Search our Database of Scientific Publications and Authors

I’m looking for a

    4 results match your criteria Cancer Genomics & Proteomics[Journal]

    1 OF 1

    Different interactomes for p70-S6K1 and p54-S6K2 revealed by proteomic analysis.
    Proteomics 2016 Oct 12;16(20):2650-2666. Epub 2016 Sep 12.
    Laboratory of Metabolic Disorders, School of Applied Sciences, University of Campinas, Limeira, São Paulo, Brazil.
    S6Ks are major effectors of the mTOR (mammalian target of rapamycin) pathway, signaling for increased protein synthesis and cell growth in response to insulin, AMP/ATP levels, and amino acids. Deregulation of this pathway has been related to disorders and diseases associated with metabolism, such as obesity, diabetes, and cancer. S6K family is composed of two main members, S6K1 and S6K2, which comprise different isoforms resulted from alternative splicing or alternative start codon use. Read More

    Uncoupling of bait-protein expression from the prey protein environment adds versatility for cell and tissue interaction proteomics and reveals a complex of CARP-1 and the PKA Cbeta1 subunit.
    Proteomics 2010 Aug;10(16):2890-900
    Structural Biochemistry, German Cancer Research Center, Heidelberg, Germany.
    An expression-uncoupled tandem affinity purification assay is introduced which differs from the standard TAP assay by uncoupling the expression of the TAP-bait protein from the target cells. Here, the TAP-tagged bait protein is expressed in Escherichia coli and purified. The two concatenated purification steps of the classical TAP are performed after addition of the purified bait to brain tissue homogenates, cell and nuclear extracts. Read More

    Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification.
    Proteomics 2009 Feb;9(3):535-49
    Institute for Biological Sciences, National Research Council Canada, Ottawa, ON, Canada.
    Exposure of glioblastoma U87MG cells to a cAMP analog leads to a decrease in proliferation, invasion, and angiogenic potential. Here, we apply a label-free MS-based approach to identify formerly N-linked glycopeptides that change in abundance upon cAMP treatment. Over 150 unique glycopeptides in three biological repetitions were quantified, leading to the identification of 14 upregulated proteins and 21 downregulated proteins due to cAMP treatment. Read More

    Triplex protein quantification based on stable isotope labeling by peptide dimethylation applied to cell and tissue lysates.
    Proteomics 2008 Nov;8(22):4624-32
    Biomolecular Mass Spectrometry and Proteomics Group, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Sorbonnelaan, Utrecht, The Netherlands.
    Stable isotope labeling is at present one of the most powerful methods in quantitative proteomics. Stable isotope labeling has been performed at both the protein as well as the peptide level using either metabolic or chemical labeling. Here, we present a straightforward and cost-effective triplex quantification method that is based on stable isotope dimethyl labeling at the peptide level. Read More

    1 OF 1