Evidence map›Paper›PMID 10211837›Full record

ArticleProtein science : a publication of the Protein Society1999

Nucleolar protein B23 has molecular chaperone activities.

A Szebeni, M O Olson

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 8% 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

98 citing papers in PubMed, 1 synthesis or guideline pooled it, 251 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Ribosomes: from conserved origin to functional/medical mobility and heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Prognostic relevance ofAmerican journal of blood research · 2023
    Article
  12. Article
  13. The Role of Nucleophosmin 1 (Life (Basel, Switzerland) · 2022
    Review
  14. Zebrafish models of acute leukemias: Current models and future directions.Wiley interdisciplinary reviews. Developmental biology · 2021
    Review
  15. Article
  16. Article
  17. Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020
    Review
  18. Review
  19. Review
  20. Review

38 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

2 authors at 2 institutions in 1 country.

A SzebeniDepartment of Biochemistry, University of Mississippi Medical Center, Jackson 39216-4505, USA.
M O Olson
Jackson Memorial Hospital · USUniversity of Mississippi Medical Center · US

Funding

INTERACTION OF HIV-1 REV WITH NUCLEOLAR PROTEIN B23R01AI034277 · NIAID · UNIVERSITY OF MISSISSIPPI MEDICAL CENTER · PI OLSON, MARK O · 1993 to 1995
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STRUCTURE AND FUNCTION OF NUCLEOLAR, NONHISTONE PROTEINSR01GM028349 · NIGMS · UNIVERSITY OF MISSISSIPPI MEDICAL CENTER · PI OLSON, MARK O · 1985 to 1995
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NIAID NIH HHS AI34277NIGMS NIH HHS GM28349
6 · The paper itself

Abstract

Protein B23 is an abundant, multifunctional nucleolar phosphoprotein whose activities are proposed to play a role in ribosome assembly. Szebeni et al. (1997) showed stimulation of nuclear import in vitro by protein B23 and suggested that this effect was due to a molecular chaperone-like activity. Protein B23 was tested for chaperone activities using several protein substrates. The temperature-dependent and -independent aggregation of the HIV-1 Rev protein was measured using a zero angle light scattering (turbidity) assay. Protein B23 inhibited the aggregation of the Rev protein, with the amount of inhibition proportional to the concentration of B23 added. This activity was saturable with nearly complete inhibition when the molar ratio of B23:Rev was slightly above one. Protein B23 also protected liver alcohol dehydrogenase (LADH), carboxypeptidase A, citrate synthase, and rhodanese from aggregation during thermal denaturation and preserved the enzyme activity of LADH under these conditions. In addition, protein B23 was able to promote the restoration of activity of LADH previously denatured with guanidine-HCl. Protein B23 preferentially bound denatured substrates and exposed hydrophobic regions when complexed with denatured proteins. Thus, by several criteria, protein B23 behaves like a molecular chaperone; these activities may be related to its role in ribosome biogenesis.

Indexed as

Alcohol DehydrogenaseDose-Response Relationship, DrugGene Products, revHIV-1LiverMolecular ChaperonesNuclear ProteinsNucleophosminProtein DenaturationProtein Foldingrev Gene Products, Human Immunodeficiency VirusTemperatureThiosulfate SulfurtransferaseTime FactorsUltracentrifugationAlcohol DehydrogenaseGene Products, revMolecular ChaperonesNuclear ProteinsNucleophosminrev Gene Products, Human Immunodeficiency VirusThiosulfate Sulfurtransferase

Identifiers

PMID10211837
PMCPMC2144306
OpenAlexW1974798462

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.