Evidence map›Paper›PMID 22955281›Full record

ArticleThe Journal of biological chemistry2012

Mapping protein-protein proximity in the purinosome.

Yijun Deng, Jongsik Gam, Jarrod B French, Hong Zhao, Songon An, Stephen J Benkovic

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

48 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Research square · 2026
    Article
  3. Review
  4. Article
  5. A high throughput assay for phosphoribosylformylglycinamidine synthase.SLAS discovery : advancing life sciences R & D · 2025
    Article
  6. Article
  7. Review
  8. A journey into the regulatory secrets of theFrontiers in pharmacology · 2024
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Human de novo purine biosynthesis.Critical reviews in biochemistry and molecular biology · 2021
    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

6 authors at 3 institutions in 2 countries.

Yijun DengDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Jongsik Gam
Jarrod B French
Hong Zhao
Songon An
Stephen J Benkovic
Pennsylvania State University · USKorea Research Institute of Bioscience and Biotechnology · KRUniversity of Maryland, Baltimore · US

Funding

TRANSFORMYLASE ENZYMES--DIHYDROFOLATE REDUCTASER01GM024129 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BENKOVIC, STEPHEN J · 1985 to 2024
$5.2M
NIGMS NIH HHS 3 R01 GM024129-31S1NIGMS NIH HHS R01 GM024129
6 · The paper itself

Abstract

The enzymes in the human de novo purine synthesis pathway were found to form a cellular complex, the purinosome, upon culturing cells in purine-depleted medium (An, S., Kumar R., Sheets, E. D., and Benkovic, S. J. (2008) Science 320, 103-106). Purinosome formation and dissociation were found to be modulated by several factors, including the microtubule network and cell signaling involving protein phosphorylation. To determine whether the pathway enzymes are in physical contact, we probed for the protein-protein interactions (PPIs) within the purinosome with a novel application of the Tango PPI reporter system (Barnea, G., Strapps, W., Herrada, G., Berman, Y., Ong, J., Kloss, B., Axel, R., and Lee, K. J. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 64-69). We found PPIs among all six enzymes within the pathway and evidence for a core involving the first three enzymes. We also captured purinosomes under both purine-rich and purine-depleted conditions. The results provide additional insights into the transient nature and topography of the purinosome.

Indexed as

EnzymesHeLa CellsHumansMetabolomePurinesEnzymesPurines

Identifiers

PMID22955281
PMCPMC3476287
OpenAlexW1964174822

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.