Evidence map›Paper›PMID 6610683›Full record

ArticleThe Journal of cell biology1984

A membrane cytoskeleton from Dictyostelium discoideum. III. Plasma membrane fragments bind predominantly to the sides of actin filaments.

C M Goodloe-Holland, E J Luna

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Ponticulin is an atypical membrane protein.The Journal of cell biology · 1994
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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.

C M Goodloe-Holland
E J Luna

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
NIGMS NIH HHS GM33048NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

The binding between sonicated Dictyostelium discoideum plasma membrane fragments and F-actin on Sephacryl S-1000 beads was found to be competitively inhibited by myosin subfragment-1. This inhibition is MgATP-sensitive, exhibits a Ki of approximately 5 X 10(-8) M, and is reciprocal, since membranes inhibit the binding of 125I-heavy meromyosin to F-actin on beads. These experiments demonstrate that membrane binding and S-1 binding to F-actin on beads are mutually exclusive and, therefore, that the membrane fragments bind predominantly to the sides, rather than to the ends, of the actin filaments. This conclusion is supported by electron micrographs that show many lateral associations between membrane fragments and bead-associated actin filaments. Such lateral associations could play an important role in the organization and lateral movement of membrane proteins by the cytomusculature.

Indexed as

ActinsAdenosine TriphosphateBinding, CompetitiveCell MembraneCytoskeletonDictyosteliumElectrophoresis, Polyacrylamide GelKineticsMembrane ProteinsMicroscopy, ElectronMyosinsMyosin SubfragmentsPeptide FragmentsActinsAdenosine TriphosphateMembrane ProteinsMyosinsMyosin SubfragmentsPeptide Fragments

Identifiers

PMID6610683
PMCPMC2275626
OpenAlexW2050641578

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.