Evidence map›Paper›PMID 19015259›Full record

ArticleThe Journal of biological chemistry2009

Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator).

Hua Li, Gerwald Jogl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

64 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
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  8. Article
  9. The role of TIGAR in nervous system diseases.Frontiers in aging neuroscience · 2022
    Review
  10. Correlation of Glucose Metabolism with Cancer and Intervention with Traditional Chinese Medicine.Evidence-based complementary and alternative medicine : eCAM · 2022
    Review
  11. Review
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  13. Article
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  15. Article
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  17. Article
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  20. Article

4 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Hua LiDepartment of Molecular Biology, Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.
Gerwald Jogl
Brown University · US

Funding

WNT SIGNALING IN HEPATOCELLULAR CARCINOMAP20RR015578 · NCRR · BROWN UNIVERSITY · PI THOMPSON, WILLIAM ALBERT · 2000 to 2009
$22.8M
NCRR NIH HHS P20RR15578
6 · The paper itself

Abstract

Activation of the p53 tumor suppressor by cellular stress leads to variable responses ranging from growth inhibition to apoptosis. TIGAR is a novel p53-inducible gene that inhibits glycolysis by reducing cellular levels of fructose-2,6-bisphosphate, an activator of glycolysis and inhibitor of gluconeogenesis. Here we describe structural and biochemical studies of TIGAR from Danio rerio. The overall structure forms a histidine phosphatase fold with a phosphate molecule coordinated to the catalytic histidine residue and a second phosphate molecule in a position not observed in other phosphatases. The recombinant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro. The TIGAR active site is open and positively charged, consistent with its enzymatic function as bisphosphatase. The closest related structures are the bacterial broad specificity phosphatase PhoE and the fructose-2,6-bisphosphatase domain of the bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The structural comparison shows that TIGAR combines an accessible active site as observed in PhoE with a charged substrate-binding pocket as seen in the fructose-2,6-bisphosphatase domain of the bifunctional enzyme.

Indexed as

Protein FoldingZebrafishAnimalsApoptosis Regulatory ProteinsCatalytic DomainEscherichia coli ProteinsFructosediphosphatesHydrolysisIntracellular Signaling Peptides and ProteinsPhosphofructokinase-2Phosphoric Monoester HydrolasesPorinsProtein Structure, TertiaryRecombinant ProteinsStructural Homology, ProteinSubstrate SpecificityApoptosis Regulatory ProteinsEscherichia coli Proteinsfructose-1,6-diphosphatefructose 2,6-diphosphateFructosediphosphatesIntracellular Signaling Peptides and ProteinsPhoE protein, E coliPhosphofructokinase-2Phosphoric Monoester HydrolasesPorinsRecombinant Proteinstigarb protein, zebrafishTIGAR protein, humanZebrafish Proteins

Identifiers

PMID19015259
PMCPMC2615519
OpenAlexW2030992905

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.