Evidence map›Paper›PMID 9108024›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Nucleolin is one component of the B cell-specific transcription factor and switch region binding protein, LR1.

L A Hanakahi, L A Dempsey, M J Li, N Maizels

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
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  3. Review
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  5. Regulation of nucleolin expression by miR-194, miR-206, and HuR.Molecular and cellular biochemistry · 2016
    Article
  6. Article
  7. Nucleolin is important for Epstein-Barr virus nuclear antigen 1-mediated episome binding, maintenance, and transcription.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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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

4 authors at 2 institutions in 1 country.

L A HanakahiDepartment of Molecular Biophysics, Yale University, New Haven, CT 06520-8114, USA.
L A Dempsey
M J Li
N Maizels
Whitney Museum of American Art · USYale University · US

Funding

VIRAL SMALL RNPS--ROLES IN CELL TRANSFORMATIONP01CA016038 · NCI · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 1985 to 2020
$25.6M
MOLECULAR MECHANISMS OF ISOTYPE SWITCH RECOMBINATIONR01GM039799 · NIGMS · YALE UNIVERSITY · PI MAIZELS, NANCY · 1988 to 2009
$2.8M
REGULATION OF LR1 ACTIVITY IN B-LYMPHOCYTESF32GM015948 · NIGMS · YALE UNIVERSITY · PI DEMPSEY, LAURIE A · 1994 to 1995
–
NCI NIH HHS P01 CA016038NCI NIH HHS P01 CA16038NIGMS NIH HHS F32 GM015948NIGMS NIH HHS R01 GM039799NIGMS NIH HHS R01 GM39799
6 · The paper itself

Abstract

LR1 is a B cell-specific, sequence-specific DNA binding activity that regulates transcription in activated B cells. LR1 also binds Ig heavy chain switch region sequences and may function in class switch recombination. LR1 contains two polypeptides, of 106 kDa and 45 kDa, and here we report that the 106-kDa component of LR1 is nucleolin. This identification, initially made by microsequence analysis, was verified by showing that (i) LR1-DNA binding activity increased in B cells transfected with a nucleolin cDNA expression construct; (ii) LR1-DNA binding activity was recognized by antibodies raised against recombinant human nucleolin; and (iii) in B cells transfected with epitope-tagged nucleolin expression constructs, the LR1-DNA complex was recognized by the anti-tag antibody. Nucleolin is an abundant nucleolar protein which is believed to play a role in rDNA transcription or organization, or rRNA processing. Homology between nucleolin and histone H1 suggests that nucleolin may alter DNA organization in response to cell cycle controls, and the nucleolin component of LR1 may therefore function to organize switch regions before, during, or after switch recombination. The demonstration that nucleolin is a component of a B cell-specific complex that binds switch region sequences suggests that the G-rich switch regions may have evolved from rDNA.

Indexed as

RNA-Binding ProteinsAmino Acid SequenceAnimalsB-LymphocytesCell LineDNA-Binding ProteinsHumansImmunoglobulin Class SwitchingImmunoglobulin Switch RegionMiceMolecular Sequence DataNuclear ProteinsNucleolinPhosphoproteinsTranscription FactorsDNA-Binding ProteinsLR1 protein, humanLR1 protein, mouseNuclear ProteinsNucleolinPhosphoproteinsRNA-Binding ProteinsTranscription Factors

Identifiers

PMID9108024
PMCPMC20487
OpenAlexW2021959562

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.