Evidence map›Paper›PMID 6164061›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1980

Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments.

D J Goldberg, D A Harris, B W Lubit, J H Schwartz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1980. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 56 citations in OpenAlex.

  1. Nucleotide- and Protein-Dependent Functions ofMolecular biology of the cell · 2022
    Article
  2. Article
  3. Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  4. Article
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  11. Interaction of actin filaments with microtubules.The Journal of cell biology · 1984
    Article
  12. Article
  13. A molecular description of nerve terminal function.Annual review of biochemistry · 1983
    Review
  14. Microinjection into an identified axon to study the mechanism of fast axonal transport.Proceedings of the National Academy of Sciences of the United States of America · 1982
    Article
  15. Article
  16. Article
  17. Article
  18. Characterization of brevin, a serum protein that shortens actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 1981
    Article
  19. 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.

D J Goldberg
D A Harris
B W Lubit
J H Schwartz
Columbia University · US

Funding

STUDIES OF AXONAL TRANSPORT USING SINGLE NEURONSR01NS014711 · NINDS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GOLDBERG, DANIEL J · 1985 to 1990
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NIGMS NIH HHS GM-07367NINDS NIH HHS NS 12066NINDS NIH HHS NS 14711
6 · The paper itself

Abstract

Although actin is thought to participate in several types of cell motility other than muscle contraction, no direct evidence has linked it to the force-generating mechanism for fast axonal transport. We have obtained evidence for the involvement of actin by microinjecting, into the serotonergic giant cerebral neuron of Aplysia, two preparations that have been shown to depolymerize actin filaments. One is a fraction of rabbit serum containing a heat-labile gamma globulin that affects actin polymerization in a manner similar to that of cytochalasin and several proteins that are thought to regulate the length of actin filaments. The other is bovine pancreatic DNase I which binds to actin stoichiometrically. Both preparations substantially decreased the transport of storage vesicles containing [3H]serotonin. Phalloidin, a toxic fungal peptide that binds to actin filaments but stabilizes rather than depolymerizes them, did not inhibit transport. We have not yet determined whether the inhibition od transport occurs during export of [3H]serotonin from the cell body into the axon or during translocation along the axon. Nevertheless, these observations provide a promising experimental indication that actin is involved in fast axonal transport.

Indexed as

Axonal TransportActinsAnimalsCytoskeletonDeoxyribonucleasesgamma-GlobulinsMacromolecular SubstancesPhalloidineThrombinActinsDeoxyribonucleasesgamma-GlobulinsMacromolecular SubstancesPhalloidineThrombin

Identifiers

PMID6164061
PMCPMC350521
OpenAlexW2076668478

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.