Evidence map›Paper›PMID 24003220›Full record

ArticleThe Journal of biological chemistry2013

Evaluation of cancer dependence and druggability of PRP4 kinase using cellular, biochemical, and structural approaches.

Qiang Gao, Ingrid Mechin, Nayantara Kothari, Zhuyan Guo, Gejing Deng, Kimberly Haas, Jessica McManus, Dietmar Hoffmann, Anlai Wang, Dmitri Wiederschain and 15 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
0.8field-weighted citation impact, top 28% 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, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Structure Activity Relationship Studies aroundMolecules (Basel, Switzerland) · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. A Challenging Pie to Splice: Drugging the Spliceosome.Angewandte Chemie (International ed. in English) · 2017
    Review
  16. Article
  17. Review
  18. Article
  19. On the accuracy of unit-cell parameters in protein crystallography.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  20. SR protein kinases promote splicing of nonconsensus introns.Nature structural & molecular biology · 2015
    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

25 authors at 2 institutions in 1 country.

Qiang GaoFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Ingrid MechinTucson Research Center, Sanofi, Tucson, Arizona 85755.
Nayantara KothariFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Zhuyan GuoFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Gejing DengFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Kimberly HaasLead Generation and Candidate Realization, Sanofi, Bridgewater, New Jersey 08807, and.
Jessica McManusFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Dietmar HoffmannFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Anlai WangFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Dmitri WiederschainFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Jennifer RocnikFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Werngard CzechtizkyLead Generation and Candidate Realization, Sanofi, Industriepark Höchst, 65926 Frankfurt, Germany.
Xin ChenLead Generation and Candidate Realization, Sanofi, Bridgewater, New Jersey 08807, and.
Larry McLeanLead Generation and Candidate Realization, Sanofi, Bridgewater, New Jersey 08807, and.
Heike ArltFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
David HarperFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Feng LiuFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Tahir MajidLead Generation and Candidate Realization, Sanofi, Waltham, Massachusetts 02451.
Vinod PatelLead Generation and Candidate Realization, Sanofi, Waltham, Massachusetts 02451.
Christoph LengauerFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Carlos Garcia-EcheverriaFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Bailin ZhangFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Hong ChengFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Marion DorschFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France.
Shih-Min A HuangFrom Discovery and Early Development, Sanofi Oncology, Cambridge, Massachusetts 02139 and 94400 Vitry-sur-Seine Cedex, France,. Electronic address: alex.huang@sanofi.com.
Sanofi (United States) · USArizona Research Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PRP4 kinase is known for its roles in regulating pre-mRNA splicing and beyond. Therefore, a wider spectrum of PRP4 kinase substrates could be expected. The role of PRP4 kinase in cancer is also yet to be fully elucidated. Attaining specific and potent PRP4 inhibitors would greatly facilitate the study of PRP4 biological function and its validation as a credible cancer target. In this report, we verified the requirement of enzymatic activity of PRP4 in regulating cancer cell growth and identified an array of potential novel substrates through orthogonal proteomics approaches. The ensuing effort in structural biology unveiled for the first time unique features of PRP4 kinase domain and its potential mode of interaction with a low molecular weight inhibitor. These results provide new and important information for further exploration of PRP4 kinase function in cancer.

Indexed as

Neoplasm ProteinsNeoplasmsProtein Kinase InhibitorsRibonucleoprotein, U4-U6 Small NuclearCell Line, TumorHumansProteomicsNeoplasm ProteinsProtein Kinase InhibitorsPRPF4 protein, humanRibonucleoprotein, U4-U6 Small NuclearCancer TherapyCrystallographyDrug DiscoveryProteomicsStructural Biology

Identifiers

PMID24003220
PMCPMC3798481
OpenAlexW1967066174

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.