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  • Book
    edited by Sandra E. Nicholson and Nicos A. Nicola.
    Contents:
    Analysis of Janus tyrosine kinase phosphorylation and activation / Jeremy A. Ross, Georgialina Rodriguez, and Robert A. Kirken
    Co-immunoprecipitation protocol to investigate cytokine receptor-associated proteins, e.g., Janus kinases or other associated signaling proteins / Claude Haan and Serge Haan
    In vitro JAK kinase activity and inhibition assays / Jeffrey J. Babon and James M. Murphy
    Quantitative analysis of JAK binding using isothermal titration calorimetry and surface plasmon resonance / Jeffrey J. Babon
    Determination of protein turnover rates in the JAK/STAT pathway using a radioactive pulse-chase approach / Anna Dittrich, Elmar Siewert, and Fred Schaper
    Designing RNAi screens to identify JAK/STAT pathway components / Katherine H. Fisher, Stephen Brown, and Martin P. Zeidler
    The use of JAK-specific inhibitors as chemical biology tools / Christopher J. Burns, David Segal, and Andrew F. Wilks
    Methods for detecting mutations in the human JAK2 gene / Anthony J. Bench, E. Joanna Baxter, and Anthony R. Green
    Detection of activated STAT proteins / Jean-Patrick Parisien and Curt M. Horvath
    Detection of activated STAT species using electrophoretic mobility shift assay (EMSA) and potential pitfalls arising from the use of detergents / Serge Haan and Claude Haan
    Flow cytometric analysis of STAT phosphorylation / Jane Murphy and Gabrielle L. Goldberg
    Acetylation of endogenous STAT proteins / Torsten Ginter, Thorsten Heinzel, and Oliver H. Krämer
    Detection and cellular localization of phospho-STAT2 in the central nervous system by immunohistochemical staining / Reza Khorooshi and Trevor Owens
    Nuclear trafficking of STAT proteins visualized by live cell imaging / Velasco Cimica and Nancy C. Reich
    Characterization of STAT self-association by analytical ultracentrifugation / Nikola Wenta and Uwe Vinkemeier
    Constitutively active STAT5 constructs / Lynn M. Heltemes-Harris and Michael A. Farrar
    Analysis of suppressor of cytokine signalling (SOCS) gene expression by real-time quantitative PCR / Tatiana B. Kolesnik and Sandra E. Nicholson
    Detection of endogenous SOCS1 and SOCS3 proteins by immunoprecipitation and western blot analysis / Jian-Guo Zhang and Sandra E. Nicholson
    In vitro ubiquitination and cytokine signaling components / Jeffrey J. Babon, Artem Laktyushin, and Nadia J. Kershaw
    Production and crystallization of recombinant JAK proteins / Isabelle S. Lucet and Rebecca Bamert
    Bacterial expression, purification, and crystallization of tyrosine phosphorylated STAT proteins / Florence Baudin and Christoph W. Müller.
    Digital Access Springer 2013
  • Book
    Contents:

    v. 1. Organization, method, and tables.
    Print 1981-
  • Article
    Bacon WL, Leclercq B, Blum JC.
    Comp Biochem Physiol B. 1978;59(3):203-6.
    1. Ten-week old broiler females were force-fed (FF) for 3 days or 3 weeks. 2. Control livers were lighter in weight and contained less total lipid, neutral lipid and phospholipid than either FF group, which did not differ. 3. Radioactivity incorporated into liver neutral lipid fractions from 1-[14C]acetate injection was greater in birds FF 3 weeks than controls. Those FF 3 days were intermediate. In all groups, the triglyceride fraction contained 90-94% of isolated radioactivity, the cholesterol fraction 4-8% and the cholesterol ester fraction 1-2%. 4. Plasma lipids were elevated in the birds FF for 3 weeks, but not in those FF 3 days. After injection of 1-[14C]acetate, plasma lipid specific radioactivities were not different between the 3 groups at 20 and 60 min post injection, but were greater in the controls at 120 min.
    Digital Access Access Options