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Titlebook: Cancer Genomics and Proteomics; Methods and Protocol Narendra Wajapeyee Book 2014Latest edition Springer Science+Business Media New York 20

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https://doi.org/10.1007/978-3-642-51175-2en coordinating homologous recombination events. Here, we describe the use of TFOs such as peptide nucleic acids for targeted genome modification. We discuss this method and its applications and describe protocols for TFO design, delivery, and evaluation of activity in vitro and in vivo.
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https://doi.org/10.1007/978-3-642-51175-2eir secondary structure when isolated from the host protein, stapled peptides incorporate an all-hydrocarbon “staple” that reinforces their natural alpha-helical structure. Thus, stapled peptides retain their functional ability to bind their native protein targets and serve multiple experimental use
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Marcel Mechali,Anne-Marie de Recondosponse to therapy, or to serve as therapeutic targets (Chapman et al., Ann Oncol 18(5):868–873, 2007; Soussi et al., Cancer Res 60:1777–1788, 2000; Anderson and LaBaer, J Proteome Res 4:1123–1133, 2005; Levenson, Biochim Biophy Acta 1770:847–856, 2007). In cancer endogenous levels of protein express
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https://doi.org/10.1007/978-3-319-70211-7ransgenic mouse models, coupled with mass spectrometry proteomics, have served as valuable platform for elucidating the in vivo function of individual genes and proteins. Here we discuss the methods we have recently employed to characterize protein–protein interactions and posttranslational modifica
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https://doi.org/10.1007/978-3-319-70211-7, soluble in the cytosol or associated to cellular membranes. Importantly, their membrane-inserted form is the main responsible for their apoptotic function. Unfortunately, there are only a limited number of methods available to study the membrane activity of these proteins. Here, we present a metho
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New Approaches in Intelligent Controlification arise when proteins are of low abundance or are unstable resulting in low yields or poor in vitro activity. In this protocol we describe a method to purify active, recombinant human proteins fused to a tandem MBP tag after expression in human 293T cells.
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