Evidence map›Paper›PMID 3863133›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1985

Heat shock increases the synthesis of the poly(A)-binding protein in HeLa cells.

M Schönfelder, A Horsch, H P Schmid

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1985. 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
3.3field-weighted citation impact, top 7% 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, 34 citations in OpenAlex.

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  12. Heat shock and the heat shock proteins.The Biochemical journal · 1986
    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.

M Schönfelder
A Horsch
H P Schmid

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When HeLa cells are shifted from 37 degrees C to 45 degrees C, the synthesis of two proteins increases. Their approximate molecular masses are 73 kDa [heat shock protein 73 (hsp73)] and 87 kDa (hsp87), respectively. One of them, the hsp73, shows a specific affinity for poly(A). This protein is identical with a protein regularly found associated with translatable mRNAs in all vertebrate cells. It is well characterized by its high affinity to the poly(A) sequence of polyribosomal mRNA, and it occurs free in cytoplasm. hsp73 and the poly(A)-binding protein have the same isoelectric point and molecular size. The peptide analysis indicates that they are identical.

Indexed as

Carrier ProteinsCytosolElectrophoresis, Polyacrylamide GelHeLa CellsHot TemperatureHumansMolecular WeightPoly APoly(A)-Binding ProteinsPolyribosomesProtein BindingCarrier ProteinsPoly APoly(A)-Binding Proteins

Identifiers

PMID3863133
PMCPMC390792
OpenAlexW2069845997

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.