Evidence map›Paper›PMID 29102083›Full record

ArticleTrends in biochemical sciences2017

Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation.

Nitika, Andrew W Truman

Abstract read
In one paragraph

Article in Trends in biochemical sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Article
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  15. Review
  16. Review
  17. Article
  18. General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021
    Article
  19. Article
  20. 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

2 authors.

NitikaDepartment of Biological Sciences, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
Andrew W TrumanDepartment of Biological Sciences, University of North Carolina at Charlotte, Charlotte, NC 28223, USA. Electronic address: atruman1@uncc.edu.

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
NCI NIH HHS R15 CA208773
6 · The paper itself

Abstract

Heat shock protein 70 (Hsp70) is a molecular chaperone required for protein folding, cell viability, and cancer cell proliferation. Recent studies suggest that Hsp70 phosphorylation regulates important cellular processes, such as cell cycle progression, apoptosis, protein degradation, and resistance to anticancer therapeutics.

Indexed as

Antineoplastic AgentsApoptosisCell ProliferationCell SurvivalHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesPhosphorylationAntineoplastic AgentsHSP70 Heat-Shock ProteinsMolecular ChaperonescancerchaperonesHsp70kinasesphosphorylation

Identifiers

PMID29102083
PMCPMC5701876

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.