Evidence map›Paper›PMID 1730754›Full record

ArticleThe Journal of cell biology1992

Characterization of the major hnRNP proteins from Drosophila melanogaster.

E L Matunis, M J Matunis, G Dreyfuss

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 129 citations in OpenAlex.

  1. From development to disease: the neuronal role of hnRNPs through the lens ofFrontiers in cell and developmental biology · 2026
    Review
  2. Review
  3. Exercise-induced changes in climbing performance.Royal Society open science · 2021
    Article
  4. Review
  5. Article
  6. An Interaction Network of RNA-Binding Proteins Involved inMolecular & cellular proteomics : MCP · 2020
    Article
  7. RNA-Binding Proteins in Acute Leukemias.International journal of molecular sciences · 2020
    Review
  8. Modulation of the Hippo pathway and organ growth by RNA processing proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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5 more citing papers are in PubMed but not listed here.

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.

E L MatunisHoward Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.
M J Matunis
G Dreyfuss
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To better understand the role(s) of hnRNP proteins in the process of mRNA formation, we have identified and characterized the major nuclear proteins that interact with hnRNAs in Drosophila melanogaster. cDNA clones of several D. melanogaster hnRNP proteins have been isolated and sequenced, and the genes encoding these proteins have been mapped cytologically on polytene chromosomes. These include the hnRNP proteins hrp36, hrp40, and hrp48, which together account for the major proteins of hnRNP complexes in D. melanogaster (Matunis et al., 1992, accompanying paper). All of the proteins described here contain two amino-terminal RNP consensus sequence RNA-binding domains and a carboxyl-terminal glycine-rich domain. We refer to this configuration, which is also found in the hnRNP A/B proteins of vertebrates, as 2 x RBD-Gly. The sequences of the D. melanogaster hnRNP proteins help define both highly conserved and variable amino acids within each RBD and support the suggestion that each RBD in multiple RBD-containing proteins has been conserved independently and has a different function. Although 2 x RBD-Gly proteins from evolutionarily distant organisms are conserved in their general structure, we find a surprising diversity among the members of this family of proteins. A mAb to the hrp40 proteins crossreacts with the human A/B and G hnRNP proteins and detects immunologically related proteins in divergent organisms from yeast to man. These data establish 2 x RBD-Gly as a prevalent hnRNP protein structure across eukaryotes. This information about the composition of hnRNP complexes and about the structure of hnRNA-binding proteins will facilitate studies of the functions of these proteins.

Indexed as

Amino Acid SequenceAnimalsBase SequenceChromosome MappingCloning, MolecularDNADrosophila melanogasterElectrophoresis, Gel, Two-DimensionalHeterogeneous-Nuclear RibonucleoproteinsIsoelectric PointMolecular Sequence DataMolecular WeightNuclear ProteinsPrecipitin TestsRibonucleoproteinsSequence AlignmentDNAHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsRibonucleoproteins

Identifiers

PMID1730754
PMCPMC2289286
OpenAlexW2140102385

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.