Evidence map›Paper›PMID 21798748›Full record

ArticleBioorganic & medicinal chemistry2011

Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins.

Rongsheng E Wang, Clayton R Hunt, Jiawei Chen, John-Stephen Taylor

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  14. PIM1, CYP1B1, and HSPA2 Targeted by Quercetin Play Important Roles in Osteoarthritis Treatment byEvidence-based complementary and alternative medicine : eCAM · 2019
    Article
  15. Article
  16. Review
  17. The heat-shock, or HSF1-mediated proteotoxic stress, response in cancer: from proteomic stability to oncogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  18. Article
  19. Article
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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

4 authors at 1 institution in 1 country.

Rongsheng E WangDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA.
Clayton R Hunt
Jiawei Chen
John-Stephen Taylor
Washington University in St. Louis · US

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
Tumor Cells Specific Targets for Combined Heat/RadiationP01CA104457 · NCI · WASHINGTON UNIVERSITY · PI ROTI ROTI, JOSEPH L · 2004 to 2008
$8.4M
REQUEST TO UPGRADE 600 MHZ NMR SYSTEMS10RR015715 · NCRR · WASHINGTON UNIVERSITY · PI ACKERMAN, JOSEPH J. H. · 2001 to 2001
$488k
NCI NIH HHS P01 CA 104457NCI NIH HHS P01 CA104457NCRR NIH HHS P41 RR000954NCRR NIH HHS RR1571501
6 · The paper itself

Abstract

Quercetin is a flavonoid natural product, that is, found in many foods and has been found to have a wide range of medicinal effects. Though a number of quercetin binding proteins have been identified, there has been no systematic approach to identifying all potential targets of quercetin. We describe an O7-biotinylated derivative of quercetin (BioQ) that can act as a photoaffinity proteomics reagent for capturing quercetin binding proteins, which can then be identified by LC-MS/MS. BioQ was shown to inhibit heat induction of HSP70 with almost the same efficiency as quercetin, and to both inhibit and photocrosslink to CK2 kinase, a known target of quercetin involved in activation of the heat shock transcription factor. BioQ was also able to pull down a number of proteins from unheated and heated Jurkat cells following UV irradiation that could be detected by both silver staining and Western blot analysis with an anti-biotin antibody. Analysis of the protein bands by trypsinization and LC-MS/MS led to the identification of heat shock proteins HSP70 and HSP90 as possible quercetin target proteins, along with ubiquitin-activating enzyme, a spliceosomal protein, RuvB-like 2 ATPases, and eukaryotic translation initiation factor 3. In addition, a mitochondrial ATPase was identified that has been previously shown to be a target of quercetin. Most of the proteins identified have also been previously suggested to be potential anticancer targets, suggesting that quercetin's antitumor activity may be due to its ability to inhibit multiple target proteins.

Indexed as

Molecular Targeted TherapyAntioxidantsBiotinylationCasein Kinase IIDrug DesignHeat-Shock ProteinsHumansJurkat CellsMolecular StructurePhotoaffinity LabelsProtein TransportProteomeQuercetinAntioxidantsCasein Kinase IIHeat-Shock ProteinsPhotoaffinity LabelsProteomeQuercetin

Identifiers

PMID21798748
PMCPMC3397245
OpenAlexW1982498283

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.