Evidence map›Paper›PMID 21126226›Full record

ReviewCurrent drug targets2011

The use of structural biology in Janus kinase targeted drug discovery.

Nilda L Alicea-Velázquez, Titus J Boggon

Open access · greenAbstract readReview
In one paragraph

Review in Current drug targets, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of Pinosylvin inPharmaceuticals (Basel, Switzerland) · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Nilda L Alicea-VelázquezDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar St., SHM B-316A, New Haven, CT 06520, USA.
Titus J Boggon
Yale University · US

Funding

Structural basis of Jak3-mediated interleukin-2 family signal transductionR01AI075133 · NIAID · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2007 to 2011
$2.2M
NIAID NIH HHS R01 AI075133NIAID NIH HHS R01 AI075133-S1
6 · The paper itself

Abstract

The Janus kinases (or Jak kinases) mediate cytokine and growth factor signal transduction. Acquired or inherited Jak mutations can result in dysregulation of Jak-mediated signal transduction and can be critical to disease acquisition in neoplasias including acute myeloid, acute lymphoblastic and acute megakaryoblastic leukemias, and in rare X-linked severe combined immunodeficiency. The discovery of an acquired Jak2 point mutation, V617F, in significant numbers of patients with classical myeloproliferative disorders has increased the interest in development of Jak2-specific tyrosine kinase inhibitors and consequently there are now over 20 publically available structures of Jak kinase domains that describe all four family members, Jak1, Jak2, Jak3, and Tyk2. Here we review the recent advances in understanding the druggable structure and function of the Jak family, with a focus on the structural biology of the Jak kinase domain. We will discuss how these advances impact the development of Jak-targeted therapeutics.

Indexed as

Drug Delivery SystemsAnimalsDrug DesignDrug DiscoveryHumansJanus KinasesMutationProtein Kinase InhibitorsSignal TransductionJanus KinasesProtein Kinase Inhibitors

Identifiers

PMID21126226
PMCPMC3786457
OpenAlexW2055150750

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.