Evidence map›Paper›PMID 9763457›Full record

ArticleMolecular biology of the cell1998

Coilin can form a complex with the U7 small nuclear ribonucleoprotein.

M Bellini, J G Gall

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed, 71 citations in OpenAlex.

  1. A Novel Role for Coilin in Vertebrate Innate Immunity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  2. Article
  3. Article
  4. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  5. Article
  6. Review
  7. Coilin: The first 25 years.RNA biology · 2015
    Review
  8. Article
  9. Article
  10. The abbreviated pluripotent cell cycle.Journal of cellular physiology · 2013
    Review
  11. Article
  12. Article
  13. Pearls are novel Cajal body-like structures in the Xenopus germinal vesicle that are dependent on RNA pol III transcription.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2012
    Article
  14. Article
  15. Review
  16. The Cajal body and histone locus body.Cold Spring Harbor perspectives in biology · 2010
    Review
  17. Genetic analysis of nuclear bodies: from nondeterministic chaos to deterministic order.Cold Spring Harbor symposia on quantitative biology · 2010
    Article
  18. Article
  19. Article
  20. Chromosome odds and ends.Annual review of cell and developmental biology · 2009
    Article
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.

M BelliniDepartment of Embryology, Carnegie Institution, Baltimore, Maryland 21210, USA.
J G Gall
Carnegie Institution for Science · 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-33397NIGMS NIH HHS R01 GM033397NIGMS NIH HHS R37 GM033397
6 · The paper itself

Abstract

Coiled bodies (CBs) in the amphibian oocyte nucleus are spherical structures up to 10 microm or more in diameter, much larger than their somatic counterparts, which rarely exceed 1 microm. Oocyte CBs may have smaller granules attached to their surface or embedded within them, which are identical in structure and composition to the many hundreds of B-snurposomes found free in the nucleoplasm. The matrix of the CBs contains the diagnostic protein p80-coilin, which is colocalized with the U7 small nuclear ribonucleoprotein (snRNP), whereas the attached and embedded B-snurposomes contain splicing snRNPs. A few of the 50-100 CBs in the oocyte nucleus are attached to lampbrush chromosomes at the histone gene loci. By coimmunoprecipitation we show that coilin and the U7 snRNP can form a weak but specific complex in the nucleoplasm, which is dependent on the special U7 Sm-binding site. Under the same conditions coilin does not associate with the U1 and U2 snRNPs. Coilin is a nucleic acid-binding protein, as shown by its interaction with single-stranded DNA and with poly r(U) and poly r(G). We suggest that an important function of coilin is to form a transient complex with the U7 snRNP and accompany it to the CBs. In the case of CBs attached to chromosomes at the histone gene loci, the U7 snRNP is thus brought close to the actual site of histone pre-mRNA transcription.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell NucleusConsensus SequenceDNA PrimersFemaleHumansMolecular Sequence DataNuclear ProteinsOocytesPhosphoproteinsPolymerase Chain ReactionProtein BindingRibonucleoproteins, Small NuclearSequence AlignmentDNA PrimersNuclear Proteinsp80-coilinPhosphoproteinsRibonucleoproteins, Small Nuclear

Identifiers

PMID9763457
PMCPMC25576
OpenAlexW2129709316

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.