Evidence map›Paper›PMID 1730739›Full record

ArticleThe Journal of cell biology1992

Localization of the nucleolar protein NO38 in amphibian oocytes.

B A Peculis, J G Gall

Open access · bronzeAbstract read
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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  3. Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  10. Conventional and nonconventional roles of the nucleolus.International review of cytology · 2002
    Review
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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 at 1 institution in 1 country.

B A PeculisDepartment of Embryology, Carnegie Institution, Baltimore, Maryland 21210.
J G Gall
Department of Embryology · US

Funding

THE ORGANIZATION OF ANIMAL CELL NUCLEIR01GM033397 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GALL, JOSEPH G. · 1985 to 2019
$8.4M
THE ORGANIZATION OF ANIMAL CELL NUCLEIR37GM033397 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GALL, JOSEPH G. · 1990 to 1999
–
NIGMS NIH HHS GM 33397
6 · The paper itself

Abstract

To examine the role of primary amino acid sequence in the localization of proteins within the nucleus, we studied the nucleolar protein NO38 of amphibian oocytes. We synthesized NO38 transcripts in vitro, injected them into the oocyte cytoplasm, and followed the distribution of the translation products. The injected RNA contained a short sequence encoding an epitope derived from the human c-myc protein. We used an mAb against this epitope to detect translation products from injected RNAs by Western blots and by immunofluoresent staining of cytological preparations. When full-length transcripts of NO38 were injected into oocytes, the translation products accumulated efficiently in the germinal vesicle, and a major fraction was localized in the multiple nucleoli. To identify protein domains involved in this nucleolus-specific accumulation, we prepared a series of carboxy-terminal deletions of the cDNA. Oocytes injected with RNA encoding truncated forms of NO38 were examined for altered patterns of protein accumulation. We defined a domain of about 24 amino acids near the carboxy terminus that was essential for nucleolar localization of NO38. This domain is separated by more than 70 amino acids from two putative nuclear localization signals near the middle of the molecule. Hybrid constructs were made which encoded part of Escherichia coli beta-galactosidase or pyruvate kinase fused to a long segment of NO38 containing the essential domain. Injection of RNA from these constructs showed that the essential domain was not sufficient to target the hybrid proteins to the nucleolus. We suggest that nucleolar accumulation of NO38 requires more than a single linear domain.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBlotting, WesternCell NucleolusCell NucleusFemaleGenes, mycMolecular Sequence DataNotophthalmus viridescensNuclear ProteinsNucleophosminOligodeoxyribonucleotidesOocytesProtein BiosynthesisRestriction MappingNuclear ProteinsNucleophosminOligodeoxyribonucleotides

Identifiers

PMID1730739
PMCPMC2289268
OpenAlexW2021295271

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.