976739233

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.