Evidence map›Paper›PMID 25057888›Full record

ReviewThe Biochemical journal2014

The molecular regulation of Janus kinase (JAK) activation.

Jeffrey J Babon, Isabelle S Lucet, James M Murphy, Nicos A Nicola, Leila N Varghese

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed, 1 pooled it
9.8field-weighted citation impact, top 1% 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

155 citing papers in PubMed, 1 synthesis or guideline pooled it, 307 citations in OpenAlex.

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  6. Targeting the JAK/STAT signalling axis in cancer: chemopreventive potential of natural compounds with emerging focus on retinoids.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
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95 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

5 authors at 2 institutions in 1 country.

Jeffrey J Babon *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
Isabelle S Lucet *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
James M Murphy *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
Nicos A Nicola *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
Leila N Varghese *The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia.
Walter and Eliza Hall Institute of Medical Research · AUUniversity of Melbourne · AU

Funding

Differentiation of Granulocytes and MacrophagesR37CA022556 · NCI · WALTER AND ELIZA HALL INST MEDICAL RES · PI METCALF, DONALD · 2005 to 2014
$2.3M
DIFFERENTIATION OF GRANULOCYTES AND MACROPHAGESR01CA022556 · NCI · WALTER AND ELIZA HALL INST MEDICAL RES · PI METCALF, DONALD · 1985 to 2004
$900k
NCI NIH HHS CA22556NCI NIH HHS R01 CA022556NCI NIH HHS R37 CA022556
6 · The paper itself

Abstract

The JAK (Janus kinase) family members serve essential roles as the intracellular signalling effectors of cytokine receptors. This family, comprising JAK1, JAK2, JAK3 and TYK2 (tyrosine kinase 2), was first described more than 20 years ago, but the complexities underlying their activation, regulation and pleiotropic signalling functions are still being explored. Here, we review the current knowledge of their physiological functions and the causative role of activating and inactivating JAK mutations in human diseases, including haemopoietic malignancies, immunodeficiency and inflammatory diseases. At the molecular level, recent studies have greatly advanced our knowledge of the structures and organization of the component FERM (4.1/ezrin/radixin/moesin)-SH2 (Src homology 2), pseudokinase and kinase domains within the JAKs, the mechanism of JAK activation and, in particular, the role of the pseudokinase domain as a suppressor of the adjacent tyrosine kinase domain's catalytic activity. We also review recent advances in our understanding of the mechanisms of negative regulation exerted by the SH2 domain-containing proteins, SOCS (suppressors of cytokine signalling) proteins and LNK. These recent studies highlight the diversity of regulatory mechanisms utilized by the JAK family to maintain signalling fidelity, and suggest alternative therapeutic strategies to complement existing ATP-competitive kinase inhibitors.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsEnzyme ActivationHumansImmunologic Deficiency SyndromesIntracellular Signaling Peptides and ProteinsJanus Kinase 1Janus Kinase 2Janus Kinase 3Leukocyte Common AntigensMyeloproliferative DisordersPrecursor Cell Lymphoblastic Leukemia-LymphomaProteinsProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 11Adaptor Proteins, Signal TransducingIntracellular Signaling Peptides and ProteinsJanus Kinase 1Janus Kinase 2Janus Kinase 3Leukocyte Common AntigensProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6PTPN1 protein, humanReceptors, CytokineSH2B3 protein, humanTYK2 Kinase

Identifiers

PMID25057888
PMCPMC4112375
OpenAlexW2086221920

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.