Evidence map›Paper›PMID 18229458›Full record

ArticleCell stress & chaperones2007

Hsp70B' regulation and function.

Emily J Noonan, Robert F Place, Charles Giardina, Lawrence E Hightower

Open access · greenAbstract readCorrected and Republished Article
In one paragraph

Article in Cell stress & chaperones, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

50 citing papers in PubMed, 111 citations in OpenAlex.

  1. Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. HSPA6 and its role in cancers and other diseases.Molecular biology reports · 2022
    Review
  7. Article
  8. Article
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  18. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Emily J NoonanDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA. emily.noonan@gmail.com
Robert F Place
Charles Giardina
Lawrence E Hightower
University of Connecticut · US

Funding

THE EPITHELIA OF THE EYE--EFFECT OF ENVIRONMENTAL AGENTSP30ES003828 · NIEHS · MOUNT DESERT ISLAND BIOLOGICAL LAB · PI HENSON, JOHN H · 1987 to 2008
$4.1M
THE EPITHELIA OF THE EYE--EFFECT OF ENVIRONMENTAL AGENTSP50ES003828 · NIEHS · MOUNT DESERT ISLAND BIOLOGICAL LAB · 1985 to 1988
–
NIEHS NIH HHS ES03828NIEHS NIH HHS P30 ES003828
6 · The paper itself

Abstract

Heat shock protein (Hsp) 70B' is a human Hsp70 chaperone that is strictly inducible, having little or no basal expression levels in most cells. Using siRNAs to knockdown Hsp70B' and Hsp72 in HT-29, SW-480, and CRL-1807 human colon cell lines, we have found that the two are regulated coordinately in response to stress. We also have found that proteasome inhibition is a potent activator of hsp70B'. Flow cytometry was used to assay hsp70B' promoter activity in HT-29eGFP cells in this study. Knockdown of both Hsp70B' and Hsp72 sensitized cells to heat stress and increasing concentrations of proteasome inhibitor. These data support the conclusion that Hsp72 is the primary Hsp70 family responder to increasing levels of proteotoxic stress, and Hsp70B' is a secondary responder. Interestingly ZnSO4 induces Hsp70B' and not Hsp72 in CRL-1807 cells, suggesting a stressor-specific primary role for Hsp70B'. Both Hsp70B' and Hsp72 are important for maintaining viability under conditions that increase the accumulation of damaged proteins in HT-29 cells. These findings are likely to be important in pathological conditions in which Hsp70B' contributes to cell survival.

Indexed as

Antineoplastic AgentsCell SurvivalFlow CytometryGreen Fluorescent ProteinsHeat-Shock ResponseHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHT29 CellsHumansLeupeptinsPromoter Regions, GeneticProteasome InhibitorsRNA, Small InterferingAntineoplastic Agentsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeenhanced green fluorescent proteinGreen Fluorescent ProteinsHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHSPA7 protein, humanLeupeptinsProteasome InhibitorsRNA, Small Interfering

Identifiers

PMID18229458
PMCPMC2134801
OpenAlexW2179824901

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.