Evidence map›Paper›PMID 23145051›Full record

ArticlePloS one2012

Identification of proteins sensitive to thermal stress in human neuroblastoma and glioma cell lines.

Guilian Xu, Stanley M Stevens, Firas Kobeissy, Firas Kobiessy, Hilda Brown, Scott McClung, Mark S Gold, David R Borchelt

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Review
  8. Curcumin may induce lipolysis via proteo-stress in Huh7 human hepatoma cells.Journal of clinical biochemistry and nutrition · 2019
    Article
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  17. Brain injection of α-synuclein induces multiple proteinopathies, gliosis, and a neuronal injury marker.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  18. Article
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4 · The record

Corrections and comments

  • Erratum issued
    Kobiessy, Firas [corrected to Kobeissy, Firas]
5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Guilian XuDepartment of Neuroscience, Santa Fe Health Alzheimer's Disease Research Center, University of Florida, Gainesville, FL, USA. xugl@ufl.edu
Stanley M Stevens
Firas Kobeissy
Firas Kobiessy
Hilda Brown
Scott McClung
Mark S Gold
David R Borchelt
University of Florida · USUniversity of Florida Health · USUniversity of South Florida · US

Funding

Protein Misfolding in NeurodegenerationR01NS044278 · NINDS · UNIVERSITY OF FLORIDA · PI BORCHELT, DAVID R · 2004 to 2007
$1.3M
Protein Ubiquitination in Cell Models of DiseaseR21AG025426 · NIA · UNIVERSITY OF FLORIDA · PI BORCHELT, DAVID R · 2004 to 2005
$345k
NIA NIH HHS R21 AG025426NIA NIH HHS R21AG025426NINDS NIH HHS R01 NS044278NINDS NIH HHS R01NS44278
6 · The paper itself

Abstract

Heat-shock is an acute insult to the mammalian proteome. The sudden elevation in temperature has far-reaching effects on protein metabolism, leads to a rapid inhibition of most protein synthesis, and the induction of protein chaperones. Using heat-shock in cells of neuronal (SH-SY5Y) and glial (CCF-STTG1) lineage, in conjunction with detergent extraction and sedimentation followed by LC-MS/MS proteomic approaches, we sought to identify human proteins that lose solubility upon heat-shock. The two cell lines showed largely overlapping profiles of proteins detected by LC-MS/MS. We identified 58 proteins in detergent insoluble fractions as losing solubility in after heat shock; 10 were common between the 2 cell lines. A subset of the proteins identified by LC-MS/MS was validated by immunoblotting of similarly prepared fractions. Ultimately, we were able to definitively identify 3 proteins as putatively metastable neural proteins; FEN1, CDK1, and TDP-43. We also determined that after heat-shock these cells accumulate insoluble polyubiquitin chains largely linked via lysine 48 (K-48) residues. Collectively, this study identifies human neural proteins that lose solubility upon heat-shock. These proteins may represent components of the human proteome that are vulnerable to misfolding in settings of proteostasis stress.

Indexed as

Cell Line, TumorChromatography, LiquidGliomaHeat-Shock ProteinsHeat-Shock ResponseHumansNeuroblastomaNeurogliaNeuronsPolyubiquitinProtein BiosynthesisProteomeProteomicsTandem Mass SpectrometryUbiquitinationHeat-Shock ProteinsPolyubiquitinProteome

Identifiers

PMID23145051
PMCPMC3493505
OpenAlexW1994266871

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.