Evidence map›Paper›PMID 3417763›Full record

ArticleThe Journal of cell biology1988

Posttranslational incorporation of contractile proteins into myofibrils in a cell-free system.

M Bouché, S M Goldfine, D A Fischman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  4. Article
  5. Mutant actin: a dead end?Journal of muscle research and cell motility · 1992
    Review
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  12. Review
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.

M BouchéDepartment of Cell Biology and Anatomy, Cornell University Medical College, New York 10021.
S M Goldfine
D A Fischman
Cornell University · US

Funding

MYOFIBRIL ASSEMBLY IN STRIATED MUSCLER01AM032147 · AM · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI FISCHMAN, DONALD A · 1985 to 1985
–
NIADDK NIH HHS AM32147
6 · The paper itself

Abstract

The incorporation of newly synthesized protein into myofibrils has been examined in a cell-free system. Myofibrils were added to a reticulocyte lysate after the in vitro translation of muscle-specific poly(A)+RNA. Only a small number of the many synthesized proteins were found to associate with the exogenously added myofibrils. These proteins were all identified as sarcomeric components and had subunit mobilities (Mr) of 200, 140, 95, 86, 43, 38, 35, 25, 23, 20, and 18 kD. The association was rapid (t1/2 less than 15 min) and, for most of the proteins, relatively temperature insensitive. Except for a 43-kD polypeptide, tentatively identified as beta-actin, none of the proteins encoded by brain poly(A)+RNA associated with the myofibrils. When filaments made from purified myosin or actin were used as the "capture" substrates, only thick or thin filament proteins, respectively, were incorporated. Incorporation was substantially reduced when cross-linked myosin filaments were used. These results are compatible with a model in which proteins of the sarcomere are in kinetic equilibrium with homologous proteins in a soluble pool.

Indexed as

AnimalsCell-Free SystemChick EmbryoChickensCytoskeletonElectrophoresis, Polyacrylamide GelMuscle ProteinsMusclesMyofibrilsOrgan SpecificityProtein BiosynthesisRNA, MessengerMuscle ProteinsRNA, Messenger

Identifiers

PMID3417763
PMCPMC2115203
OpenAlexW2132167520

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.