Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Janus kinases in interleukin-2-mediated signaling: JAK1 and JAK3 are differentially regulated by tyrosine phosphorylation.

Current biology : CB | 1997

Cytokines mediate a variety of effector cell functions, including cellular proliferation, differentiation, and modulation of the immune response. Many cytokines activate receptor-associated Janus kinases (JAKs) that promote tyrosine phosphorylation of signal transducers and activators of transcription (STAT) factors. Although JAK activation has been correlated with phosphorylation, the role of this tyrosine phosphorylation in the regulation of JAK1 and JAK3 remains unclear. Furthermore, the relative roles of JAK1 and JAK3 in the activation of STAT5 by interleukin-2 (IL-2) remain poorly understood.

Pubmed ID: 9382798 RIS Download

Research resources used in this publication

None found

Additional research tools detected in this publication

Antibodies used in this publication

None found

Associated grants

  • Agency: NIAID NIH HHS, United States
    Id: AI-36452
  • Agency: NIGMS NIH HHS, United States
    Id: GM-54351

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

This is a list of tools and resources that we have found mentioned in this publication.


New England Biolabs (tool)

RRID:SCR_013517

An Antibody supplier

View all literature mentions