Evidence map›Paper›PMID 30519713›Full record

ReviewCurrent genetics2019

Novel insights into molecular chaperone regulation of ribonucleotide reductase.

Laura E Knighton, Lena E Delgado, Andrew W Truman

Abstract readReview
In one paragraph

Review in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Versatility of the Mec1Current genetics · 2019
    Review
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.

Laura E KnightonDepartment of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC, 28223, USA.
Lena E DelgadoDepartment of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC, 28223, USA.
Andrew W TrumanDepartment of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC, 28223, USA. atruman1@uncc.edu.ORCID http://orcid.org/0000-0002-6409-3723
University of North Carolina at Charlotte · US

Funding

Regulation of Hsp70-Mediated Cyclin D1 Destruction in Breast CancerR15CA208773 · NCI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI TRUMAN, ANDREW WILLIAM · 2017 to 2017
$440k
National Cancer Institute R15CA208773NCI NIH HHS R15 CA208773
6 · The paper itself

Abstract

The molecular chaperones Hsp70 and Hsp90 bind and fold a significant proportion of the proteome. They are responsible for the activity and stability of many disease-related proteins including those in cancer. Substantial effort has been devoted to developing a range of chaperone inhibitors for clinical use. Recent studies have identified the oncogenic ribonucleotide reductase (RNR) complex as an interactor of chaperones. While several generations of RNR inhibitor have been developed for use in cancer patients, many of these produce severe side effects such as nausea, vomiting and hair loss. Development of more potent, less patient-toxic anti-RNR strategies would be highly desirable. Inhibition of chaperones and associated co-chaperone molecules in both cancer and model organisms such as budding yeast result in the destabilization of RNR subunits and a corresponding sensitization to RNR inhibitors. Going forward, this may form part of a novel strategy to target cancer cells that are resistant to standard RNR inhibitors.

Indexed as

AnimalsAntineoplastic AgentsDNA DamageDNA ReplicationEnzyme ActivationGene Expression RegulationHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesNeoplasmsProtein BindingProteomicsRibonucleotide ReductasesAntineoplastic AgentsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesRibonucleotide ReductasesDNA damage responseHdj2Hsp70Hsp90Molecular chaperonesRibonucleotide reductaseYdj1

Identifiers

PMID30519713
PMCPMC6421096
OpenAlexW2903279818

What OpenQuestion holds

Textmetadata
LicenceTDM
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.