Evidence map›Paper›PMID 12214272›Full record

ArticleOncogene2002

Thioredoxin reductase regulates AP-1 activity as well as thioredoxin nuclear localization via active cysteines in response to ionizing radiation.

Shervin Karimpour, Junyang Lou, Lilie L Lin, Luis M Rene, Lucio Lagunas, Xinrong Ma, Sreenivasu Karra, C Matthew Bradbury, Stephanie Markovina, Prabhat C Goswami and 5 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Thioredoxin-dependent system. Application of inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2021
    Review
  3. Article
  4. Disulfide reductase systems in liver.British journal of pharmacology · 2019
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The cysteine proteome.Free radical biology & medicine · 2015
    Review
  11. Article
  12. Article
  13. Review
  14. Annexin A2: the importance of being redox sensitive.International journal of molecular sciences · 2013
    Article
  15. Nuclear expression of thioredoxin-1 in the invasion front is associated with outcome in patients with gallbladder carcinoma.HPB : the official journal of the International Hepato Pancreato Biliary Association · 2012
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

15 authors at 6 institutions in 2 countries.

Shervin KarimpourRadiation Oncology Branch, Radiation Oncology Sciences Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Junyang Lou
Lilie L Lin
Luis M Rene
Lucio Lagunas
Xinrong Ma
Sreenivasu Karra
C Matthew Bradbury
Stephanie Markovina
Prabhat C Goswami
Douglas R Spitz
Kiichi Hirota
Dhananjaya V Kalvakolanu
Junji Yodoi
David Gius
Mallinckrodt (United States) · USUniversity of Maryland, Baltimore · USCenter for Cancer Research · USUniversity of Iowa · USKyoto University · JPKyoto University Hospital · JP

Funding

MODULATION OF IFN ACTION VIA NOVEL REGULATORY FACTORSR01CA078282 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI KALVAKOLANU, DHAN V. · 1998 to 2014
$4.4M
NITRIC OXIDE INDUCED CELL INJURY--MOLECULAR MECHANISMSR01HL051469 · NHLBI · WASHINGTON UNIVERSITY · PI SPITZ, DOUGLAS ROBERT · 1994 to 2003
$1.0M
TUMOR GROWTH INHIBITION BY INTERFERON B AND RETINOIDSR01CA071401 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI KALVAKOLANU, DHAN V. · 1996 to 2001
$595k
X RAY, HEAT SHOCK AND CELL CYCLE COUPLED GENE EXPRESSIONR29CA069593 · NCI · WASHINGTON UNIVERSITY · PI GOSWAMI, PRABHAT C · 1996 to 2000
$103k
GI RESTRICTION POINT &TCR ACTIVATION INDUCED APOPTOSISK08CA072602 · NCI · WASHINGTON UNIVERSITY · PI GIUS, DAVID · 1997 to 2000
$83k
NCI NIH HHS 1 K08 CA72602-01NCI NIH HHS CA69593NCI NIH HHS CA 71401NCI NIH HHS R01 CA 78282NHLBI NIH HHS R01 HL51469
6 · The paper itself

Abstract

A recently identified class of signaling factors uses critical cysteine motif(s) that act as redox-sensitive 'sulfhydryl switches' to reversibly modulate specific signal transduction cascades regulating downstream proteins with similar redox-sensitive sites. For example, signaling factors such as redox factor-1 (Ref-1) and transcription factors such as the AP-1 complex both contain redox-sensitive cysteine motifs that regulate activity in response to oxidative stress. The mammalian thioredoxin reductase-1 (TR) is an oxidoreductase selenocysteine-containing flavoprotein that also appears to regulate multiple downstream intracellular redox-sensitive proteins. Since ionizing radiation (IR) induces oxidative stress as well as increases AP-1 DNA-binding activity via the activation of Ref-1, the potential roles of TR and thioredoxin (TRX) in the regulation of AP-1 activity in response to IR were investigated. Permanently transfected cell lines that overexpress wild type TR demonstrated constitutive increases in AP-1 DNA-binding activity as well as AP-1-dependent reporter gene expression, relative to vector control cells. In contrast, permanently transfected cell lines expressing a TR gene with the active site cysteine motif deleted were unable to induce AP-1 activity or reporter gene expression in response to IR. Transient genetic overexpression of either the TR wild type or dominant-negative genes demonstrated similar results using a transient assay system. One mechanism through which TR regulates AP-1 activity appears to involve TRX sub-cellular localization, with no change in the total TRX content of the cell. These results identify a novel function of the TR enzyme as a signaling factor in the regulation of AP-1 activity via a cysteine motif located in the protein.

Indexed as

Signal TransductionCysteineHeLa CellsHumansThioredoxin-Disulfide ReductaseThioredoxin Reductase 1ThioredoxinsTranscription Factor AP-1CysteineThioredoxin-Disulfide ReductaseThioredoxin Reductase 1ThioredoxinsTranscription Factor AP-1TXNRD1 protein, human

Identifiers

PMID12214272
OpenAlexW2006105383

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.